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Protein

Chemotaxis protein CheA

Gene

cheA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Chemotaxis, Two-component regulatory system

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciBSUB:BSU16430-MONOMER.
BRENDAi2.7.13.3. 658.

Names & Taxonomyi

Protein namesi
Recommended name:
Chemotaxis protein CheA (EC:2.7.13.3)
Gene namesi
Name:cheA
Synonyms:cheN
Ordered Locus Names:BSU16430
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

  • Membrane Curated

  • 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.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 672672Chemotaxis protein CheAPRO_0000074711Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei46 – 461Phosphohistidine; by autocatalysisPROSITE-ProRule annotation

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP29072.

Interactioni

Protein-protein interaction databases

IntActiP29072. 7 interactions.
STRINGi224308.Bsubs1_010100009061.

Structurei

3D structure databases

ProteinModelPortaliP29072.
SMRiP29072. Positions 3-104, 292-670.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 103103HPtPROSITE-ProRule annotationAdd
BLAST
Domaini290 – 540251Histidine kinasePROSITE-ProRule annotationAdd
BLAST
Domaini542 – 672131CheW-likePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 cheW-like domain.PROSITE-ProRule annotation
Contains 1 histidine kinase domain.PROSITE-ProRule annotation
Contains 1 HPt domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105CBS. Bacteria.
COG0643. LUCA.
HOGENOMiHOG000255264.
InParanoidiP29072.
KOiK03407.
OMAiYHSGNHV.
OrthoDBiEOG62RS8P.
PhylomeDBiP29072.

Family and domain databases

Gene3Di1.10.287.560. 1 hit.
1.20.120.160. 1 hit.
3.30.565.10. 1 hit.
3.30.70.1110. 1 hit.
InterProiIPR004105. CheA-like_dim.
IPR002545. CheW.
IPR015162. CheY-binding.
IPR003594. HATPase_C.
IPR005467. His_kinase_dom.
IPR003661. HisK_dim/P.
IPR004358. Sig_transdc_His_kin-like_C.
IPR008207. Sig_transdc_His_kin_Hpt_dom.
IPR010808. Sig_transdc_His_kinase_P2-bd.
[Graphical view]
PfamiPF01584. CheW. 1 hit.
PF02895. H-kinase_dim. 1 hit.
PF02518. HATPase_c. 1 hit.
PF01627. Hpt. 1 hit.
PF07194. P2. 1 hit.
[Graphical view]
PRINTSiPR00344. BCTRLSENSOR.
SMARTiSM00260. CheW. 1 hit.
SM01231. H-kinase_dim. 1 hit.
SM00387. HATPase_c. 1 hit.
SM00073. HPT. 1 hit.
[Graphical view]
SUPFAMiSSF47226. SSF47226. 1 hit.
SSF47384. SSF47384. 1 hit.
SSF50341. SSF50341. 1 hit.
SSF55052. SSF55052. 1 hit.
SSF55874. SSF55874. 1 hit.
PROSITEiPS50851. CHEW. 1 hit.
PS50109. HIS_KIN. 1 hit.
PS50894. HPT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P29072-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDMNQYLDVF IDESKEHLQT CNEKLLLLEK DPTDLQLVHD IFRAAHTLKG
60 70 80 90 100
MSATMGYTDL AHLTHLLENV LDAIRNGDME VTSDWLDILF EALDHLETMV
110 120 130 140 150
QSIIDGGDGK RDISEVSAKL DVNGAHAESA ASAEPAEAQS SASDWEYDEF
160 170 180 190 200
ERTVIQEAEE QGFKRYEIKI SLNENCMLKA VRVYMVFEKL NEVGEVAKTI
210 220 230 240 250
PSAEVLETED FGTDFQVCFL THQSAEDIEQ LINGVSEIEH VEVIQGAPLT
260 270 280 290 300
SAEKPEESKQ EDSPAAAVPA KQEKQKQPAK NDEQAKHSAG GSKTIRVNID
310 320 330 340 350
RLDSLMNLFE ELVIDRGRLE QIAKELEHNE LTETVERMTR ISGDLQSIIL
360 370 380 390 400
NMRMVPVETV FNRFPRMIRQ LQKELNKKIE LSIIGAETEL DRTVIDEIGD
410 420 430 440 450
PLVHLIRNSI DHGIEAPETR LQKGKPESGK VVLKAYHSGN HVFIEVEDDG
460 470 480 490 500
AGLNRKKILE KALERGVITE KEAETLEDNQ IYELIFAPGF STADQISDIS
510 520 530 540 550
GRGVGLDVVK NKLESLGGSV SVKSAEGQGS LFSIQLPLTL SIISVLLIKL
560 570 580 590 600
EEETFAIPIS SIIETAVIDR KDILQTHDRE VIDFRGHIVP VVYLKEEFKI
610 620 630 640 650
EDTRKDAEQL HIIVVKKGDK PTAFVVDSFI GQQEVVLKSL GDYLTNVFAI
660 670
SGATILGDGE VALIIDCNAL II
Length:672
Mass (Da):74,812
Last modified:June 16, 2009 - v2
Checksum:i7BC3456AC34CB999
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti271 – 2722KQ → NE in AAA22313 (PubMed:1938941).Curated
Sequence conflicti462 – 4621A → P in AAA22313 (PubMed:1938941).Curated
Sequence conflicti466 – 4661Missing in AAA22313 (PubMed:1938941).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M57894 Genomic DNA. Translation: AAA22313.1.
AL009126 Genomic DNA. Translation: CAB13516.2.
PIRiA41653. QRBSCN.
RefSeqiNP_389525.2. NC_000964.3.
WP_003245734.1. NZ_JNCM01000035.1.

