Q9X005 (CHED_THEMA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Chemoreceptor glutamine deamidase CheD
EC=3.5.1.44

Alternative name(s):
Chemoreceptor glutamate methylesterase CheD
EC=3.1.1.61

Gene names

Name:	cheD
Ordered Locus Names:	TM_0903

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	157 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Deamidates glutamine residues on chemoreceptors (MCPs). CheD-mediated MCP deamidation is required for productive communication of the conformational signals of the chemoreceptors to the CheA kinase. In addition, demethylates methylated glutamate residues on chemoreceptors Mcp2 and Mcp4. Enhances the activity of CheC. HAMAP-Rule MF_01440
Catalytic activity	Protein L-glutamine + H2O = protein L-glutamate + NH3. HAMAP-Rule MF_01440 Protein L-glutamate O(5)-methyl ester + H2O = protein L-glutamate + methanol. HAMAP-Rule MF_01440
Subunit structure	Heterodimer with CheC. The CheC-CheD heterodimer interacts with phosphorylated CheY.
Sequence similarities	Belongs to the CheD 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: HAMAP
Molecular_function	protein-glutamate methylesterase activity Inferred from electronic annotation. Source: EC protein-glutamine glutaminase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 157

157

Chemoreceptor glutamine deamidase CheD HAMAP-Rule MF_01440

PRO_0000251072

Sites

Active site

27

1

Nucleophile

Experimental info

Mutagenesis

21

1

T → A: 6-fold reduction in activity. Ref.2

Mutagenesis

26

1

S → A or H: Loss of activity. Ref.2

Mutagenesis

26

1

S → N: Reduced activity. Ref.2

Mutagenesis

27

1

C → A: Loss of activity. Does not prevent binding to mcp2. Ref.2

Mutagenesis

27

1

C → H or N: Loss of activity. Ref.2

Mutagenesis

44

1

H → A: Loss of activity. Ref.2

Secondary structure

1

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157

Helix Strand Turn

Details...

Beta strand

2 – 4

3

Beta strand

10 – 14

5

Beta strand

18 – 26

9

Beta strand

28 – 34

7

Turn

35 – 38

4

Beta strand

39 – 45

7

Helix

57 – 59

3

Helix

61 – 73

13

Turn

74 – 76

3

Helix

79 – 81

3

Beta strand

83 – 88

6

Helix

100 – 114

15

Beta strand

119 – 124

6

Beta strand

130 – 135

6

Turn

136 – 139

4

Beta strand

140 – 144

5

Beta strand

154 – 157

4

Sequences

	Sequence		Length	Mass (Da)
	Q9X005 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: E5B03D96D2DDEDBE	FASTA	157	16,657
	10 20 30 40 50 60 MKKVIGIGEY AVMKNPGVIV TLGLGSCVAV CMRDPVAKVG AMAHVMLPDS GGKTDKPGKY 70 80 90 100 110 120 ADTAVKTLVE ELKKMGAKVE RLEAKIAGGA SMFESKGMNI GARNVEAVKK HLKDFGIKLL 130 140 150 AEDTGGNRAR SVEYNIETGK LLVRKVGGGE QLEIKEI

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]	"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 CHEC, MUTAGENESIS OF THR-21; SER-26; CYS-27 AND HIS-44.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE000512 Genomic DNA. Translation: AAD35984.1.

PIR

F72318.

RefSeq

NP_228711.1. NC_000853.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2F9Z	X-ray	2.40	C/D	1-157	[»]

ProteinModelPortal

Q9X005.

SMR

Q9X005. Positions 1-157.

ModBase

Search...

Protein-protein interaction databases

STRING

243274.TM0903.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAD35984; AAD35984; TM_0903.

GeneID

898577.

KEGG

tma:TM0903.

PATRIC

23936737. VBITheMar51294_0917.

Phylogenomic databases

eggNOG

COG1871.

KO

K03411.

OMA

IGRRNHA.

ProtClustDB

PRK13495.

Family and domain databases

HAMAP

MF_01440. CheD.

InterPro

IPR005659. Chemorcpt_Glu_NH3ase_CheD.
[Graphical view]

Pfam

PF03975. CheD. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9X005.

Entry information

Entry name

CHED_THEMA

Accession

Primary (citable) accession number: Q9X005

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2006
Last sequence update:	November 1, 1999
Last modified:	May 1, 2013
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program