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Q9X005

- CHED_THEMA

UniProt

Q9X005 - CHED_THEMA

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Protein

Chemoreceptor glutamine deamidase CheD

Gene
cheD, TM_0903
Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed - Annotation score: 5 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.UniRule annotation

Catalytic activityi

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

Sites

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

GO - Molecular functioni

  1. protein-glutamate methylesterase activity Source: UniProtKB-EC
  2. protein-glutamine glutaminase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. chemotaxis Source: UniProtKB-HAMAP
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: 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 CheDUniRule annotationPRO_0000251072Add
BLAST

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi243274.TM0903.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2F9ZX-ray2.40C/D1-157[»]
ProteinModelPortaliQ9X005.
SMRiQ9X005. Positions 1-157.

Miscellaneous databases

EvolutionaryTraceiQ9X005.

Family & Domainsi

Sequence similaritiesi

Belongs to the CheD family.

Phylogenomic databases

eggNOGiCOG1871.
KOiK03411.
OMAiIGMIHIM.
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

MKKVIGIGEY AVMKNPGVIV TLGLGSCVAV CMRDPVAKVG AMAHVMLPDS    50
GGKTDKPGKY ADTAVKTLVE ELKKMGAKVE RLEAKIAGGA SMFESKGMNI 100
GARNVEAVKK HLKDFGIKLL AEDTGGNRAR SVEYNIETGK LLVRKVGGGE 150
QLEIKEI 157
Length:157
Mass (Da):16,657
Last modified:November 1, 1999 - v1
Checksum:iE5B03D96D2DDEDBE
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE000512 Genomic DNA. Translation: AAD35984.1.
PIRiF72318.
RefSeqiNP_228711.1. NC_000853.1.
YP_007977255.1. NC_021214.1.
YP_008990127.1. NC_023151.1.

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:
EMBL
GenBank
DDBJ
Links Updated
AE000512 Genomic DNA. Translation: AAD35984.1 .
PIRi F72318.
RefSeqi NP_228711.1. NC_000853.1.
YP_007977255.1. NC_021214.1.
YP_008990127.1. NC_023151.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2F9Z X-ray 2.40 C/D 1-157 [» ]
ProteinModelPortali Q9X005.
SMRi Q9X005. Positions 1-157.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 243274.TM0903.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAD35984 ; AAD35984 ; TM_0903 .
GeneIDi 898577.
KEGGi tma:TM0903.
tmi:THEMA_00120.
tmm:Tmari_0905.
PATRICi 23936737. VBITheMar51294_0917.

Phylogenomic databases

eggNOGi COG1871.
KOi K03411.
OMAi IGMIHIM.
OrthoDBi EOG6WHNQB.

Miscellaneous databases

EvolutionaryTracei Q9X005.

Family and domain databases

HAMAPi MF_01440. CheD.
InterProi IPR005659. Chemorcpt_Glu_NH3ase_CheD.
IPR011324. Cytotoxic_necrot_fac-like_cat.
[Graphical view ]
Pfami PF03975. CheD. 1 hit.
[Graphical view ]
SUPFAMi SSF64438. SSF64438. 1 hit.
ProtoNeti Search...

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 9, 2014
This is version 72 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

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