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Q9X006

- CHEC_THEMA

UniProt

Q9X006 - CHEC_THEMA

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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: 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.1 Publication

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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9X006.

Family & Domainsi

Sequence similaritiesi

Belongs to the CheC family.Curated

Phylogenomic databases

eggNOGiCOG1776.
InParanoidiQ9X006.
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

        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:
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.
GeneIDi18091879.
898578.
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 18091879.
898578.
KEGGi tma:TM0904.
tmi:THEMA_00115.
tmm:Tmari_0906.
PATRICi 23936739. VBITheMar51294_0918.

Phylogenomic databases

eggNOGi COG1776.
InParanoidi Q9X006.
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: October 29, 2014
This is version 69 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