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Protein

Chemoreceptor glutamine deamidase CheD

Gene

cheD

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.

Catalytic activityi

Protein L-glutamine + H2O = protein L-glutamate + NH3.
Protein L-glutamate O(5)-methyl ester + H2O = protein L-glutamate + methanol.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei27 – 271Nucleophile

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Chemotaxis

Names & Taxonomyi

Protein namesi
Recommended name:
Chemoreceptor glutamine deamidase CheD (EC:3.5.1.44)
Alternative name(s):
Chemoreceptor glutamate methylesterase CheD (EC:3.1.1.61)
Gene namesi
Name:cheD
Ordered Locus Names:TM_0903
OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Taxonomic identifieri243274 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
ProteomesiUP000008183 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi21 – 211T → A: 6-fold reduction in activity. 1 Publication
Mutagenesisi26 – 261S → A or H: Loss of activity. 1 Publication
Mutagenesisi26 – 261S → N: Reduced activity. 1 Publication
Mutagenesisi27 – 271C → A: Loss of activity. Does not prevent binding to mcp2. 1 Publication
Mutagenesisi27 – 271C → H or N: Loss of activity. 1 Publication
Mutagenesisi44 – 441H → A: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 157157Chemoreceptor glutamine deamidase CheDPRO_0000251072Add
BLAST

Interactioni

Subunit structurei

Heterodimer with CheC. The CheC-CheD heterodimer interacts with phosphorylated CheY.1 Publication

Protein-protein interaction databases

STRINGi243274.TM0903.

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 43Combined sources
Beta strandi10 – 145Combined sources
Beta strandi18 – 269Combined sources
Beta strandi28 – 347Combined sources
Turni35 – 384Combined sources
Beta strandi39 – 457Combined sources
Helixi57 – 593Combined sources
Helixi61 – 7313Combined sources
Turni74 – 763Combined sources
Helixi79 – 813Combined sources
Beta strandi83 – 886Combined sources
Helixi100 – 11415Combined sources
Beta strandi119 – 1246Combined sources
Beta strandi130 – 1356Combined sources
Turni136 – 1394Combined sources
Beta strandi140 – 1445Combined sources
Beta strandi154 – 1574Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2F9ZX-ray2.40C/D1-157[»]
ProteinModelPortaliQ9X005.
SMRiQ9X005. Positions 1-157.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9X005.

Family & Domainsi

Sequence similaritiesi

Belongs to the CheD family.Curated

Phylogenomic databases

eggNOGiCOG1871.
InParanoidiQ9X005.
KOiK03411.
OMAiAGGSDML.
OrthoDBiEOG6WHNQB.

Family and domain databases

HAMAPiMF_01440. CheD.
InterProiIPR005659. Chemorcpt_Glu_NH3ase_CheD.
IPR011324. Cytotoxic_necrot_fac-like_cat.
[Graphical view]
PfamiPF03975. CheD. 1 hit.
[Graphical view]
SUPFAMiSSF64438. SSF64438. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9X005-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKVIGIGEY AVMKNPGVIV TLGLGSCVAV CMRDPVAKVG AMAHVMLPDS
60 70 80 90 100
GGKTDKPGKY ADTAVKTLVE ELKKMGAKVE RLEAKIAGGA SMFESKGMNI
110 120 130 140 150
GARNVEAVKK HLKDFGIKLL AEDTGGNRAR SVEYNIETGK LLVRKVGGGE

QLEIKEI
Length:157
Mass (Da):16,657
Last modified:November 1, 1999 - v1
Checksum:iE5B03D96D2DDEDBE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD35984.1.
PIRiF72318.
RefSeqiNP_228711.1. NC_000853.1.
WP_004080666.1. NZ_CP011107.1.

Genome annotation databases

EnsemblBacteriaiAAD35984; AAD35984; TM_0903.
GeneIDi898577.
KEGGitma:TM0903.
tmi:THEMA_00120.
tmm:Tmari_0905.
PATRICi23936737. VBITheMar51294_0917.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD35984.1.
PIRiF72318.
RefSeqiNP_228711.1. NC_000853.1.
WP_004080666.1. NZ_CP011107.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2F9ZX-ray2.40C/D1-157[»]
ProteinModelPortaliQ9X005.
SMRiQ9X005. Positions 1-157.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243274.TM0903.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD35984; AAD35984; TM_0903.
GeneIDi898577.
KEGGitma:TM0903.
tmi:THEMA_00120.
tmm:Tmari_0905.
PATRICi23936737. VBITheMar51294_0917.

Phylogenomic databases

eggNOGiCOG1871.
InParanoidiQ9X005.
KOiK03411.
OMAiAGGSDML.
OrthoDBiEOG6WHNQB.

Miscellaneous databases

EvolutionaryTraceiQ9X005.

Family and domain databases

HAMAPiMF_01440. CheD.
InterProiIPR005659. Chemorcpt_Glu_NH3ase_CheD.
IPR011324. Cytotoxic_necrot_fac-like_cat.
[Graphical view]
PfamiPF03975. CheD. 1 hit.
[Graphical view]
SUPFAMiSSF64438. SSF64438. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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.

Entry informationi

Entry nameiCHED_THEMA
AccessioniPrimary (citable) accession number: Q9X005
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: November 1, 1999
Last modified: July 22, 2015
This is version 81 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.