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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)DescriptionActionsGraphical viewLength
Active sitei27Nucleophile1

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
Proteomesi
  • UP000008183 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi21T → A: 6-fold reduction in activity. 1 Publication1
Mutagenesisi26S → A or H: Loss of activity. 1 Publication1
Mutagenesisi26S → N: Reduced activity. 1 Publication1
Mutagenesisi27C → A: Loss of activity. Does not prevent binding to mcp2. 1 Publication1
Mutagenesisi27C → H or N: Loss of activity. 1 Publication1
Mutagenesisi44H → A: Loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002510721 – 157Chemoreceptor glutamine deamidase CheDAdd BLAST157

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

1157
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 4Combined sources3
Beta strandi10 – 14Combined sources5
Beta strandi18 – 26Combined sources9
Beta strandi28 – 34Combined sources7
Turni35 – 38Combined sources4
Beta strandi39 – 45Combined sources7
Helixi57 – 59Combined sources3
Helixi61 – 73Combined sources13
Turni74 – 76Combined sources3
Helixi79 – 81Combined sources3
Beta strandi83 – 88Combined sources6
Helixi100 – 114Combined sources15
Beta strandi119 – 124Combined sources6
Beta strandi130 – 135Combined sources6
Turni136 – 139Combined sources4
Beta strandi140 – 144Combined sources5
Beta strandi154 – 157Combined sources4

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ9X005.

Family & Domainsi

Sequence similaritiesi

Belongs to the CheD family.Curated

Phylogenomic databases

eggNOGiENOG4108Z4W. Bacteria.
COG1871. LUCA.
InParanoidiQ9X005.
KOiK03411.
OMAiKVRMRKV.

Family and domain databases

HAMAPiMF_01440. CheD. 1 hit.
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.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2F9ZX-ray2.40C/D1-157[»]
ProteinModelPortaliQ9X005.
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.
PATRICi23936737. VBITheMar51294_0917.

Phylogenomic databases

eggNOGiENOG4108Z4W. Bacteria.
COG1871. LUCA.
InParanoidiQ9X005.
KOiK03411.
OMAiKVRMRKV.

Miscellaneous databases

EvolutionaryTraceiQ9X005.

Family and domain databases

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

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: October 5, 2016
This is version 88 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

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 one 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.