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Q9X005 (CHED_THEMA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 72. 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:
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
OrganismThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) [Reference proteome] [HAMAP]
Taxonomic identifier243274 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga

Protein attributes

Sequence length157 AA.
Sequence statusComplete.
Protein existenceEvidence 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 processChemotaxis
   Molecular functionHydrolase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processchemotaxis

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functionprotein-glutamate methylesterase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein-glutamine glutaminase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 157157Chemoreceptor glutamine deamidase CheD HAMAP-Rule MF_01440
PRO_0000251072

Sites

Active site271Nucleophile

Experimental info

Mutagenesis211T → A: 6-fold reduction in activity. Ref.2
Mutagenesis261S → A or H: Loss of activity. Ref.2
Mutagenesis261S → N: Reduced activity. Ref.2
Mutagenesis271C → A: Loss of activity. Does not prevent binding to mcp2. Ref.2
Mutagenesis271C → H or N: Loss of activity. Ref.2
Mutagenesis441H → A: Loss of activity. Ref.2

Secondary structure

............................. 157
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9X005 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: E5B03D96D2DDEDBE

FASTA15716,657
        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 

« 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]"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.
PIRF72318.
RefSeqNP_228711.1. NC_000853.1.
YP_007977255.1. NC_021214.1.
YP_008990127.1. NC_023151.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2F9ZX-ray2.40C/D1-157[»]
ProteinModelPortalQ9X005.
SMRQ9X005. Positions 1-157.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243274.TM0903.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD35984; AAD35984; TM_0903.
GeneID898577.
KEGGtma:TM0903.
tmi:THEMA_00120.
tmm:Tmari_0905.
PATRIC23936737. VBITheMar51294_0917.

Phylogenomic databases

eggNOGCOG1871.
KOK03411.
OMAIGMIHIM.
OrthoDBEOG6WHNQB.

Family and domain databases

HAMAPMF_01440. CheD.
InterProIPR005659. Chemorcpt_Glu_NH3ase_CheD.
IPR011324. Cytotoxic_necrot_fac-like_cat.
[Graphical view]
PfamPF03975. CheD. 1 hit.
[Graphical view]
SUPFAMSSF64438. SSF64438. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ9X005.

Entry information

Entry nameCHED_THEMA
AccessionPrimary (citable) accession number: Q9X005
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 72 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