Delta2D Report: Labels
for Project 'Demonstration'

Project Properties

Author	DECODON	Project Creation Date	Wed Feb 22 20:00:00 CET 2006
Use Internal Standard	no	Pool	C:\data\demopool
Description	Delta2D demonstration project. A time-course experiment with three samples. We thank Falko Hochgr�fe for the gel images
Report created by user "bielz" with Delta2D, Fri Jul 15 11:46:13 CEST 2016. Please let us know if you have any comment or suggestion using our contact form.

Labels

Labels for selected spots on gel image 'control_01'
All Labels on gel image 'control_01'

Table shows label data for the expression profile of selected spots on gel image 'control_01'.
Total number of selected spots shown in this report: 9.

control_01	control																							Fused Images
	control_01																							Fused Image
Spot	Label name(s)	Pi/MW Estimation		GenoList			Uniprot																	Label name(s)	Pi/MW Estimation		GenoList
ID	Name	Pi	MW	Gene Size (bp)	Protein Size (aa)	Function	Accession	Amino Acids	Function	Gene name	Gene Ontology	Isoelectric Point	Keywords	Molecular Weight	NCBI Taxonomy	Organism	Original label name	Protein name	Query text	References	Sequence	Title	Uniprot entry	Name	Pi	MW	Gene Size (bp)	Protein Size (aa)	Function
Sorry, but iframe obviously are not supported by your browser.	(no label)	N.A.	N.A.																					(no label)	N.A.	N.A.
Sorry, but iframe obviously are not supported by your browser.	(no label)	N.A.	N.A.																					(no label)	N.A.	N.A.
	EF-Ts	N.A.	N.A.	0	0		P80700	293	Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome (By similarity).	tsf	C:cytoplasm [GO:0005737] F:translation elongation factor activity [GO:0003746]	4.9005	Complete proteome Cytoplasm Direct protein sequencing Elongation factor Phosphoprotein Protein biosynthesis Reference proteome	32353.77	224308	Bacillus subtilis (strain 168)	EF-Ts	Elongation factor Ts	EF-Ts	3 references	MAITAQQVKELREKTGAGMMDCKKALTETDGDMDKAIDLLREKGIAKAAKKADRIAAEGS TLIKTDGNKGVILEVNSETDFVAKNEGFKELLNTLADHLLANTPADVEEAMGQKMENGST VEEYITSAVAKIGEKITLRRFTVLTKDDSSAFGAYLHMGGRIGVLTVLNGTTDEETAKDI AMHVAAVNPRYISRDQVSEEETNHERQILTQQALQEGKPENIVAKMVEGRLNKFFEEICL LDQAFVKNPDEKVKQVIAAKNATVQTFVRYEVGEGIEKRQENFAEEVMNQVKK	EFTS_BACSU	P80700	EF-Ts	N.A.	N.A.	0	0
Sorry, but iframe obviously are not supported by your browser.	(no label)	N.A.	N.A.																					(no label)	N.A.	N.A.
Sorry, but iframe obviously are not supported by your browser.	(no label)	N.A.	N.A.																					(no label)	N.A.	N.A.
Sorry, but iframe obviously are not supported by your browser.	(no label)	N.A.	N.A.																					(no label)	N.A.	N.A.
	EF-G	N.A.	N.A.	0	0		P80868	692	Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (By similarity).	fusA	C:cytoplasm [GO:0005737] C:intracellular [GO:0005622] F:GTP binding [GO:0005525] F:GTPase activity [GO:0003924] F:translation elongation factor activity [GO:0003746]	4.5136	Complete proteome Cytoplasm Direct protein sequencing Elongation factor GTP-binding Nucleotide-binding Phosphoprotein Protein biosynthesis Reference proteome	76616.6	224308	Bacillus subtilis (strain 168)	EF-G	Elongation factor G	EF-G	6 references	MAREFSLEKTRNIGIMAHIDAGKTTTTERILFYTGRIHKIGETHEGASQMDWMEQEQERG ITITSAATTAQWKGYRVNIIDTPGHVDFTVEVERSLRVLDGAVAVLDAQSGVEPQTETVW RQATTYGVPRIVFVNKMDKIGADFLYSVGTLRDRLQANAHAIQLPIGAEDNFEGIIDLVE NVAYFYEDDLGTRSDAKEIPEEYKEQAEELRNSLIEAVCELDEELMDKYLEGEEITIDEL KAGIRKGTLNVEFYPVLVGSAFKNKGVQLVLDAVLDYLPAPTDVAAIKGTRPDTNEEIER HSSDEEPFSALAFKVMTDPYVGKLTFFRVYSGTLDSGSYVKNSTKGKRERVGRILQMHAN SREEISTVYAGDIAAAVGLKDTTTGDTLCDEKDLVILESMEFPEPVIDVAIEPKSKADQD KMGIALAKLAEEDPTFRTQTNPETGQTIISGMGELHLDIIVDRMKREFKVEANVGAPQVA YRETFRTGAKVEGKFVRQSGGRGQFGHVWIEFEPNEEGAGFEFENAIVGGVVPREYIPAV QAGLEDALENGVLAGFPLIDIKAKLFDGSYHDVDSNEMAFKVAASMALKNAVSKCNPVLL EPIMKVEVVIPEEYMGDIMGDITSRRGRVEGMEARGNAQVVRAMVPLAEMFGYATALRSN TQGRGTFTMHMDHYEEVPKSVAEEIIKKNKGE	EFG_BACSU	P80868	EF-G	N.A.	N.A.	0	0
Sorry, but iframe obviously are not supported by your browser.	(no label)	N.A.	N.A.																					(no label)	N.A.	N.A.
Sorry, but iframe obviously are not supported by your browser.	(no label)	N.A.	N.A.																					(no label)	N.A.	N.A.

Table shows label data for all labels on gel image 'control_01'. If a label is annotating a detected spot, this spot is shown as well.
Total number of labels shown in this report: 29.

