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Reviewed, UniProtKB/Swiss-Prot Q394I6 (CHEB1_BURS3)

Last modified November 3, 2009. Version 30. 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 1
    EC=3.1.1.61
Gene names
Name: cheB1
Ordered Locus Names: Bcep18194_B2017
OrganismBurkholderia sp. (strain 383) (Burkholderia cepacia (strain ATCC 17760 / NCIB 9086 / R18194)) [Complete proteome] [HAMAP]
Taxonomic identifier269483 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

Protein attributes

Sequence length334 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 – 334334Chemotaxis response regulator protein-glutamate methylesterase 1 HAMAP MF_00099
PRO_0000225449

Regions

Domain2 – 120119Response regulatory
Domain145 – 334190CheB-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
Q394I6-1 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: 75A9209A9F46423E

FASTA33434,802
        10         20         30         40         50         60 
MNIGIVNDLP LAVEAMRRAI ARRPEHRVLW VATDGAQAVE LCAAQPPDVV LMDLIMPKFD 

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

       130        140        150        160        170        180 
LAKIDQIGRL LDAPGGTRLA GTAARAGGGP LIAIGASAGG PGALASILGG LPADFSAPIV 

       190        200        210        220        230        240 
IVQHVDRAFA EGMAQWLDGQ TPLAVRVARE 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 sp. 383."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000152 Genomic DNA. Translation: ABB12130.1.
RefSeqYP_372774.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ394I6.

Genome annotation databases

GeneID3753782.
GenomeReviewsGene locus Bcep18194_B2017 in contig CP000152_GR.
KEGGbur:Bcep18194_B2017.
NMPDRfig|269483.3.peg.2024.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ394I6.
OMARPCAILI.

Enzyme and pathway databases

BioCycBSP36773:BCEP18194_B2017-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 nameCHEB1_BURS3
AccessionPrimary (citable) accession number: Q394I6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: November 22, 2005
Last modified: November 3, 2009
This is version 30 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