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Protein

Chemotaxis protein CheY

Gene

cheY

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. Phosphorylated CheY interacts with the flagella switch components FliM and FliY, which causes counterclockwise rotation of the flagella, resulting in smooth swimming.2 Publications

Cofactori

Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi9 – 91MagnesiumBy similarity
Metal bindingi10 – 101MagnesiumBy similarity
Metal bindingi54 – 541MagnesiumBy similarity
Metal bindingi56 – 561Magnesium; via carbonyl oxygenBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Chemotaxis, Two-component regulatory system

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciBSUB:BSU16330-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Chemotaxis protein CheY
Gene namesi
Name:cheY
Synonyms:cheB
Ordered Locus Names:BSU16330
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi10 – 101D → K or R: No chemotaxis, tumbly swimming behavior and shows exclusively clockwise rotation. 1 Publication
Mutagenesisi54 – 541D → A: Lack of phosphorylation. No chemotaxis, tumbly swimming behavior and shows exclusively clockwise rotation. 2 Publications
Mutagenesisi54 – 541D → S or T: No chemotaxis, tumbly swimming behavior and shows exclusively clockwise rotation. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 120119Chemotaxis protein CheYPRO_0000081057Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei54 – 5414-aspartylphosphatePROSITE-ProRule annotation

Post-translational modificationi

Phosphorylated by CheA. Dephosphorylated (inactivated) by FliY and CheC.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP24072.

Interactioni

Subunit structurei

Phosphorylated CheY binds to FliM and FliY.1 Publication

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100009011.

Structurei

3D structure databases

ProteinModelPortaliP24072.
SMRiP24072. Positions 4-117.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 119116Response regulatoryPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 response regulatory domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4107YTP. Bacteria.
COG0784. LUCA.
HOGENOMiHOG000034820.
InParanoidiP24072.
KOiK03413.
OMAiLFMRKML.
OrthoDBiEOG6PKFC7.
PhylomeDBiP24072.

Family and domain databases

InterProiIPR011006. CheY-like_superfamily.
IPR001789. Sig_transdc_resp-reg_receiver.
[Graphical view]
PfamiPF00072. Response_reg. 1 hit.
[Graphical view]
SMARTiSM00448. REC. 1 hit.
[Graphical view]
SUPFAMiSSF52172. SSF52172. 1 hit.
PROSITEiPS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P24072-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAHRILIVDD AAFMRMMIKD ILVKNGFEVV AEAENGAQAV EKYKEHSPDL
60 70 80 90 100
VTMDITMPEM DGITALKEIK QIDAQARIIM CSAMGQQSMV IDAIQAGAKD
110 120
FIVKPFQADR VLEAINKTLN
Length:120
Mass (Da):13,310
Last modified:January 23, 2007 - v3
Checksum:iC3F1A0F02CE67505
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M59781 Genomic DNA. Translation: AAA22311.1.
AL009126 Genomic DNA. Translation: CAB13506.1.
M86738 Genomic DNA. Translation: AAA22450.1.
M87005 Genomic DNA. Translation: AAA22451.1.
PIRiA40874.
RefSeqiNP_389515.1. NC_000964.3.
WP_003244957.1. NZ_JNCM01000035.1.

Genome annotation databases

EnsemblBacteriaiCAB13506; CAB13506; BSU16330.
GeneIDi940120.
KEGGibsu:BSU16330.
PATRICi18975073. VBIBacSub10457_1728.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M59781 Genomic DNA. Translation: AAA22311.1.
AL009126 Genomic DNA. Translation: CAB13506.1.
M86738 Genomic DNA. Translation: AAA22450.1.
M87005 Genomic DNA. Translation: AAA22451.1.
PIRiA40874.
RefSeqiNP_389515.1. NC_000964.3.
WP_003244957.1. NZ_JNCM01000035.1.

3D structure databases

ProteinModelPortaliP24072.
SMRiP24072. Positions 4-117.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100009011.

Proteomic databases

PaxDbiP24072.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB13506; CAB13506; BSU16330.
GeneIDi940120.
KEGGibsu:BSU16330.
PATRICi18975073. VBIBacSub10457_1728.

Phylogenomic databases

eggNOGiENOG4107YTP. Bacteria.
COG0784. LUCA.
HOGENOMiHOG000034820.
InParanoidiP24072.
KOiK03413.
OMAiLFMRKML.
OrthoDBiEOG6PKFC7.
PhylomeDBiP24072.

Enzyme and pathway databases

BioCyciBSUB:BSU16330-MONOMER.

Family and domain databases

InterProiIPR011006. CheY-like_superfamily.
IPR001789. Sig_transdc_resp-reg_receiver.
[Graphical view]
PfamiPF00072. Response_reg. 1 hit.
[Graphical view]
SMARTiSM00448. REC. 1 hit.
[Graphical view]
SUPFAMiSSF52172. SSF52172. 1 hit.
PROSITEiPS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and characterization of Bacillus subtilis CheB, a homolog of Escherichia coli CheY, and its role in a different mechanism of chemotaxis."
    Bischoff D.S., Ordal G.W.
    J. Biol. Chem. 266:12301-12305(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168 / OI1085.
  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. "Identification and characterization of FliY, a novel component of the Bacillus subtilis flagellar switch complex."
    Bischoff D.S., Ordal G.W.
    Mol. Microbiol. 6:2715-2723(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8.
    Strain: 168 / OI1085.
  4. "Nucleotide sequences of Bacillus subtilis flagellar biosynthetic genes fliP and fliQ and identification of a novel flagellar gene, fliZ."
    Bischoff D.S., Weinreich M.D., Ordal G.W.
    J. Bacteriol. 174:4017-4025(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 96-120.
    Strain: 168 / OI1085.
  5. "Cold shock stress-induced proteins in Bacillus subtilis."
    Graumann P., Schroeder K., Schmid R., Marahiel M.A.
    J. Bacteriol. 178:4611-4619(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-13.
    Strain: 168 / JH642.
  6. "Purification and characterization of Bacillus subtilis CheY."
    Bischoff D.S., Bourret R.B., Kirsch M.L., Ordal G.W.
    Biochemistry 32:9256-9261(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION BY CHEA, MUTAGENESIS OF ASP-10 AND ASP-54.
    Strain: 168 / OI1085.
  7. "Bacillus subtilis hydrolyzes CheY-P at the location of its action, the flagellar switch."
    Szurmant H., Bunn M.W., Cannistraro V.J., Ordal G.W.
    J. Biol. Chem. 278:48611-48616(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT ASP-54, DEPHOSPHORYLATION BY FLIY, INTERACTION WITH FLIM AND FLIY, MUTAGENESIS OF ASP-54.
    Strain: 168 / OI1085.
  8. "Bacillus subtilis CheC and FliY are members of a novel class of CheY-P-hydrolyzing proteins in the chemotactic signal transduction cascade."
    Szurmant H., Muff T.J., Ordal G.W.
    J. Biol. Chem. 279:21787-21792(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEPHOSPHORYLATION BY FLIY AND CHEC.
    Strain: 168 / OI1085.

Entry informationi

Entry nameiCHEY_BACSU
AccessioniPrimary (citable) accession number: P24072
Secondary accession number(s): P37583
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: January 23, 2007
Last modified: February 17, 2016
This is version 116 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The signaling mechanism of chemotaxis in B.subtilis appears to be inverted in comparison to E.coli.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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.