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P29072 (CHEA_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chemotaxis protein CheA
EC=2.7.13.3
Gene names
Name:cheA
Synonyms:cheN
Ordered Locus Names:BSU16430
OrganismBacillus subtilis
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length672 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. CheA is autophosphorylated; it can transfer its phosphate group to CheB, CheY or CheV. Ref.4

Catalytic activity

ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. Ref.4

Subcellular location

Membrane Potential. Note: It is not known whether CheA is actually membrane bound although CheA has two regions at the C-terminal end with the potential to be transmembrane regions.

Sequence similarities

Contains 1 cheW-like domain.

Contains 1 histidine kinase domain.

Contains 1 HPt domain.

Ontologies

Keywords
   Biological processChemotaxis
Two-component regulatory system
   Cellular componentMembrane
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processcellular component movement

Inferred from electronic annotation. Source: InterPro

chemotaxis

Inferred from electronic annotation. Source: UniProtKB-KW

peptidyl-histidine phosphorylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: InterPro

membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

two-component sensor activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 672672Chemotaxis protein CheA
PRO_0000074711

Regions

Domain1 – 103103HPt
Domain290 – 540251Histidine kinase
Domain542 – 672131CheW-like

Amino acid modifications

Modified residue461Phosphohistidine; by autocatalysis By similarity

Experimental info

Sequence conflict271 – 2722KQ → NE in AAA22313. Ref.1
Sequence conflict4621A → P in AAA22313. Ref.1
Sequence conflict4661Missing in AAA22313. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P29072 [UniParc].

Last modified June 16, 2009. Version 2.
Checksum: 7BC3456AC34CB999

FASTA67274,812
        10         20         30         40         50         60 
MDMNQYLDVF IDESKEHLQT CNEKLLLLEK DPTDLQLVHD IFRAAHTLKG MSATMGYTDL 

        70         80         90        100        110        120 
AHLTHLLENV LDAIRNGDME VTSDWLDILF EALDHLETMV QSIIDGGDGK RDISEVSAKL 

       130        140        150        160        170        180 
DVNGAHAESA ASAEPAEAQS SASDWEYDEF ERTVIQEAEE QGFKRYEIKI SLNENCMLKA 

       190        200        210        220        230        240 
VRVYMVFEKL NEVGEVAKTI PSAEVLETED FGTDFQVCFL THQSAEDIEQ LINGVSEIEH 

       250        260        270        280        290        300 
VEVIQGAPLT SAEKPEESKQ EDSPAAAVPA KQEKQKQPAK NDEQAKHSAG GSKTIRVNID 

       310        320        330        340        350        360 
RLDSLMNLFE ELVIDRGRLE QIAKELEHNE LTETVERMTR ISGDLQSIIL NMRMVPVETV 

       370        380        390        400        410        420 
FNRFPRMIRQ LQKELNKKIE LSIIGAETEL DRTVIDEIGD PLVHLIRNSI DHGIEAPETR 

       430        440        450        460        470        480 
LQKGKPESGK VVLKAYHSGN HVFIEVEDDG AGLNRKKILE KALERGVITE KEAETLEDNQ 

       490        500        510        520        530        540 
IYELIFAPGF STADQISDIS GRGVGLDVVK NKLESLGGSV SVKSAEGQGS LFSIQLPLTL 

       550        560        570        580        590        600 
SIISVLLIKL EEETFAIPIS SIIETAVIDR KDILQTHDRE VIDFRGHIVP VVYLKEEFKI 

       610        620        630        640        650        660 
EDTRKDAEQL HIIVVKKGDK PTAFVVDSFI GQQEVVLKSL GDYLTNVFAI SGATILGDGE 

       670 
VALIIDCNAL II

« Hide

References

« Hide 'large scale' references
[1]"Bacillus subtilis CheN, a homolog of CheA, the central regulator of chemotaxis in Escherichia coli."
Fuhrer D.K., Ordal G.W.
J. Bacteriol. 173:7443-7448(1991) [PubMed: 1938941] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[3]"From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
Microbiology 155:1758-1775(2009) [PubMed: 19383706] [Abstract]
Cited for: SEQUENCE REVISION TO 271-272; 462 AND 466.
[4]"Phosphorylation of the response regulator CheV is required for adaptation to attractants during Bacillus subtilis chemotaxis."
Karatan E., Saulmon M.M., Bunn M.W., Ordal G.W.
J. Biol. Chem. 276:43618-43626(2001) [PubMed: 11553614] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, PHOSPHORYLATION OF CHEV.
Strain: 168 / OI1085.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M57894 Genomic DNA. Translation: AAA22313.1.
AL009126 Genomic DNA. Translation: CAB13516.2.
PIRQRBSCN. A41653.
RefSeqNP_389525.2. NC_000964.3.

3D structure databases

ProteinModelPortalP29072.
SMRP29072. Positions 3-104, 292-670.
ModBaseSearch...

Protein-protein interaction databases

IntActP29072. 6 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000001730; EBBACP00000001730; EBBACG00000001728.
GeneID939600.
GenomeReviewsGene locus BSU16430 in contig AL009126_GR.
KEGGbsu:BSU16430.
NMPDRfig|224308.1.peg.1646.
PATRIC18975093. VBIBacSub10457_1738.

Organism-specific databases

GenoListBSU16430. [Micado]

Phylogenomic databases

GeneTreeEBGT00050000002175.
HOGENOMHBG705053.
PhylomeDBP29072.
ProtClustDBCLSK873472.

Enzyme and pathway databases

BioCycBSUB:BSU16430-MONOMER.
BRENDA2.7.13.3. 700.

Family and domain databases

InterProIPR003594. ATPase-like_ATP-bd.
IPR002545. CheW.
IPR004358. Sig_transdc_His_kin-like_C.
IPR008207. Sig_transdc_His_kin_Hpt_dom.
IPR004105. Sig_transdc_His_kin_subgr_dim.
IPR005467. Sig_transdc_His_kinase_core.
IPR009082. Sig_transdc_His_kinase_dimeric.
IPR010808. Sig_transdc_His_kinase_P2-bd.
[Graphical view]
Gene3DG3DSA:3.30.565.10. ATP_bd_ATPase. 1 hit.
G3DSA:3.30.70.1110. G3DSA:3.30.70.1110. 1 hit.
G3DSA:1.20.120.160. Sig_transdc_His_kin_Hpt_dom. 1 hit.
G3DSA:1.10.287.560. Sig_transdc_His_kin_subgr_dim. 1 hit.
KOK03407.
PfamPF01584. CheW. 1 hit.
PF02895. H-kinase_dim. 1 hit.
PF02518. HATPase_c. 1 hit.
PF01627. Hpt. 1 hit.
PF07194. P2. 1 hit.
[Graphical view]
PRINTSPR00344. BCTRLSENSOR.
SMARTSM00260. CheW. 1 hit.
SM00387. HATPase_c. 1 hit.
SM00073. HPT. 1 hit.
[Graphical view]
SUPFAMSSF55874. ATP_bd_ATPase. 1 hit.
SSF50341. CheW. 1 hit.
SSF47384. His_kin_homodim. 1 hit.
SSF47226. Hpt. 1 hit.
PROSITEPS50851. CHEW. 1 hit.
PS50109. HIS_KIN. 1 hit.
PS50894. HPT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCHEA_BACSU
AccessionPrimary (citable) accession number: P29072
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: June 16, 2009
Last modified: January 25, 2012
This is version 98 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents