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Q1BMF9 (CHEB2_BURCA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 39. 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 2

EC=3.1.1.61
Gene names
Name:cheB2
Ordered Locus Names:Bcen_4310
OrganismBurkholderia cenocepacia (strain AU 1054) [Complete proteome] [HAMAP]
Taxonomic identifier331271 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

Protein attributes

Sequence length334 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 – 334334Chemotaxis response regulator protein-glutamate methylesterase 2 HAMAP MF_00099
PRO_0000264265

Regions

Domain2 – 120119Response regulatory
Domain134 – 334201CheB-type methylesterase

Sites

Active site1571 By similarity
Active site1841 By similarity
Active site2771 By similarity

Amino acid modifications

Modified residue5314-aspartylphosphate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1BMF9 [UniParc].

Last modified July 11, 2006. Version 1.
Checksum: BD6430F17EB27BD8

FASTA33434,982
        10         20         30         40         50         60 
MNIGIVNDLP LAVEAMRRAI ARRPEHRVLW VATDGPQAVE LCAAQPPDIV LMDLIMPKFD 

        70         80         90        100        110        120 
GIEATRRIMR PERPCAILIV TSCIGANAWR VFEAMGAGAL DAVDTPRLGD GAAGDTTKLL 

       130        140        150        160        170        180 
LAKIDQIGRL LDAPGSSRLA GAAARGGAGP LIAIGASAGG PGALASILGN LPADFNAPIV 

       190        200        210        220        230        240 
IVQHVDRAFA EGMAQWLDGQ TRLAVRVARE GDRPQPGVAL LAATDDHLRI TRAGTLEYTR 

       250        260        270        280        290        300 
EPAATPYRPS VDVFFNSLTE HWPGRVIGVL LTGMGRDGAI GLKALRMKGY HTIAQDEATS 

       310        320        330 
AVYGMPKAAA TLGAARAILP LGRIAGELAA LARI 

« Hide

References

[1]"Complete sequence of chromosome 2 of Burkholderia cenocepacia AU 1054."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Lykidis A., LiPuma J.J., Konstantinidis K., Tiedje J.M., Richardson P.
Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AU 1054.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000379 Genomic DNA. Translation: ABF79196.1.
RefSeqYP_624169.1. NC_008061.1.

3D structure databases

ProteinModelPortalQ1BMF9.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1BMF9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4094897.
GenomeReviewsGene locus Bcen_4310 in contig CP000379_GR.
KEGGbcn:Bcen_4310.
PATRIC19052566. VBIBurCen11237_4492.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2201.
HOGENOMHBG705324.
OMARPCAILI.
ProtClustDBPRK12555.

Enzyme and pathway databases

BioCycBCEN331271:BCEN_4310-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 nameCHEB2_BURCA
AccessionPrimary (citable) accession number: Q1BMF9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: July 11, 2006
Last modified: January 25, 2012
This is version 39 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