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Q9X006

- CHEC_THEMA

UniProt

Q9X006 - CHEC_THEMA

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Protein

CheY-P phosphatase CheC

Gene
cheC, TM_0904
Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed - 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

  1. hydrolase activity Source: UniProtKB-KW

GO - Biological processi

  1. chemotaxis Source: UniProtKB-KW
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
ProteomesiUP000008183: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi13 – 131E → 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 Publication
Mutagenesisi16 – 161N → 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 Publication
Mutagenesisi112 – 1121E → 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 Publication
Mutagenesisi115 – 1151N → 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 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 205205CheY-P phosphatase CheCPRO_0000250997Add
BLAST

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.

Protein-protein interaction databases

STRINGi243274.TM0904.

Structurei

Secondary structure

1
205
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 3026
Beta strandi34 – 374
Beta strandi41 – 455
Helixi46 – 527
Beta strandi59 – 7113
Beta strandi73 – 797
Helixi81 – 9212
Helixi104 – 12926
Beta strandi133 – 1353
Beta strandi139 – 1446
Helixi145 – 15713
Beta strandi164 – 17411
Beta strandi177 – 1793
Beta strandi181 – 1899
Helixi193 – 1997

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XKRX-ray1.75A1-205[»]
2F9ZX-ray2.40A/B1-205[»]
ProteinModelPortaliQ9X006.
SMRiQ9X006. Positions 1-204.

Miscellaneous databases

EvolutionaryTraceiQ9X006.

Family & Domainsi

Sequence similaritiesi

Belongs to the CheC family.

Phylogenomic databases

eggNOGiCOG1776.
KOiK03410.
OMAiAPGNMFF.
OrthoDBiEOG6ZPSZN.

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

MKISERQKDL LKEIGNIGAG NAATAISYMI NKKVEISVPN VEIVPISKVI    50
FIAKDPEEIV VGVKMPVTGD IEGSVLLIMG TTVVKKILEI LTGRAPDNLL 100
NLDEFSASAL REIGNIMCGT YVSALADFLG FKIDTLPPQL VIDMISAIFA 150
EASIEELEDN SEDQIVFVET LLKVEEEEEP LTSYMMMIPK PGYLVKIFER 200
MGIQE 205
Length:205
Mass (Da):22,549
Last modified:November 1, 1999 - v1
Checksum:i0FF88D0E26A927B7
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE000512 Genomic DNA. Translation: AAD35985.1.
PIRiG72318.
RefSeqiNP_228712.1. NC_000853.1.
YP_007977256.1. NC_021214.1.
YP_008990126.1. NC_023151.1.

Genome annotation databases

EnsemblBacteriaiAAD35985; AAD35985; TM_0904.
GeneIDi898578.
KEGGitma:TM0904.
tmi:THEMA_00115.
tmm:Tmari_0906.
PATRICi23936739. VBITheMar51294_0918.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE000512 Genomic DNA. Translation: AAD35985.1 .
PIRi G72318.
RefSeqi NP_228712.1. NC_000853.1.
YP_007977256.1. NC_021214.1.
YP_008990126.1. NC_023151.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1XKR X-ray 1.75 A 1-205 [» ]
2F9Z X-ray 2.40 A/B 1-205 [» ]
ProteinModelPortali Q9X006.
SMRi Q9X006. Positions 1-204.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 243274.TM0904.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAD35985 ; AAD35985 ; TM_0904 .
GeneIDi 898578.
KEGGi tma:TM0904.
tmi:THEMA_00115.
tmm:Tmari_0906.
PATRICi 23936739. VBITheMar51294_0918.

Phylogenomic databases

eggNOGi COG1776.
KOi K03410.
OMAi APGNMFF.
OrthoDBi EOG6ZPSZN.

Miscellaneous databases

EvolutionaryTracei Q9X006.

Family and domain databases

Gene3Di 3.40.1550.10. 1 hit.
InterProi IPR007597. CheC.
IPR028976. CheC-like_dom.
[Graphical view ]
Pfami PF04509. CheC. 2 hits.
[Graphical view ]
SUPFAMi SSF103039. SSF103039. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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.

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: July 9, 2014
This is version 67 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

External Data

Dasty 3

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