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Protein

CheY-P phosphatase CheC

Gene

cheC

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Involved in restoring normal CheY-P levels by dephosphorylating CheY-P. Inhibits CheD by incorporating in its fold a structural motif that mimics a CheD substrate recognition site to bait and inactivate it.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Chemotaxis

Names & Taxonomyi

Protein namesi
Recommended name:
CheY-P phosphatase CheC (EC:3.-.-.-)
Gene namesi
Name:cheC
Ordered Locus Names:TM_0904
OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Taxonomic identifieri243274 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
Proteomesi
  • UP000008183 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi13E → S: Loss of activity, in absence of CheD; in presence of CheD, activity greater than wild-type CheC alone. Loss of activity, in absence of CheD; when associated with S-112. In presence of CheD, reduced activity but exceeds activity of CheC alone; when associated with S-112. 1 Publication1
Mutagenesisi16N → S: Loss of activity, in absence of CheD; in presence of CheD, activity greater than wild-type CheC alone. Loss of activity, in absence of CheD; when associated with S-115. In presence of CheD, almost no activity; when associated with S-115. 1 Publication1
Mutagenesisi112E → S: Loss of activity, in absence of CheD; in presence of CheD, activity greater than wild-type CheC alone. Loss of activity, in absence of CheD; when associated with S-13. In presence of CheD, reduced activity but exceeds activity of CheC alone; when associated with S-13. 1 Publication1
Mutagenesisi115N → S: Loss of activity, in absence of CheD; in presence of CheD, reduced activity. Loss of activity, in absence of CheD; when associated with S-16. In presence of CheD, almost no activity; when associated with S-16. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002509971 – 205CheY-P phosphatase CheCAdd BLAST205

Interactioni

Subunit structurei

Heterodimer with CheD. The CheC-CheD heterodimer interacts with phosphorylated CheY. The CheC-CheD dimer has higher phosphatase activity than CheC alone.1 Publication

Protein-protein interaction databases

STRINGi243274.TM0904.

Structurei

Secondary structure

1205
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 30Combined sources26
Beta strandi34 – 37Combined sources4
Beta strandi41 – 45Combined sources5
Helixi46 – 52Combined sources7
Beta strandi59 – 71Combined sources13
Beta strandi73 – 79Combined sources7
Helixi81 – 92Combined sources12
Helixi104 – 129Combined sources26
Beta strandi133 – 135Combined sources3
Beta strandi139 – 144Combined sources6
Helixi145 – 157Combined sources13
Beta strandi164 – 174Combined sources11
Beta strandi177 – 179Combined sources3
Beta strandi181 – 189Combined sources9
Helixi193 – 199Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1XKRX-ray1.75A1-205[»]
2F9ZX-ray2.40A/B1-205[»]
ProteinModelPortaliQ9X006.
SMRiQ9X006.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9X006.

Family & Domainsi

Sequence similaritiesi

Belongs to the CheC family.Curated

Phylogenomic databases

eggNOGiENOG4107PHP. Bacteria.
COG1776. LUCA.
InParanoidiQ9X006.
KOiK03410.
OMAiYIETEIF.

Family and domain databases

Gene3Di3.40.1550.10. 1 hit.
InterProiIPR007597. CheC.
IPR028976. CheC-like_dom.
[Graphical view]
PfamiPF04509. CheC. 2 hits.
[Graphical view]
SUPFAMiSSF103039. SSF103039. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9X006-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKISERQKDL LKEIGNIGAG NAATAISYMI NKKVEISVPN VEIVPISKVI
60 70 80 90 100
FIAKDPEEIV VGVKMPVTGD IEGSVLLIMG TTVVKKILEI LTGRAPDNLL
110 120 130 140 150
NLDEFSASAL REIGNIMCGT YVSALADFLG FKIDTLPPQL VIDMISAIFA
160 170 180 190 200
EASIEELEDN SEDQIVFVET LLKVEEEEEP LTSYMMMIPK PGYLVKIFER

MGIQE
Length:205
Mass (Da):22,549
Last modified:November 1, 1999 - v1
Checksum:i0FF88D0E26A927B7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD35985.1.
PIRiG72318.
RefSeqiNP_228712.1. NC_000853.1.
WP_004080665.1. NZ_CP011107.1.

Genome annotation databases

EnsemblBacteriaiAAD35985; AAD35985; TM_0904.
GeneIDi898578.
KEGGitma:TM0904.
PATRICi23936739. VBITheMar51294_0918.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD35985.1.
PIRiG72318.
RefSeqiNP_228712.1. NC_000853.1.
WP_004080665.1. NZ_CP011107.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1XKRX-ray1.75A1-205[»]
2F9ZX-ray2.40A/B1-205[»]
ProteinModelPortaliQ9X006.
SMRiQ9X006.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243274.TM0904.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD35985; AAD35985; TM_0904.
GeneIDi898578.
KEGGitma:TM0904.
PATRICi23936739. VBITheMar51294_0918.

Phylogenomic databases

eggNOGiENOG4107PHP. Bacteria.
COG1776. LUCA.
InParanoidiQ9X006.
KOiK03410.
OMAiYIETEIF.

Miscellaneous databases

EvolutionaryTraceiQ9X006.

Family and domain databases

Gene3Di3.40.1550.10. 1 hit.
InterProiIPR007597. CheC.
IPR028976. CheC-like_dom.
[Graphical view]
PfamiPF04509. CheC. 2 hits.
[Graphical view]
SUPFAMiSSF103039. SSF103039. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiCHEC_THEMA
AccessioniPrimary (citable) accession number: Q9X006
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: November 1, 1999
Last modified: November 2, 2016
This is version 84 of the entry and version 1 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.