Label			Spot	Pi/MW Estimation		GenoList			Uniprot
Name	X	Y	ID	Pi	MW	Gene Size (bp)	Protein Size (aa)	Function	Accession	Amino Acids	Function	Gene name	Gene Ontology	Isoelectric Point	Keywords	Molecular Weight	NCBI Taxonomy	Organism	Original label name	Protein name	Query text	References	Sequence	Title	Uniprot entry
AhpC	876	689	Sorry, but iframe obviously are not supported by your browser.	N.A.	N.A.	561	187		P80239	187	Directly reduces organic hydroperoxides in its reduced dithiol form.	ahpC	F:peroxidase activity [GO:0004601] F:peroxiredoxin activity [GO:0051920] P:response to oxidative stress [GO:0006979]	4.2224	Antioxidant Complete proteome Direct protein sequencing Disulfide bond Oxidoreductase Peroxidase Redox-active center Reference proteome Stress response	20627.12	224308	Bacillus subtilis (strain 168)	AhpC	Alkyl hydroperoxide reductase subunit C	AhpC	4 references	MSLIGKEVLPFEAKAFKNGEFIDVTNEDLKGQWSVFCFYPADFSFVCPTELEDLQEQYAA LKELGVEVYSVSTDTHFVHKGWHDSSEKISKITYAMIGDPSQTISRNFDVLDEETGLADR GTFIIDPDGVIQTVEINAGGIGRDASNLVNKVKAAQYVRQNPGEVCPAKWEEGGETLTPS LDLVGKI	AHPC_BACSU	P80239
AhpF	711	271	Sorry, but iframe obviously are not supported by your browser.	N.A.	N.A.	1527	509		P42974	509	Transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).	ahpF	C:plasma membrane [GO:0005886] F:alkyl hydroperoxide reductase activity [GO:0008785] F:electron carrier activity [GO:0009055] F:flavin adenine dinucleotide binding [GO:0050660] F:NAD binding [GO:0051287] F:NADH dehydrogenase activity [GO:0003954] F:protein disulfide oxidoreductase activity [GO:0015035] P:cell redox homeostasis [GO:0045454] P:response to reactive oxygen species [GO:0000302]	4.6273	Cell membrane Complete proteome Direct protein sequencing Disulfide bond Electron transport FAD Flavoprotein Membrane NAD Oxidoreductase Redox-active center Reference proteome Transport Ubiquinone	54874.4	224308	Bacillus subtilis (strain 168)	AhpF	NADH dehydrogenase	AhpF	4 references	MVLDANIKAQLNQYMQLIENDIVLKVSAGEDDTSKDMLALVDELASMSSKISVEKAELNR TPSFSVNRVGEDTGVTFAGIPLGHEFTSLVLALLQVSGRPPKVDQKVIDQVKKISGEYHF ESYISLTCHNCPDVVQALNMMSVLNPNITHTMIDGAAYKAEVESKNIMAVPTVYLNGESF GSGRMTLEEILAKMGSGTDASEFADKEPFDVLVVGGGPAGASAAIYTARKGIRTGVVAER FGGQVLDTMSIENFISVKATEGPKLAASLEEHVKEYDIDVMNLQRAKRLEKKDLFELELE NGAVLKSKTVILSTGARWRNVNVPGEQEFKNKGVAYCPHCDGPLFEGKDVAVIGGGNSGI EAAIDLAGIVNHVTVLEFAPELKADEVLQKRLYSLPNVTVVKNAQTKEITGDQSVNGITY VDRETGEEKHVELQGVFVQIGLVPNTEWLEGTVERNRMGEIIVDKHGATSVPGLFAAGDC TDSAYNQIIISMGSGATAALGAFDYLIRN	DHNA_BACSU	P42974
AroA	450	398	Sorry, but iframe obviously are not supported by your browser.	N.A.	N.A.	1074	358		P39912	358		aroA	F:3-deoxy-7-phosphoheptulonate synthase activity [GO:0003849] F:aldehyde-lyase activity [GO:0016832] F:chorismate mutase activity [GO:0004106] P:aromatic amino acid family biosynthetic process [GO:0009073] P:chorismate biosynthetic process [GO:0009423]	5.3532	Amino-acid biosynthesis Aromatic amino acid biosynthesis Complete proteome Isomerase Multifunctional enzyme Phosphoprotein Reference proteome Transferase	39539.46	224308	Bacillus subtilis (strain 168)	AroA	Protein AroA(G)	AroA	4 references	MSNTELELLRQKADELNLQILKLINERGNVVKEIGKAKEAQGVNRFDPVRERTMLNNIIE NNDGPFENSTIQHIFKEIFKAGLELQEEDHSKALLVSRKKKPEDTIVDIKGEKIGDGQQR FIVGPCAVESYEQVAEVAAAAKKQGIKILRGGAFKPRTSPYDFQGLGVEGLQILKRVADE FDLAVISEIVTPAHIEEALDYIDVIQIGARNMQNFELLKAAGAVKKPVLLKRGLAATISE FINAAEYIMSQGNDQIILCERGIRTYETATRNTLDISAVPILKQETHLPVFVDVTHSTGR RDLLLPTAKAALAIGADGVMAEVHPDPSVALSDSAQQMAIPEFEKWLNELKPMVKVNA	AROG_BACSU	P39912
CysK	384	535	Sorry, but iframe obviously are not supported by your browser.	N.A.	N.A.	924	308		P37887	308	Catalyzes the conversion of O-acetylserine to cysteine. Also acts as a sensor of cysteine availability in the signal transduction pathway modulating CymR activity. When cysteine is present, the pool of O-acetylserine (OAS) is low, which leads to the formation of a CymR-CysK complex and transcriptional repression of the CymR regulon occurs. In the absence of cysteine, the OAS pool is high and the CymR-CysK complex is mostly dissociated, leading to a faster dissociation of CymR from its DNA targets and the lifting of CymR-dependent repression.	cysK	C:cytoplasm [GO:0005737] F:cysteine synthase activity [GO:0004124] F:L-cysteine desulfhydrase activity [GO:0080146] F:pyridoxal phosphate binding [GO:0030170] F:transferase activity [GO:0016740] P:cysteine biosynthetic process from serine [GO:0006535]	5.5093	Amino-acid biosynthesis Complete proteome Cysteine biosynthesis Direct protein sequencing Pyridoxal phosphate Reference proteome Transferase	32819.6	224308	Bacillus subtilis (strain 168)	CysK	Cysteine synthase	CysK	7 references	MVRVANSITELIGNTPIVKLNRLADENSADVYLKLEYMNPGSSVKDRIGLAMIEAAEKEG KLKAGNTIIEPTSGNTGIGLAMVAAAKGLKAILVMPDTMSMERRNLLRAYGAELVLTPGA EGMKGAIKKAEELAEKHGYFVPQQFNNPSNPEIHRQTTGKEIVEQFGDDQLDAFVAGIGT GGTITGAGEVLKEAYPSIKIYAVEPSDSPVLSGGKPGPHKIQGIGAGFVPDILNTEVYDE IFPVKNEEAFEYARRAAREEGILGGISSGAAIYAALQVAKKLGKGKKVLAIIPSNGERYL STPLYQFD	CYSK_BACSU	P37887
