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Q39WQ9 (CHEB1_GEOMG) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Chemotaxis response regulator protein-glutamate methylesterase 1

EC=3.1.1.61
Gene names
Name:cheB1
Ordered Locus Names:Gmet_1075
OrganismGeobacter metallireducens (strain GS-15 / ATCC 53774 / DSM 7210) [Complete proteome] [HAMAP]
Taxonomic identifier269799 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesGeobacteraceaeGeobacter

Protein attributes

Sequence length363 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Involved in the modulation of the chemotaxis system; catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins) by CheR By similarity. HAMAP MF_00099

Catalytic activity

Protein L-glutamate O(5)-methyl ester + H2O = protein L-glutamate + methanol. HAMAP MF_00099

Subcellular location

Cytoplasm HAMAP MF_00099.

Domain

The N-terminal regulatory domain inhibits the activity of the C-terminal effector domain. HAMAP MF_00099

Post-translational modification

Phosphorylated by CheA. Phosphorylation suppresses the inhibitory activity of the N-terminal domain By similarity. HAMAP MF_00099

Sequence similarities

Contains 1 cheB-type methylesterase domain.

Contains 1 response regulatory domain.

Ontologies

Keywords
   Biological processChemotaxis
   Cellular componentCytoplasm
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processchemotaxis

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of transcription, DNA-dependent

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionprotein-glutamate methylesterase activity

Inferred from electronic annotation. Source: EC

two-component response regulator activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 363363Chemotaxis response regulator protein-glutamate methylesterase 1 HAMAP MF_00099
PRO_0000264276

Regions

Domain7 – 124118Response regulatory
Domain164 – 356193CheB-type methylesterase

Sites

Active site1761 By similarity
Active site2021 By similarity
Active site2981 By similarity

Amino acid modifications

Modified residue5814-aspartylphosphate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q39WQ9 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: 5C8D858CA230EB40

FASTA36339,686
        10         20         30         40         50         60 
MSTQPIKVLI VDDSALIRSL LTDIINSQTD MEVVGVAPDP LVAREKIKAL NPDVLTLDVE 

        70         80         90        100        110        120 
MPRMDGLVFL EKLMRLRPMP VLMVSSLTEK SSFLTLRALE LGAVDFVTKP KIDISRGMQE 

       130        140        150        160        170        180 
YAREITDKLR VAAKARVRQP PHVHLSVERK NTADAVLPME HRTFSSTEKI IVIGASTGGT 

       190        200        210        220        230        240 
EALKSFLVAM PADSPGILIT QHMPEAFTRT FAQRLNSLCR ISVKEAEHGE RILPGHAYVA 

       250        260        270        280        290        300 
PGNRHLLLAR SGANYVVELS DGPPVSRHRP SVDVLFRSAA NRAGRNAVGI IMTGMGDDGA 

       310        320        330        340        350        360 
AGMLEMREAG AYTFAQDEKS CVVFGMPKEA IARGGVDEVA PLGEMPRRLF GWLESQGNRA 


FRV 

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References

[1]"Complete sequence of Geobacter metallireducens GS-15."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GS-15 / ATCC 53774 / DSM 7210.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000148 Genomic DNA. Translation: ABB31315.1.
RefSeqYP_384040.1. NC_007517.1.

3D structure databases

ProteinModelPortalQ39WQ9.
SMRQ39WQ9. Positions 6-351.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ39WQ9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3741282.
GenomeReviewsGene locus Gmet_1075 in contig CP000148_GR.
KEGGgme:Gmet_1075.
NMPDRfig|269799.3.peg.1459.
PATRIC22001344. VBIGeoMet55070_1112.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2201.
HOGENOMHBG705324.
OMAFVTKPKL.
PhylomeDBQ39WQ9.
ProtClustDBPRK00742.

Enzyme and pathway databases

BioCycGMET269799:GMET_1075-MONOMER.

Family and domain databases

HAMAPMF_00099. CheB_methylest.
[Tree]
InterProIPR011006. CheY-like_superfamily.
IPR008248. Sig_transdc_resp-reg_CheB.
IPR000673. Sig_transdc_resp-reg_Me-estase.
IPR001789. Sig_transdc_resp-reg_receiver.
[Graphical view]
Gene3DG3DSA:3.40.50.180. Chemotax_RR_pGlu_Me-esterase. 1 hit.
KOK03412.
PfamPF01339. CheB_methylest. 1 hit.
PF00072. Response_reg. 1 hit.
[Graphical view]
PIRSFPIRSF000876. RR_chemtxs_CheB. 1 hit.
SMARTSM00448. REC. 1 hit.
[Graphical view]
SUPFAMSSF52738. Chemotax_RR_pGlu_Me-esterase. 1 hit.
SSF52172. CheY_like. 1 hit.
PROSITEPS50122. CHEB. 1 hit.
PS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCHEB1_GEOMG
AccessionPrimary (citable) accession number: Q39WQ9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: November 22, 2005
Last modified: January 25, 2012
This is version 51 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