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Q2T8Y6 (CHEB2_BURTA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 46. 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:BTH_II0161
OrganismBurkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301) [Complete proteome] [HAMAP]
Taxonomic identifier271848 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group

Protein attributes

Sequence length354 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.

Sequence caution

The sequence ABC35113.1 differs from that shown. Reason: Erroneous initiation.

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 – 354354Chemotaxis response regulator protein-glutamate methylesterase 2 HAMAP MF_00099
PRO_0000264268

Regions

Domain3 – 120118Response regulatory
Domain164 – 354191CheB-type methylesterase

Sites

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

Amino acid modifications

Modified residue5414-aspartylphosphate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2T8Y6 [UniParc].

Last modified December 12, 2006. Version 2.
Checksum: C113B279BEF61B90

FASTA35437,092
        10         20         30         40         50         60 
MIRVVVVDDS MSMRTLLERI INGCDGMTCV GAAEDASAAR EMIRALDPDV VTLDVEMPGM 

        70         80         90        100        110        120 
DGLEFLRRMM LLKPTPTIMV SGRTTSGSDA ALRALELGAV DVIAKPLLTR PADLADYARD 

       130        140        150        160        170        180 
IAELIRGAAA ARVKGGALAA ASSAGRERAC AHRPRGAKKA GIAATRLSRV IAIGASTGGT 

       190        200        210        220        230        240 
EALRTVLQDM SGTPPPILIC QHMPEGFTAS FAARLDAICG IRVKEAEQGE PLHYGCAYVA 

       250        260        270        280        290        300 
PGHSHLSLAA TGRLYVCRLE ASPPVNRHRP SVDVLFDSVA RLAGKRALGA ILTGMGKDGA 

       310        320        330        340        350 
AGLLRMRASG ARTFAQDEPS CVVFGMPKEA IAMGAVDEIL PLARMGARLS EALQ 

« Hide

References

[1]"Bacterial genome adaptation to niches: divergence of the potential virulence genes in three Burkholderia species of different survival strategies."
Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C., DeShazer D.
BMC Genomics 6:174-174(2005) [PubMed: 16336651] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: E264 / ATCC 700388 / DSM 13276 / CIP 106301.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000085 Genomic DNA. Translation: ABC35113.1. Different initiation.
RefSeqYP_438363.1. NC_007650.1.

3D structure databases

ProteinModelPortalQ2T8Y6.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2T8Y6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3846303.
GenomeReviewsGene locus BTH_II0161 in contig CP000085_GR.
KEGGbte:BTH_II0161.
PATRIC19297690. VBIBurTha36512_0176.
TIGRBTH_II0161.

Phylogenomic databases

eggNOGCOG2201.
HOGENOMHBG705324.
ProtClustDBCLSK719951.

Enzyme and pathway databases

BioCycBTHA271848:BTH_II0161-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_BURTA
AccessionPrimary (citable) accession number: Q2T8Y6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: December 12, 2006
Last modified: January 25, 2012
This is version 46 of the entry and version 2 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