DnaK	751	178	Sorry, but iframe obviously are not supported by your browser.	N.A.	N.A.	1833	611		P17820	611	Acts as a chaperone.	dnaK	F:ATP binding [GO:0005524] P:protein folding [GO:0006457]	4.4949	3D-structure ATP-binding Chaperone Complete proteome Direct protein sequencing Nucleotide-binding Phosphoprotein Reference proteome Stress response	66002.12	224308	Bacillus subtilis (strain 168)	DnaK	Chaperone protein DnaK	DnaK	7 references	MSKVIGIDLGTTNSCVAVLEGGEPKVIANAEGNRTTPSVVAFKNGERQVGEVAKRQSITN PNTIMSIKRHMGTDYKVEIEGKDYTPQEVSAIILQHLKSYAESYLGETVSKAVITVPAYF NDAERQATKDAGKIAGLEVERIINEPTAAALAYGLDKTDEDQTILVYDLGGGTFDVSILE LGDGVFEVRSTAGDNRLGGDDFDQVIIDHLVSEFKKENGIDLSKDKMALQRLKDAAEKAK KDLSGVSSTQISLPFITAGEAGPLHLELTLTRAKFEELSSHLVERTMGPVRQALQDAGLS ASEIDKVILVGGSTRIPAVQEAIKKETGKEAHKGVNPDEVVALGAAIQGGVITGDVKDVV LLDVTPLSLGIETMGGVFTKLIDRNTTIPTSKSQVFSTAADNQTAVDIHVLQGERPMSAD NKTLGRFQLTDIPPAPRGVPQIEVSFDIDKNGIVNVRAKDLGTGKEQNITIKSSSGLSDE EIERMVKEAEENADADAKKKEEIEVRNEADQLVFQTEKTLKDLEGKVDEEQVKKANDAKD ALKAAIEKNEFEEIKAKKDELQTIVQELSMKLYEEAAKAQQAQGGANAEGKADDNVVDAE YEEVNDDQNKK	DNAK_BACSU	P17820
Dps	778	804	Sorry, but iframe obviously are not supported by your browser.	N.A.	N.A.	435	145		P80879	145		dps	C:cell [GO:0005623] F:ferric iron binding [GO:0008199] F:oxidoreductase activity, oxidizing metal ions [GO:0016722] P:cellular iron ion homeostasis [GO:0006879] P:response to stress [GO:0006950]	4.368	Complete proteome Direct protein sequencing Reference proteome Stress response	16593.73	224308	Bacillus subtilis (strain 168)	Dps	General stress protein 20U	Dps	3 references	MSEQLIQAVNKQVANWTVMYVKLHNYHWYVKGKDFFTLHEKFEELYNETATYIDDLAERL LALNGKPIATMKESLETASVKEAAGNETAEQMVQSVYDDFTVIAEELKNGMDLADEVGDE TTGDMLLAIHQNIEKHNWMLKAYLG	G20U_BACSU	P80879
Dps	815	783	Sorry, but iframe obviously are not supported by your browser.	N.A.	N.A.	435	145		P80879	145		dps	C:cell [GO:0005623] F:ferric iron binding [GO:0008199] F:oxidoreductase activity, oxidizing metal ions [GO:0016722] P:cellular iron ion homeostasis [GO:0006879] P:response to stress [GO:0006950]	4.368	Complete proteome Direct protein sequencing Reference proteome Stress response	16593.73	224308	Bacillus subtilis (strain 168)	Dps	General stress protein 20U	Dps	3 references	MSEQLIQAVNKQVANWTVMYVKLHNYHWYVKGKDFFTLHEKFEELYNETATYIDDLAERL LALNGKPIATMKESLETASVKEAAGNETAEQMVQSVYDDFTVIAEELKNGMDLADEVGDE TTGDMLLAIHQNIEKHNWMLKAYLG	G20U_BACSU	P80879
EF-G	708	131	Sorry, but iframe obviously are not supported by your browser.	N.A.	N.A.	0	0		P80868	692	Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (By similarity).	fusA	C:cytoplasm [GO:0005737] C:intracellular [GO:0005622] F:GTP binding [GO:0005525] F:GTPase activity [GO:0003924] F:translation elongation factor activity [GO:0003746]	4.5136	Complete proteome Cytoplasm Direct protein sequencing Elongation factor GTP-binding Nucleotide-binding Phosphoprotein Protein biosynthesis Reference proteome	76616.6	224308	Bacillus subtilis (strain 168)	EF-G	Elongation factor G	EF-G	6 references	MAREFSLEKTRNIGIMAHIDAGKTTTTERILFYTGRIHKIGETHEGASQMDWMEQEQERG ITITSAATTAQWKGYRVNIIDTPGHVDFTVEVERSLRVLDGAVAVLDAQSGVEPQTETVW RQATTYGVPRIVFVNKMDKIGADFLYSVGTLRDRLQANAHAIQLPIGAEDNFEGIIDLVE NVAYFYEDDLGTRSDAKEIPEEYKEQAEELRNSLIEAVCELDEELMDKYLEGEEITIDEL KAGIRKGTLNVEFYPVLVGSAFKNKGVQLVLDAVLDYLPAPTDVAAIKGTRPDTNEEIER HSSDEEPFSALAFKVMTDPYVGKLTFFRVYSGTLDSGSYVKNSTKGKRERVGRILQMHAN SREEISTVYAGDIAAAVGLKDTTTGDTLCDEKDLVILESMEFPEPVIDVAIEPKSKADQD KMGIALAKLAEEDPTFRTQTNPETGQTIISGMGELHLDIIVDRMKREFKVEANVGAPQVA YRETFRTGAKVEGKFVRQSGGRGQFGHVWIEFEPNEEGAGFEFENAIVGGVVPREYIPAV QAGLEDALENGVLAGFPLIDIKAKLFDGSYHDVDSNEMAFKVAASMALKNAVSKCNPVLL EPIMKVEVVIPEEYMGDIMGDITSRRGRVEGMEARGNAQVVRAMVPLAEMFGYATALRSN TQGRGTFTMHMDHYEEVPKSVAEEIIKKNKGE	EFG_BACSU	P80868
