Q9X006 (CHEC_THEMA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
CheY-P phosphatase CheC
EC=3.-.-.-

Gene names

Name:	cheC
Ordered Locus Names:	TM_0904

Organism

Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) [Reference proteome] [HAMAP]

Taxonomic identifier

243274 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Thermotogae › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga › Thermotoga maritima

Protein attributes

Sequence length	205 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Chemotaxis
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	chemotaxis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	hydrolase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 205

205

CheY-P phosphatase CheC

PRO_0000250997

Experimental info

Mutagenesis

13

1

E → 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

Mutagenesis

16

1

N → 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

Mutagenesis

112

1

E → 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

Mutagenesis

115

1

N → 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

1

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205

Helix Strand Turn

Details...

Helix

5 – 30

26

Beta strand

34 – 37

4

Beta strand

41 – 45

5

Helix

46 – 52

7

Beta strand

59 – 71

13

Beta strand

73 – 79

7

Helix

81 – 92

12

Helix

104 – 129

26

Beta strand

133 – 135

3

Beta strand

139 – 144

6

Helix

145 – 157

13

Beta strand

164 – 174

11

Beta strand

177 – 179

3

Beta strand

181 – 189

9

Helix

193 – 199

7

Sequences

	Sequence		Length	Mass (Da)
	Q9X006 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 0FF88D0E26A927B7	FASTA	205	22,549
	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

References

	« Hide 'large scale' referencesShow '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. , 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.

PIR

G72318.

RefSeq

NP_228712.1. NC_000853.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1XKR	X-ray	1.75	A	1-205	[»]
2F9Z	X-ray	2.40	A/B	1-205	[»]

ProteinModelPortal

Q9X006.

SMR

Q9X006. Positions 1-204.

ModBase

Search...

Protein-protein interaction databases

STRING

243274.TM0904.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAD35985; AAD35985; TM_0904.

GeneID

898578.

KEGG

tma:TM0904.

PATRIC

23936739. VBITheMar51294_0918.

Phylogenomic databases

eggNOG

COG1776.

KO

K03410.

OMA

PALAIDM.

ProtClustDB

CLSK875461.

Family and domain databases

InterPro

IPR007597. CheC.
[Graphical view]

Pfam

PF04509. CheC. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9X006.

Entry information

Entry name

CHEC_THEMA

Accession

Primary (citable) accession number: Q9X006

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2006
Last sequence update:	November 1, 1999
Last modified:	May 1, 2013
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program