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Protein

Chemotaxis protein CheY

Gene

cheY

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. In its active (phosphorylated or acetylated) form, CheY exhibits enhanced binding to a switch component, FliM, at the flagellar motor which induces a change from counterclockwise to clockwise flagellar rotation. Shows autophosphatase activity which is enhanced by CheZ.

Cofactori

Mg2+Note: Binds 1 Mg2+ ion per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi12Magnesium1
Metal bindingi13Magnesium1
Metal bindingi57Magnesium1
Metal bindingi59Magnesium; via carbonyl oxygen1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Chemotaxis, Flagellar rotation, Two-component regulatory system

Keywords - Ligandi

Magnesium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Chemotaxis protein CheY
Gene namesi
Name:cheY
Ordered Locus Names:STM1916
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeSalmonella
Proteomesi
  • UP000001014 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi13D → N: Abolishes function, reduced rate of phosphorylation and affinity for magnesium ion. 1 Publication1
Mutagenesisi14F → A: Diminished rate of phosphorylation. 1 Publication1
Mutagenesisi57D → N: Abolishes function and phosphorylation. 1 Publication1
Mutagenesisi59N → A: Diminished rate of phosphorylation. 1 Publication1
Mutagenesisi109K → R: Abolishes function, decreased autophosphatase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00000810452 – 129Chemotaxis protein CheYAdd BLAST128

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei574-aspartylphosphatePROSITE-ProRule annotation2 Publications1
Modified residuei92N6-acetyllysineBy similarity1
Modified residuei109N6-acetyllysineBy similarity1

Post-translational modificationi

Phosphorylated by CheA or acetylated by acetyl-CoA synthetase, depending on which acetate metabolism pathway is available (By similarity). Dephosphorylated (inactivated) by CheZ.By similarity2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP0A2D5.
PRIDEiP0A2D5.

Interactioni

Subunit structurei

Interacts (phosphorylated CheY) with CheZ (via C-terminus).3 Publications

Protein-protein interaction databases

STRINGi99287.STM1916.

Structurei

Secondary structure

1129
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi8 – 11Combined sources4
Helixi15 – 28Combined sources14
Beta strandi33 – 38Combined sources6
Helixi39 – 46Combined sources8
Beta strandi53 – 58Combined sources6
Beta strandi61 – 63Combined sources3
Helixi65 – 74Combined sources10
Turni76 – 80Combined sources5
Beta strandi83 – 89Combined sources7
Helixi92 – 100Combined sources9
Beta strandi104 – 110Combined sources7
Helixi113 – 127Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CHEX-ray1.80A2-129[»]
2CHFX-ray1.80A2-129[»]
2CHYX-ray2.70A2-129[»]
2FKAX-ray2.00A1-129[»]
2FLKX-ray2.10A1-129[»]
2FLWX-ray2.00A1-129[»]
2FMFX-ray2.00A1-129[»]
2FMHX-ray2.00A1-129[»]
2FMIX-ray2.30A1-129[»]
2FMKX-ray2.00A1-129[»]
2PL9X-ray2.60A/B/C2-129[»]
2PMCX-ray2.69A/B/C/D2-129[»]
ProteinModelPortaliP0A2D5.
SMRiP0A2D5.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A2D5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini7 – 124Response regulatoryPROSITE-ProRule annotationAdd BLAST118

Sequence similaritiesi

Contains 1 response regulatory domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4108VYJ. Bacteria.
COG0784. LUCA.
HOGENOMiHOG000034820.
KOiK03413.
OMAiMLQSGAF.
PhylomeDBiP0A2D5.

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.

P0A2D5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADKELKFLV VDDFSTMRRI VRNLLKELGF NNVEEAEDGV DALNKLQAGG
60 70 80 90 100
FGFIISDWNM PNMDGLELLK TIRADSAMSA LPVLMVTAEA KKENIIAAAQ
110 120
AGASGYVVKP FTAATLEEKL NKIFEKLGM
Length:129
Mass (Da):14,125
Last modified:January 23, 2007 - v2
Checksum:iA0B4712E18626207
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12131 Genomic DNA. Translation: AAA27037.1.
AE006468 Genomic DNA. Translation: AAL20832.1.
PIRiA23567. QREBCY.
RefSeqiNP_460873.1. NC_003197.1.
WP_000763861.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL20832; AAL20832; STM1916.
GeneIDi1253437.
KEGGistm:STM1916.
PATRICi32382387. VBISalEnt20916_2032.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12131 Genomic DNA. Translation: AAA27037.1.
AE006468 Genomic DNA. Translation: AAL20832.1.
PIRiA23567. QREBCY.
RefSeqiNP_460873.1. NC_003197.1.
WP_000763861.1. NC_003197.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CHEX-ray1.80A2-129[»]
2CHFX-ray1.80A2-129[»]
2CHYX-ray2.70A2-129[»]
2FKAX-ray2.00A1-129[»]
2FLKX-ray2.10A1-129[»]
2FLWX-ray2.00A1-129[»]
2FMFX-ray2.00A1-129[»]
2FMHX-ray2.00A1-129[»]
2FMIX-ray2.30A1-129[»]
2FMKX-ray2.00A1-129[»]
2PL9X-ray2.60A/B/C2-129[»]
2PMCX-ray2.69A/B/C/D2-129[»]
ProteinModelPortaliP0A2D5.
SMRiP0A2D5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi99287.STM1916.

Proteomic databases

PaxDbiP0A2D5.
PRIDEiP0A2D5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL20832; AAL20832; STM1916.
GeneIDi1253437.
KEGGistm:STM1916.
PATRICi32382387. VBISalEnt20916_2032.

Phylogenomic databases

eggNOGiENOG4108VYJ. Bacteria.
COG0784. LUCA.
HOGENOMiHOG000034820.
KOiK03413.
OMAiMLQSGAF.
PhylomeDBiP0A2D5.

Miscellaneous databases

EvolutionaryTraceiP0A2D5.

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...

Entry informationi

Entry nameiCHEY_SALTY
AccessioniPrimary (citable) accession number: P0A2D5
Secondary accession number(s): P06657
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 89 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.