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Q9X006 (CHEC_THEMA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 67. Feed History...

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

Names and origin

Protein namesRecommended name:
CheY-P phosphatase CheC

EC=3.-.-.-
Gene names
Name:cheC
Ordered Locus Names:TM_0904
OrganismThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) [Reference proteome] [HAMAP]
Taxonomic identifier243274 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga

Protein attributes

Sequence length205 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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

Sequence similarities

Belongs to the CheC family.

Ontologies

Keywords
   Biological processChemotaxis
   Molecular functionHydrolase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processchemotaxis

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionhydrolase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 205205CheY-P phosphatase CheC
PRO_0000250997

Experimental info

Mutagenesis131E → 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. Ref.2
Mutagenesis161N → 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. Ref.2
Mutagenesis1121E → 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. Ref.2
Mutagenesis1151N → 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. Ref.2

Secondary structure

............................. 205
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9X006 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 0FF88D0E26A927B7

FASTA20522,549
        10         20         30         40         50         60 
MKISERQKDL LKEIGNIGAG NAATAISYMI NKKVEISVPN VEIVPISKVI FIAKDPEEIV 

        70         80         90        100        110        120 
VGVKMPVTGD IEGSVLLIMG TTVVKKILEI LTGRAPDNLL NLDEFSASAL REIGNIMCGT 

       130        140        150        160        170        180 
YVSALADFLG FKIDTLPPQL VIDMISAIFA EASIEELEDN SEDQIVFVET LLKVEEEEEP 

       190        200 
LTSYMMMIPK PGYLVKIFER MGIQE 

« Hide

References

« Hide 'large scale' references
[1]"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima."
Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. expand/collapse author list , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.
Nature 399:323-329(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[2]"Structure and function of an unusual family of protein phosphatases: the bacterial chemotaxis proteins CheC and CheX."
Park S.-Y., Chao X., Gonzalez-Bonet G., Beel B.D., Bilwes A.M., Crane B.R.
Mol. Cell 16:563-574(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS), MUTAGENESIS OF GLU-13; ASN-16; GLU-112 AND ASN-115.
[3]"A receptor-modifying deamidase in complex with a signaling phosphatase reveals reciprocal regulation."
Chao X., Muff T.J., Park S.-Y., Zhang S., Pollard A.M., Ordal G.W., Bilwes A.M., Crane B.R.
Cell 124:561-571(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH CHED.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000512 Genomic DNA. Translation: AAD35985.1.
PIRG72318.
RefSeqNP_228712.1. NC_000853.1.
YP_007977256.1. NC_021214.1.
YP_008990126.1. NC_023151.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1XKRX-ray1.75A1-205[»]
2F9ZX-ray2.40A/B1-205[»]
ProteinModelPortalQ9X006.
SMRQ9X006. Positions 1-204.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243274.TM0904.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD35985; AAD35985; TM_0904.
GeneID898578.
KEGGtma:TM0904.
tmi:THEMA_00115.
tmm:Tmari_0906.
PATRIC23936739. VBITheMar51294_0918.

Phylogenomic databases

eggNOGCOG1776.
KOK03410.
OMAAPGNMFF.
OrthoDBEOG6ZPSZN.

Family and domain databases

Gene3D3.40.1550.10. 1 hit.
InterProIPR007597. CheC.
IPR028976. CheC-like_dom.
[Graphical view]
PfamPF04509. CheC. 2 hits.
[Graphical view]
SUPFAMSSF103039. SSF103039. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ9X006.

Entry information

Entry nameCHEC_THEMA
AccessionPrimary (citable) accession number: Q9X006
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references