EF-Ts	589	467	Sorry, but iframe obviously are not supported by your browser.	N.A.	N.A.	0	0		P80700	293	Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome (By similarity).	tsf	C:cytoplasm [GO:0005737] F:translation elongation factor activity [GO:0003746]	4.9005	Complete proteome Cytoplasm Direct protein sequencing Elongation factor Phosphoprotein Protein biosynthesis Reference proteome	32353.77	224308	Bacillus subtilis (strain 168)	EF-Ts	Elongation factor Ts	EF-Ts	3 references	MAITAQQVKELREKTGAGMMDCKKALTETDGDMDKAIDLLREKGIAKAAKKADRIAAEGS TLIKTDGNKGVILEVNSETDFVAKNEGFKELLNTLADHLLANTPADVEEAMGQKMENGST VEEYITSAVAKIGEKITLRRFTVLTKDDSSAFGAYLHMGGRIGVLTVLNGTTDEETAKDI AMHVAAVNPRYISRDQVSEEETNHERQILTQQALQEGKPENIVAKMVEGRLNKFFEEICL LDQAFVKNPDEKVKQVIAAKNATVQTFVRYEVGEGIEKRQENFAEEVMNQVKK	EFTS_BACSU	P80700
EF-Tu	680	317	Sorry, but iframe obviously are not supported by your browser.	N.A.	N.A.	0	0		P33166	396	This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.	tuf	C:cytoplasm [GO:0005737] C:intracellular [GO:0005622] F:GTP binding [GO:0005525] F:GTPase activity [GO:0003924] F:translation elongation factor activity [GO:0003746] P:translational elongation [GO:0006414]	4.6467	Complete proteome Cytoplasm Elongation factor GTP-binding Nucleotide-binding Protein biosynthesis Reference proteome	43593.27	224308	Bacillus subtilis (strain 168)	EF-Tu	Elongation factor Tu	EF-Tu	3 references	MAKEKFDRSKSHANIGTIGHVDHGKTTLTAAITTVLHKKSGKGTAMAYDQIDGAPEERER GITISTAHVEYETETRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREH ILLSKNVGVPYIVVFLNKCDMVDDEELLELVEMEVRDLLSEYDFPGDDVPVVKGSALKAL EGDAEWEAKIFELMDAVDEYIPTPERDTEKPFMMPVEDVFSITGRGTVATGRVERGQVKV GDEVEIIGLQEENKKTTVTGVEMFRKLLDYAEAGDNIGALLRGVSREEIQRGQVLAKPGT ITPHSKFKAEVYVLSKEEGGRHTPFFSNYRPQFYFRTTDVTGIIHLPEGVEMVMPGDNTE MNVELISTIAIEEGTRFSIREGGRTVGSGVVSTITE	EFTU_BACSU	P33166
Eno	772	340	Sorry, but iframe obviously are not supported by your browser.	N.A.	N.A.	1290	430		P37869	430	Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.	eno	C:cell surface [GO:0009986] C:extracellular region [GO:0005576] C:phosphopyruvate hydratase complex [GO:0000015] F:magnesium ion binding [GO:0000287] F:phosphopyruvate hydratase activity [GO:0004634] P:glycolytic process [GO:0006096] P:sporulation resulting in formation of a cellular spore [GO:0030435]	4.4037	3D-structure Complete proteome Cytoplasm Direct protein sequencing Glycolysis Lyase Magnesium Metal-binding Phosphoprotein Reference proteome Secreted Sporulation	46581.39	224308	Bacillus subtilis (strain 168)	Eno	Enolase	Eno	9 references	MPYIVDVYAREVLDSRGNPTVEVEVYTETGAFGRALVPSGASTGEYEAVELRDGDKDRYL GKGVLTAVNNVNEIIAPELLGFDVTEQNAIDQLLIELDGTENKGKLGANAILGVSMACAR AAADFLQIPLYQYLGGFNSKTLPVPMMNIVNGGEHADNNVDIQEFMIMPVGAPNFREALR MGAQIFHSLKSVLSAKGLNTAVGDEGGFAPNLGSNEEALQTIVEAIEKAGFKPGEEVKLA MDAASSEFYNKEDGKYHLSGEGVVKTSAEMVDWYEELVSKYPIISIEDGLDENDWEGHKL LTERLGKKVQLVGDDLFVTNTKKLSEGIKNGVGNSILIKVNQIGTLTETFDAIEMAKRAG YTAVISHRSGETEDSTIADIAVATNAGQIKTGAPSRTDRVAKYNQLLRIEDQLAETAQYH GINSFYNLNK	ENO_BACSU	P37869
GapA	544	371	Sorry, but iframe obviously are not supported by your browser.	N.A.	N.A.	1005	335	catabolic enzyme	E0U2V1	340		cggR	F:carbohydrate binding [GO:0030246]	5.8363	Complete proteome Reference proteome	37410.17	655816	Bacillus subtilis subsp. spizizenii (strain ATCC 23059 / NRRL B-14472 / W23)	GapA		GapA	2 references	MNQLIQAQKKLLPDLLLVMQKRFEILQYIRLTEPIGRRSLSASLGISERVLRGEVQFLKE QNLVDIKTNGMTLTEEGYELLSVLEDTMKDVLGLTLLEKTLKERLNLKDAIIVSGDSDQS PWVKKEMGRAAVACMKKRFSGKNIVAVTGGTTIEAVAEMMTPDSKNRELLFVPARGGLGE DVKNQANTICAHMAEKASGTYRLLFVPGQLSQGAYSSIIEEPSVKEVLNTIKSASMLVHG IGEAKTMAQRRNTPLEDLKKIDDNDAVTEAFGYYFNVDGEVVHKVHSVGMQLDDIDAIPD IIAVAGGSSKAEAIEAYFKKPRNTVLVTDEGAAKKLLRDE	E0U2V1_BACPZ	E0U2V1
GlnA	629	297	Sorry, but iframe obviously are not supported by your browser.	N.A.	N.A.	1332	444		P94459	3603	This protein is a multifunctional enzyme, able to activate and polymerize the amino acids Pro, Gln and Tyr as part of the biosynthesis of the lipopeptide antibiotic plipastatin. The Tyr residue is further epimerized to the D-isomer form. The activation sites for these amino acids consist of individual domains.	ppsD	F:phosphopantetheine binding [GO:0031177] F:transferase activity [GO:0016740] P:antibiotic biosynthetic process [GO:0017000]	5.4998	Antibiotic biosynthesis Complete proteome Multifunctional enzyme Phosphopantetheine Phosphoprotein Reference proteome Repeat Transferase	406812.3	224308	Bacillus subtilis (strain 168)	GlnA	Plipastatin synthase subunit D	GlnA	5 references	MTKANSIQDIYPLSYMQEGMLFHSLLQKDSQAYVEQASFTIEGKVNPQFFQNSINALVER HDIFRTIFISQNVSSPQQVVLRERNVIVLEEDITHLNEAEQSQFIEQWKEKDRDRGFHLQ KDVLMRIALIQTGESQYSCIWTFHHIMMDGWCLSIVLKEFLHIYASYVNASPITLEPVQP YGKYIKWLMEQDKEQAVSYWDHYLSGHEQQTVLPKQKKTKGKSRQEHVTFSFSKEESSRL SELAAREEVTLSTIFHTIWGILLQKYNNNDDAVFGSVISGRPAEIEGIEHMVGLFINTMP VRVQGAKTPFLQLIKDMQKDRLAAEAYSYHPLYEIQSRSAVKQGLIDHILVFENYPVQQE IQMLNKQEHASDLFQIHNFTVADETNYSFYLMVAPGEEIHIKMNYDAEQHDRSFVLSVKE HLLNAVSQILNNPNLPPEEIDITTDTEKRQLIGEITDQTPVYETIHAMFEKQAEKTPDAH AVIDQACSLTYRELNKAANRLARHLRMKGVVRQEPVAIMMERSAAFITGVLGILKAGGAI VPVDPHYPADRIRYILHDCGCSHVVSQAHLPSSLEDNYIITHPEDIESKVDGSNIKSVNN ADDLLYMIYTSGTTGKPKGVQFEHRNMANLLKFEYTHSGIDFEADVLQFATPSFDVCYQE IFSALLKGGTLHIVPEAIKRDVPQLFAFINKHQTNIVFLPTAFIKMIFSERELANSFPDG VKHLIAAGEQLMISDLFQDVLRKRGIHLHNHYGPSETHVVSTYTIHPGDPIPELPPIGKP IGCTDLYILNHQKQLQPCGVPGELYISGASVARGYVNHDKLTSDKFSSDPFKPDVIMYRT GDLARRLEDGNIEYIGRADNQVKIRGYRIEPQEIEVTLMNHPDISEAAILIWQDQNGEHE LCAYYCSVQKLNTIDLRSYMASELPEYMIPAKWIWVDSIPLTPNGKVDRAALPEPDASIS GNPYTAPRNLLEAKLSQLFEDVLKNGHIGIQDNFFDNGGHSLKATVLMSRIAKEFHVQVS LKDIFAHPTVEGLALIIREAEQNLYAAIEPAEKRDTYPVSSAQKRIYVLQQLDEGVAYNM PAVLELEGALDVAKLSAVCKELISRHEPLRTSFVSGADDEPVQRIHTEVPFTLSKETTIE GFVRPFDLSQAPLFRAGLIEVSNEKHVLLVDMHHIISDGVSVQLLIREFTDLYANRQLKP LRIQYKDYAVWQQKFKKGDSYQKQETYWQQQFSGDLPILELPTDKRRPAERQFIGGKVTF QLDKEITARIKRLAHKNRSTLYMTLLALYSAFLSRLSGQDDIVIGSPIAGRPHADLEAVL GMFVNTLALRTRPAGNKTFEEFLKEVRQTALEAYEHQDYPFEELVDKLGVQREMSRNPLF DTTLVLQNMEQQKLKMNDVQLQWNDLEHPISKFDISLYVTEHDSELFCQFEYSTALFEKE TIQRWASLFTTLVEHTAASPETELDNIPILTKEEERDFIESCHLFEETGYSMNQTLHYAL EQQAEKTPDQAAVIFEDGVMTYKELNEQANRIAWELIGRGVKPETTVAIIGKRSPEMLLG IYGILKAGGAYLPIDPDYPEERISFLLEDSGTNILLLQSAGLHVPEFTGEIVYLNQTNSG LAHRLSNPNVDVLPQSLAYVIYTSGSTGMPKGVEIEHRSAVNFLNSLQSRYQLKHSDMIM HKTSYSFDASIWELFWWPYAGASVYLLPQGGEKEPEVIAKAIEEQKITAMHFVPSMLHAF LEHIKYRSVPIKTNRLKRVFSGGEQLGTHLVSRFYELLPNVSITNSYGPTEATVEAAFFD CPPHEKLERIPIGKPVHHVRLYLLNQNQRMLPVGCIGELYIAGAGVARGYLNRPALTEER FLEDPFYPGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVR EAAVTVRTDSGEPELCAYVEGLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDR NALPAPGGAADAETYTAPRNVTEMKLSQLWEDVLKNGPVGIHDNFFDRGGHSLKATALVS RITKEFDVQVPLKDVFAHPTVEGLATVIREGTDSPYEAIKPAEKQETYPVSSAQKRIYVL QQLEDGGTGYNMPAVLELEGKLNPERMDRAFQELIKRHESLRTSFEQDEGGDPVQRIHDE VPFTLQTTVLGARTEQEAAAAFIKPFDLSQAPLFRAQIVKVSDERHLLLVDMHHIISDGV SVNILIQEFGELYNNRKLPALRIQYKDYAVWQEGFKTGDAYKMQEAYWLKQLEGELPVLD LPADHARPPVRSFAGDKVSFTLEPEVASGLHKLARENGSTLYMVLLAAYTAFLSRLSGQE DIIVGSPIAGRPHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETALEAFEHQNYP FEELVDKLELTRDMSRNPVFDAMLVVQNNDYEPLHLHDLQMKPAQVSHLVSKFDLTLQAS EGDGNIHFLFEYSTALFEKTTIERWASHLTNVLSIIGKNPKVTLNHIDILTQEERHQLLN EFNTGQANQYGVQTISQLFEQQAARTPKASALVSGDKTLTYQELDEWSNGIARALRSRGV KPDTPVGIMMHRSFSMIASILGVWKAGGCYVPIDPEYPKERKRYILSDSGTKLLMTINEA DLGVLADFEGEILTIESVEEDDKSPLPQMSSAHHLAYIIYTSGTTGRPKGVMVEHKGIAN TLQWRRNAYAFNETDTILQLFSFSFDGFITSMFTPLLSGAKAVLLHEEEAKDILAIKHQL SRQRITHMIIVPVLYRALLDVVQPEDVKTLRVVTLAGEAADRELIARSLAICPHTELANE YGPTENSVATTVMRHMEKQAYVSIGQPIDGTQVLILNSNHQLQPIGVAGELCIAGTGLAR GYVNLPELTERAFTQNPFKPEARMYRTGDAARWMADGTLEYLGRIDDQVKIRGYRVETKE IESVIRCIKGVKDAAVVAHVTASGQTELSAYVVTKPGLSTNAVRSELQNKLPVFMHPAFI EKLDSLPLSPNGKLDRGALPKPVYNHEGERPFLPPSSKMEQILADIWKEVLGAEKIGTAD SFFELGGDSIKALQVSARLHRIGKQMAVKDLFSHPTIQELAAYIRDSDTSSSQAAVEGDV QWSPVQKWFLSQDIKEKHHFNQSVMLHRSTSVQEDALRKTLKAITCHHDALRMVFTQNEQ GKWDQYNRPLSHSDDALYGLQMIDLSAPDGTDGNRPYEPLIKRHVLDIQQKMDLKNGPLL QAGLFHTIDGDFLFLSAHHLVVDGISWRVLLEDLALGYRQAAGGEDIKLPPKTSSFKAYA KKLSDYAESQQLMKQLKYWREAEEYQTEALPFDQIDGTRAHEGQRSTISFTLNDKETAAL LKDANSAYNTDTQDMLLASVILALRHWTNQSAFKLSLEGHGREDVLKGIDVSRTIGWFTA IYPLLIKLNADLPDSEESMVHVLKTTKDTLRRVPDKGFGYGVIKYLTPPGKKDINFTGAP EISFNYLGQFESGRTAEVPEEDAFSFSPLGAGGDISTTWNREQSLDISAIAAEGKLTVNM TYDNARFQRKTIEQLSETCRQFLLQLIEHCQNKSETEKTISDFDDQELTEDALQEIADML SFH	PPSD_BACSU	P94459
GroEL	748	213	Sorry, but iframe obviously are not supported by your browser.	N.A.	N.A.	1632	544		P28598	544	Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.	groL	C:cytoplasm [GO:0005737] F:ATP binding [GO:0005524] P:protein refolding [GO:0042026]	4.4284	ATP-binding Chaperone Complete proteome Cytoplasm Direct protein sequencing Nucleotide-binding Reference proteome Stress response	57424.58	224308	Bacillus subtilis (strain 168)	GroEL	60 kDa chaperonin	GroEL	8 references	MAKEIKFSEEARRAMLRGVDALADAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIE LEDAFENMGAKLVAEVASKTNDVAGDGTTTATVLAQAMIREGLKNVTAGANPVGVRKGME QAVAVAIENLKEISKPIEGKESIAQVAAISAADEEVGSLIAEAMERVGNDGVITIEESKG FTTELEVVEGMQFDRGYASPYMVTDSDKMEAVLDNPYILITDKKITNIQEILPVLEQVVQ QGKPLLLIAEDVEGEALATLVVNKLRGTFNAVAVKAPGFGDRRKAMLEDIAVLTGGEVIT EDLGLDLKSTQIAQLGRASKVVVTKENTTIVEGAGETDKISARVTQIRAQVEETTSEFDR EKLQERLAKLAGGVAVIKVGAATETELKERKLRIEDALNSTRAAVEEGIVSGGGTALVNV YNKVAAVEAEGDAQTGINIVLRALEEPIRQIAHNAGLEGSVIVERLKNEEIGVGFNAATG EWVNMIEKGIVDPTKVTRSALQNAASVAAMFLTTEAVVADKPEENGGGAGMPDMGGMGGM GGMM	CH60_BACSU	P28598
