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Reviewed, UniProtKB/Swiss-Prot Q3JJY2 (CHEB2_BURP1)

Last modified November 3, 2009. Version 28. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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: BURPS1710b_A0963
OrganismBurkholderia pseudomallei (strain 1710b) [Complete proteome] [HAMAP]
Taxonomic identifier320372 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group

Protein attributes

Sequence length342 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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.

Sequence similarities

Contains 1 cheB-type methylesterase domain.

Contains 1 response regulatory domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 342342Chemotaxis response regulator protein-glutamate methylesterase 2 HAMAP MF_00099
PRO_0000225448

Regions

Domain2 – 119118Response regulatory
Domain144 – 337194CheB-type methylesterase

Sites

Active site1591 By similarity
Active site1861 By similarity
Active site2791 By similarity

Amino acid modifications

Modified residue5314-aspartylphosphate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3JJY2-1 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: E7BA20EC1E01B7DB

FASTA34236,134
        10         20         30         40         50         60 
MNIGIVNDLP LAVEALRRTI ALRPEHRVLW VATDGAQALD FCVAQPPDLV LMDLVMPRID 

        70         80         90        100        110        120 
GVSATRSIME RSPCAILIVT ANVGANASYV YEAMGAGALD AVDTPTLEQG GSADPSQPLL 

       130        140        150        160        170        180 
AKIDQIGRLL ATRMPLAAPA AAAPAPQGAL PPLVAIGASA GGPTALTALL RRLPDDFPAA 

       190        200        210        220        230        240 
LVIVQHVDQA FAIGMAQWLD GYSPLPVRIA RQGSVPQAGE VLLAATNDHL HLTSRGVLAY 

       250        260        270        280        290        300 
TRRPEETPYR PSVDVFFHSV VDHWKGEAIG VLLTGMGRDG ALGLKAMRTK GHYTIAQDEA 

       310        320        330        340 
TSAVYGMPKA AAAIGAASAV LPLERIADQL ISLVQRNRQR WR 

« Hide

References

[1]Woods D.E., Nierman W.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000125 Genomic DNA. Translation: ABA51495.1.
RefSeqYP_336121.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ3JJY2.

Genome annotation databases

GeneID3693886.
GenomeReviewsGene locus BURPS1710b_A0963 in contig CP000125_GR.
KEGGbpm:BURPS1710b_A0963.
TIGRBURPS1710b_A0963.

Phylogenomic databases

HOGENOMQ3JJY2.
OMAEAMGHGA.

Enzyme and pathway databases

BioCycBPSE320372:BURPS1710B_B1128-MON.

Family and domain databases

HAMAPMF_00099.
[Tree]
InterProIPR008248. 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.
PfamPF01339. CheB_methylest. 1 hit.
PF00072. Response_reg. 1 hit.
[Graphical view]
PIRSFPIRSF000876. RR_chemtxs_CheB. 1 hit.
ProDomPD005328. CheB_methylest. 1 hit.
PD000039. Response_reg. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00448. REC. 1 hit.
[Graphical view]
PROSITEPS50122. CHEB. 1 hit.
PS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCHEB2_BURP1
AccessionPrimary (citable) accession number: Q3JJY2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: November 8, 2005
Last modified: November 3, 2009
This is version 28 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents