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Reviewed, UniProtKB/Swiss-Prot Q62G12 (CHEB1_BURMA)

Last modified November 3, 2009. Version 38. 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: BMA2854
OrganismBurkholderia mallei (Pseudomonas mallei) [Complete proteome] [HAMAP]
Taxonomic identifier13373 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group

Protein attributes

Sequence length364 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 – 364364Chemotaxis response regulator protein-glutamate methylesterase 1 HAMAP MF_00099
PRO_0000225443

Regions

Domain6 – 123118Response regulatory
Domain165 – 357193CheB-type methylesterase

Sites

Active site1771 By similarity
Active site2031 By similarity
Active site2991 By similarity

Amino acid modifications

Modified residue5714-aspartylphosphate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q62G12-1 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: 576F62E7C17085C5

FASTA36439,068
        10         20         30         40         50         60 
MQKKIKVLCV DDSALIRSLM TEIINSQPDM EVCATAPDPL VARELIKQHN PDVLTLDVEM 

        70         80         90        100        110        120 
PRMDGLDFLE KLMRLRPMPV VMVSSLTERG SEITLRALEL GAVDFVTKPR VGIRDGMLDY 

       130        140        150        160        170        180 
SEKLADKVRA ASRARVRQNP QPHAAAAAAA HGHAGAAAPL INNPLVSTEK LIIVGASTGG 

       190        200        210        220        230        240 
TEAIREVLTP LPPDAPAVLI AQHMPPGFTR SFAQRLNGLC RISVKEAEHG ERVLPGHAYI 

       250        260        270        280        290        300 
APGHAHLLLA RSGANYIAHL SDEPPVNRHR PSVDVLFRSA AQHAGKNALG VILTGMGRDG 

       310        320        330        340        350        360 
AAGLLEMKKA GAYTFAQDEA SCVVFGMPRE AIAMGGVDDV APLSDMSRRI MARLASMGDR 


VQRV 

« Hide

Cross-references

Sequence databases

CP000010 Genomic DNA. Translation: AAU48333.1.
RefSeqYP_104365.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3088424.
GenomeReviewsGene locus BMA2854 in contig CP000010_GR.
KEGGbma:BMA2854.
TIGRBMA2854.

Phylogenomic databases

HOGENOMQ62G12.
OMAIVIAQHI.

Enzyme and pathway databases

BioCycBMAL243160:BMA_2854-MON.
BRENDA3.1.1.61. 260531.

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_BURMA
AccessionPrimary (citable) accession number: Q62G12
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: October 25, 2004
Last modified: November 3, 2009
This is version 38 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