GspA	584	513	Sorry, but iframe obviously are not supported by your browser.	N.A.	N.A.	858	286		P25148	286		gspA	F:transferase activity, transferring glycosyl groups [GO:0016757] P:polysaccharide biosynthetic process [GO:0000271]	5.1072	Complete proteome Direct protein sequencing Glycosyltransferase Reference proteome Stress response Transferase	33521.99	224308	Bacillus subtilis (strain 168)	GspA	General stress protein A	GspA	5 references	MRKDEIMHIVSCADDNYARHLGGMFVSLLTNMDQEREVKLYVIDGGIKPDNKKRLEETTL KFGVPIEFLEVDTNMYEHAVESSHITKAAYYRISIPDLIKDESIKRMIYIDCDALVLEDI SKLWDLDIAPYTVAAVEDAGQHERLKEMNVTDTGKYFNSGIMIIDFESWRKQNITEKVIN FINEHPDEDFLVLHDQDALNAILYDQWYELHPRWNAQTYIMLKLKTPSTLLGRKQYNETR ENPAIVHFCGGEKPWNSNTKHPYRDEYFHYMSYTKWNTIGNPAINQ	GSPA_BACSU	P25148
GspA	551	512	Sorry, but iframe obviously are not supported by your browser.	N.A.	N.A.	858	286		P25148	286		gspA	F:transferase activity, transferring glycosyl groups [GO:0016757] P:polysaccharide biosynthetic process [GO:0000271]	5.1072	Complete proteome Direct protein sequencing Glycosyltransferase Reference proteome Stress response Transferase	33521.99	224308	Bacillus subtilis (strain 168)	GspA	General stress protein A	GspA	5 references	MRKDEIMHIVSCADDNYARHLGGMFVSLLTNMDQEREVKLYVIDGGIKPDNKKRLEETTL KFGVPIEFLEVDTNMYEHAVESSHITKAAYYRISIPDLIKDESIKRMIYIDCDALVLEDI SKLWDLDIAPYTVAAVEDAGQHERLKEMNVTDTGKYFNSGIMIIDFESWRKQNITEKVIN FINEHPDEDFLVLHDQDALNAILYDQWYELHPRWNAQTYIMLKLKTPSTLLGRKQYNETR ENPAIVHFCGGEKPWNSNTKHPYRDEYFHYMSYTKWNTIGNPAINQ	GSPA_BACSU	P25148
GtaB	612	514	Sorry, but iframe obviously are not supported by your browser.	N.A.	N.A.	876	292	glucosylation of teichoic acid	Q05852	292	Catalyzes the formation of UDP-glucose from glucose-1-phosphate and UTP. This is an intermediate step in the biosynthesis of diglucosyl-diacylglycerol (Glc2-DAG), i.e. the predominant glycolipid found in B.subtilis membrane, which is also used as a membrane anchor for lipoteichoic acid (LTA). Has a role in the biosynthesis of all phosphate-containing envelope polymers, since UDP-glucose serves as a glucosyl donor not only for the biosynthesis of LTA but also for wall teichoic acids (WTAs). Is required for biofilm formation. This is likely due to another role of UDP-glucose, which might also act as a metabolic signal regulating biofilm formation or may be involved in some unknown biosynthetic pathway essential for biofilm formation, e.g. the synthesis of an exopolysaccharide.	gtaB	F:UTP:glucose-1-phosphate uridylyltransferase activity [GO:0003983] P:enterobacterial common antigen biosynthetic process [GO:0009246] P:UDP-glucose metabolic process [GO:0006011]	4.8217	Carbohydrate metabolism Complete proteome Direct protein sequencing Nucleotidyltransferase Reference proteome Stress response Transferase	33070.03	224308	Bacillus subtilis (strain 168)	GtaB	UTP--glucose-1-phosphate uridylyltransferase	GtaB	6 references	MKKVRKAIIPAAGLGTRFLPATKAMPKEMLPIVDKPTIQYIIEEAVEAGIEDIIIVTGKS KRAIEDHFDYSPELERNLEEKGKTELLEKVKKASNLADIHYIRQKEPKGLGHAVWCARNF IGDEPFAVLLGDDIVQAETPGLRQLMDEYEKTLSSIIGVQQVPEEETHRYGIIDPLTSEG RRYQVKNFVEKPPKGTAPSNLAILGRYVFTPEIFMYLEEQQVGAGGEIQLTDAIQKLNEI QRVFAYDFEGKRYDVGEKLGFITTTLEFAMQDKELRDQLVPFMEGLLNKEEI	GTAB_BACSU	Q05852
Hag	662	420	Sorry, but iframe obviously are not supported by your browser.	N.A.	N.A.	912	304		A0A0K6MGG5	462		BN2127_JRS10_00642		8.5596		50607.65	1423	Bacillus subtilis	Hag		Hag	1 references	MKKKSSKQKRKCPPFYLPMYGINNWCSIRAAALEELEEQEAAPKNKARPKYVSLQNAVMS RIIDNQITKRQQKNKPLSTHTEQIVPSEQAEKKTEENIPVAINKKAESEIPAAIINQVKK IKEALATSGDRQTEKTIIIHPPTPEISKVKKGGRYVHAEGLHSHAEGTASHAEGLLTHAK GSFSHAEGSKTKATGHSSHSEGSETTAGGSYSHAEGKHTIALGEAAHAEGTATIANGFSS HAEGNHTSTAHFAGSHIMGRFGTAEESYSWFIANGTNETDHNIGAKWLAHNGEMYIDGAS YNASGTDFAQMFEAVDNTLIDVGYFVTFSSEEKIRIATSNDSFILGISSATPALIGNSGA LSWQKRYKTDSFGKRQYVRTESQDIQPLLNTEWDPACKYIARKDRTEWLPVGLIGQMLVR DDGTCKTHGYCRPNDKGIATKSESGFFVIKRTGDNQILILFR	A0A0K6MGG5_BACIU	A0A0K6MGG5
Icd	664	358	Sorry, but iframe obviously are not supported by your browser.	N.A.	N.A.	1269	423		P39126	423		icd	F:isocitrate dehydrogenase (NADP+) activity [GO:0004450] F:magnesium ion binding [GO:0000287] F:NAD binding [GO:0051287] P:glyoxylate cycle [GO:0006097] P:tricarboxylic acid cycle [GO:0006099]	4.7444	3D-structure Complete proteome Glyoxylate bypass Magnesium Manganese Metal-binding NADP Oxidoreductase Reference proteome Tricarboxylic acid cycle	46417.77	224308	Bacillus subtilis (strain 168)	Icd	Isocitrate dehydrogenase [NADP]	Icd	5 references	MAQGEKITVSNGVLNVPNNPIIPFIEGDGTGPDIWNAASKVLEAAVEKAYKGEKKITWKE VYAGEKAYNKTGEWLPAETLDVIREYFIAIKGPLTTPVGGGIRSLNVALRQELDLFVCLR PVRYFTGVPSPVKRPEDTDMVIFRENTEDIYAGIEYAKGSEEVQKLISFLQNELNVNKIR FPETSGIGIKPVSEEGTSRLVRAAIDYAIEHGRKSVTLVHKGNIMKFTEGAFKNWGYELA EKEYGDKVFTWAQYDRIAEEQGKDAANKAQSEAEAAGKIIIKDSIADIFLQQILTRPNEF DVVATMNLNGDYISDALAAQVGGIGIAPGANINYETGHAIFEATHGTAPKYAGLDKVNPS SVILSGVLLLEHLGWNEAADLVIKSMEKTIASKVVTYDFARLMDGATEVKCSEFGEELIK NMD	IDH_BACSU	P39126