Genome annotation databases

EnsemblBacteriaiCAB13516; CAB13516; BSU16430.
GeneIDi939600.
KEGGibsu:BSU16430.
PATRICi18975093. VBIBacSub10457_1738.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M57894 Genomic DNA. Translation: AAA22313.1.
AL009126 Genomic DNA. Translation: CAB13516.2.
PIRiA41653. QRBSCN.
RefSeqiNP_389525.2. NC_000964.3.
WP_003245734.1. NZ_JNCM01000035.1.

3D structure databases

ProteinModelPortaliP29072.
SMRiP29072. Positions 3-104, 292-670.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP29072. 7 interactions.
STRINGi224308.Bsubs1_010100009061.

Proteomic databases

PaxDbiP29072.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB13516; CAB13516; BSU16430.
GeneIDi939600.
KEGGibsu:BSU16430.
PATRICi18975093. VBIBacSub10457_1738.

Phylogenomic databases

eggNOGiENOG4105CBS. Bacteria.
COG0643. LUCA.
HOGENOMiHOG000255264.
InParanoidiP29072.
KOiK03407.
OMAiYHSGNHV.
OrthoDBiEOG62RS8P.
PhylomeDBiP29072.

Enzyme and pathway databases

BioCyciBSUB:BSU16430-MONOMER.
BRENDAi2.7.13.3. 658.

Family and domain databases

Gene3Di1.10.287.560. 1 hit.
1.20.120.160. 1 hit.
3.30.565.10. 1 hit.
3.30.70.1110. 1 hit.
InterProiIPR004105. CheA-like_dim.
IPR002545. CheW.
IPR015162. CheY-binding.
IPR003594. HATPase_C.
IPR005467. His_kinase_dom.
IPR003661. HisK_dim/P.
IPR004358. Sig_transdc_His_kin-like_C.
IPR008207. Sig_transdc_His_kin_Hpt_dom.
IPR010808. Sig_transdc_His_kinase_P2-bd.
[Graphical view]
PfamiPF01584. CheW. 1 hit.
PF02895. H-kinase_dim. 1 hit.
PF02518. HATPase_c. 1 hit.
PF01627. Hpt. 1 hit.
PF07194. P2. 1 hit.
[Graphical view]
PRINTSiPR00344. BCTRLSENSOR.
SMARTiSM00260. CheW. 1 hit.
SM01231. H-kinase_dim. 1 hit.
SM00387. HATPase_c. 1 hit.
SM00073. HPT. 1 hit.
[Graphical view]
SUPFAMiSSF47226. SSF47226. 1 hit.
SSF47384. SSF47384. 1 hit.
SSF50341. SSF50341. 1 hit.
SSF55052. SSF55052. 1 hit.
SSF55874. SSF55874. 1 hit.
PROSITEiPS50851. CHEW. 1 hit.
PS50109. HIS_KIN. 1 hit.
PS50894. HPT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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.
    , 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, PHOSPHORYLATION OF CHEV.
    Strain: 168 / OI1085.

Entry informationi

Entry nameiCHEA_BACSU
AccessioniPrimary (citable) accession number: P29072
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: June 16, 2009
Last modified: May 11, 2016
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.