IlvC	433	407	Sorry, but iframe obviously are not supported by your browser.	N.A.	N.A.	1026	342		A0A0K6MM04	336		ilvC_1	F:isomerase activity [GO:0016853] F:ketol-acid reductoisomerase activity [GO:0004455] P:isoleucine biosynthetic process [GO:0009097] P:valine biosynthetic process [GO:0009099]	5.0436	Amino-acid biosynthesis Branched-chain amino acid biosynthesis Isomerase NADP Oxidoreductase	36678.64	1423	Bacillus subtilis	IlvC	Ketol-acid reductoisomerase	IlvC	1 references	MAKVYYEKDVTVNVLKEKKVAIIGYGSQGHAHAQNLRDNGFDVVVGLRKGKSWDKAKEDG FSVYTVAEAAKQADVVMILLPDELQPEVYEAEIAPNLQAGNSLVFAHGFNVHFDQVKPPV NVDVFLVAPKGPGHLVRRTFSEGGAVPALFAVYQDATGVATEKALSYADGIGATRAGVLE TTFKEETETDLFGEQAVLCGGVTALVKAGFETLVDAGYQPELAYFECLHELKLIVDLMYE GGLENMRYSVSDTAQWGDFVSGPRVVTEDTKKAMGAVLAEIQDGTFARGWIAEHKAGRPN FHATNEKENEHEIEVVGRKLREMMPFVQPRVKAGVK	A0A0K6MM04_BACIU	A0A0K6MM04
KatA	203	259	Sorry, but iframe obviously are not supported by your browser.	N.A.	N.A.	1449	483		P26901	483	Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide.	katA	C:cytoplasm [GO:0005737] F:catalase activity [GO:0004096] F:heme binding [GO:0020037] F:metal ion binding [GO:0046872] P:hydrogen peroxide catabolic process [GO:0042744] P:response to hydrogen peroxide [GO:0042542]	6.5104	Complete proteome Cytoplasm Direct protein sequencing Heme Hydrogen peroxide Iron Metal-binding Oxidoreductase Peroxidase Reference proteome	54791.29	224308	Bacillus subtilis (strain 168)	KatA	Vegetative catalase	KatA	8 references	MSSNKLTTSWGAPVGDNQNSMTAGSRGPTLIQDVHLLEKLAHFNRERVPERVVHAKGAGA HGYFEVTNDVTKYTKAAFLSEVGKRTPLFIRFSTVAGELGSADTVRDPRGFAVKFYTEEG NYDIVGNNTPVFFIRDAIKFPDFIHTQKRDPKTHLKNPTAVWDFWSLSPESLHQVTILMS DRGIPATLRHMHGFGSHTFKWTNAEGEGVWIKYHFKTEQGVKNLDVNTAAKIAGENPDYH TEDLFNAIENGDYPAWKLYVQIMPLEDANTYRFDPFDVTKVWSQKDYPLIEVGRMVLDRN PENYFAEVEQATFSPGTLVPGIDVSPDKMLQGRLFAYHDAHRYRVGANHQALPINRARNK VNNYQRDGQMRFDDNGGGSVYYEPNSFGGPKESPEDKQAAYPVQGIADSVSYDHYDHYTQ AGDLYRLMSEDERTRLVENIVNAMKPVEKEEIKLRQIEHFYKADPEYGKRVAEGLGLPIK KDS	CATA_BACSU	P26901
Mdh	691	446	Sorry, but iframe obviously are not supported by your browser.	N.A.	N.A.	936	312		P49814	312	Catalyzes the reversible oxidation of malate to oxaloacetate.	mdh	F:L-malate dehydrogenase activity [GO:0030060] P:carbohydrate metabolic process [GO:0005975] P:tricarboxylic acid cycle [GO:0006099]	4.6439	Complete proteome Direct protein sequencing NAD Oxidoreductase Phosphoprotein Reference proteome Tricarboxylic acid cycle	33643.53	224308	Bacillus subtilis (strain 168)	Mdh	Malate dehydrogenase	Mdh	6 references	MGNTRKKVSVIGAGFTGATTAFLIAQKELADVVLVDIPQLENPTKGKALDMLEASPVQGF DAKITGTSNYEDTAGSDIVVITAGIARKPGMSRDDLVSTNEKIMRSVTQEIVKYSPDSII VVLTNPVDAMTYAVYKESGFPKERVIGQSGVLDTARFRTFVAEELNLSVKDVTGFVLGGH GDDMVPLVRYSYAGGIPLETLIPKERIDAIVERTRKGGGEIVNLLGNGSAYYAPAASLTE MVEAILKDQRRVLPTIAYLEGEYGYEGIYLGVPTIVGGNGLEQIIELELTDYERAQLNKS VESVKNVMKVLS	MDH_BACSU	P49814
Pgk	674	348	Sorry, but iframe obviously are not supported by your browser.	N.A.	N.A.	1182	394		P40924	394		pgk	C:cytoplasm [GO:0005737] F:ATP binding [GO:0005524] F:phosphoglycerate kinase activity [GO:0004618] P:glycolytic process [GO:0006096]	4.7054	ATP-binding Complete proteome Cytoplasm Direct protein sequencing Glycolysis Kinase Nucleotide-binding Phosphoprotein Reference proteome Transferase	42190.29	224308	Bacillus subtilis (strain 168)	Pgk	Phosphoglycerate kinase	Pgk	4 references	MNKKTLKDIDVKGKVVFCRVDFNVPMKDGEVTDDTRIRAALPTIKHLADQGAKVLLASHL GRPKGEVVEELRLTPVAARLGELLGKEVKKADEAYGDAVKAQISEMKDGDVLVLENVRFY PGEEKNDPELAKAFAELADVYVNDAFGAAHRAHASTAGIAEHLPAVAGFLMEKELDVLGK AVSNPDRPFTAIIGGAKVKDKIGVIESLLDKVDNLIIGGGLAYTFVKALGYEVGKSLLEE DKIELAKSFMDRAKEKGVNFYMPEDVLVADDFSNDANVKIVPISEIPSDLEAIDIGTKTR ETYADVIKNSKLVVWNGPMGVFEIDLFAQGTKAVAEALAEAKDTYSVIGGGDSAAAVEKF GLADKMSHISTGGGASLEFMEGKELPGVAALNDK	PGK_BACSU	P40924
PtsH	676	997	Sorry, but iframe obviously are not supported by your browser.	N.A.	N.A.	264	88	transfers phosphate from enzyme I to specific enzymes II/III permeases; mediates carbon catabolite repression (CCR)	P08877	88	General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The phosphoryl group from phosphoenolpyruvate (PEP) is transferred to the phosphoryl carrier protein HPr by enzyme I. Phospho-HPr then transfers it to the permease (enzymes II/III).	ptsH	C:cytoplasm [GO:0005737] F:protein serine/threonine kinase activity [GO:0004674] P:phosphoenolpyruvate-dependent sugar phosphotransferase system [GO:0009401] P:regulation of carbohydrate utilization [GO:0043610] P:regulation of transcription, DNA-templated [GO:0006355] P:transcription, DNA-templated [GO:0006351]	4.5183	3D-structure Complete proteome Cytoplasm Direct protein sequencing Kinase Phosphoprotein Phosphotransferase system Reference proteome Serine/threonine-protein kinase Sugar transport Transcription Transcription regulation Transferase Transport	9189.36	224308	Bacillus subtilis (strain 168)	PtsH	Phosphocarrier protein HPr	PtsH	13 references	MAQKTFKVTADSGIHARPATVLVQTASKYDADVNLEYNGKTVNLKSIMGVMSLGIAKGAE ITISASGADENDALNALEETMKSEGLGE	PTHP_BACSU	P08877
RsbW	870	775	Sorry, but iframe obviously are not supported by your browser.	N.A.	N.A.	480	160	negative regulation of sigma-B-dependent gene expression; phosphorylation of RsbV	P17904	160	Negative regulator of sigma-B activity. Phosphorylates and inactivates its specific antagonist protein, RsbV. Upon phosphorylation of RsbV, RsbW is released and binds to sigma-B, thereby blocking its ability to form an RNA polymerase holoenzyme (E-sigma-B).	rsbW	F:ATP binding [GO:0005524] F:protein serine/threonine kinase activity [GO:0004674] F:sigma factor antagonist activity [GO:0016989] P:negative regulation of transcription, DNA-templated [GO:0045892]	4.231	ATP-binding Complete proteome Direct protein sequencing Kinase Nucleotide-binding Reference proteome Serine/threonine-protein kinase Stress response Transferase	17993.0	224308	Bacillus subtilis (strain 168)	RsbW	Serine-protein kinase RsbW	RsbW	9 references	MKNNADYIEMKVPAQPEYVGIIRLTLSGVASRMGYTYDEIEDLKIAVSEACTNAVQHAYK EDKNGEVSIRFGVFEDRLEVIVADEGDSFDFDQKQQDLGPYTPSHTVDQLSEGGLGLYLM ETLMDEVRVQNHSGVTVAMTKYLNGERVDHDTTIKNYETN	RSBW_BACSU	P17904
SodA	608	665	Sorry, but iframe obviously are not supported by your browser.	N.A.	N.A.	606	202		P54375	202	Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.	sodA	C:cytoplasm [GO:0005737] F:metal ion binding [GO:0046872] F:superoxide dismutase activity [GO:0004784]	5.0621	3D-structure Complete proteome Cytoplasm Direct protein sequencing Manganese Metal-binding Oxidoreductase Phosphoprotein Reference proteome Stress response	22489.95	224308	Bacillus subtilis (strain 168)	SodA	Superoxide dismutase [Mn]	SodA	8 references	MAYELPELPYAYDALEPHIDKETMTIHHTKHHNTYVTNLNKAVEGNTALANKSVEELVAD LDSVPENIRTAVRNNGGGHANHKLFWTLLSPNGGGEPTGALAEEINSVFGSFDKFKEQFA AAAAGRFGSGWAWLVVNNGKLEITSTPNQDSPLSEGKTPILGLDVWEHAYYLNYQNRRPD YISAFWNVVNWDEVARLYSEAK	SODM_BACSU	P54375
YdbD	644	513	Sorry, but iframe obviously are not supported by your browser.	N.A.	N.A.	819	273	unknown	P80878	273		ydbD	F:catalase activity [GO:0004096] F:metal ion binding [GO:0046872]	4.7873	Calcium Complete proteome Direct protein sequencing Manganese Metal-binding Oxidoreductase Peroxidase Reference proteome Stress response	30257.37	224308	Bacillus subtilis (strain 168)	YdbD	Probable manganese catalase	YdbD	3 references	MFKHTKMLQHPAKPDRPDPLFAKKMQEILGGQFGEISVAMQYLFQGWNTRGNEKYKDLLM DTATEELGHVEMIATMIARLLEDAPLDQQEKAAEDPVIGSILGGMNPHHAIVSGLGAMPE SSTGVPWSGGYIVASGNLLADFRANLNAESQGRLQVARLFEMTDDKGVKDMLSFLLARDT MHQNQWLAAIKELEAQEGPVVPGTFPKALEKQEFSHQLINFSEGEVSAEQNWLNEKAPDG EAFEYVKEAKTFGEKPELKPAPPFVHNTLPGRE	MCAT_BACSU	P80878
YtxH	565	743	Sorry, but iframe obviously are not supported by your browser.	N.A.	N.A.	456	152	unknown	P40780	151		ytxH		5.0714	Complete proteome Reference proteome	16554.59	224308	Bacillus subtilis (strain 168)	YtxH	Uncharacterized protein YtxH	YtxH	3 references	MSKDGINSKDFLIGTLIGGIIGATTALFLAPKSGKELRDDLGSQAVALRDKTDKMTADAK EKGTQYVSIAKDKTSNITQLVADQSGQIMNKVKDLRDRSKSDKTDSSTAMQDMREEAMQA ADETKDQVLQTKEDVKDELKDAQKQAEQLNR	YTXH_BACSU	P40780
YvyD	518	622	Sorry, but iframe obviously are not supported by your browser.	N.A.	N.A.	567	189	unknown	G4P1B5	189		raiA	P:primary metabolic process [GO:0044238]	5.3935	Complete proteome	21950.72	1052585	Bacillus subtilis subsp. spizizenii (strain TU-B-10)	YvyD		YvyD	1 references	MNYNIRGENIEVTPALKDHVEKKIGKLERYFDHSVNADVNVNLKFYNDKESKVEVTIPMT DLALRSEVHNEDMYNAIDLATNKLERQIRKHKTKVNRKFREQGSPKYLLANGLGSDTDIA VQDEIEDEESLDIVRQKRFNLKPMDSEEAILQMNMLGHNFFVFTNAETNLTNVVYRRNDG KYGLIEPTE	G4P1B5_BACPT	G4P1B5

Delta2D Report: Labelsfor Project 'Demonstration'

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Delta2D Report: Labels
for Project 'Demonstration'