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Reviewed, UniProtKB/Swiss-Prot Q2STS8 (CHEB1_BURTA)

Last modified January 19, 2010. Version 34. 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: BTH_I3177
OrganismBurkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301) [Complete proteome] [HAMAP]
Taxonomic identifier271848 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group

Protein attributes

Sequence length364 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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 364364Chemotaxis response regulator protein-glutamate methylesterase 1 HAMAP MF_00099
PRO_0000264267

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
Q2STS8-1 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: A625E0BA909A1BEB

FASTA36439,087
        10         20         30         40         50         60 
MQKKIKVLCV DDSALIRSLM TEIINSQPDM EVCATAPDPL VARELIKQHN PDVLTLDVEM 

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

       130        140        150        160        170        180 
AEKLADKVRA ASRARVRQNP QPHAAAAAAA HGQTAAAAPL INNPLVSTEK LIIVGASTGG 

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

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

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


VQRV 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000086 Genomic DNA. Translation: ABC38609.1.
RefSeqYP_443671.1.

3D structure databases

SMRQ2STS8. Positions 4-356.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2STS8.

Genome annotation databases

GeneID3847881.
GenomeReviewsGene locus BTH_I3177 in contig CP000086_GR.
KEGGbte:BTH_I3177.
TIGRBTH_I3177.

Phylogenomic databases

eggNOGCOG2201.
HOGENOMHBG705324.
OMAIINIREH.

Enzyme and pathway databases

BioCycBTHA271848:BTH_I3177-MONOMER.

Family and domain databases

HAMAPMF_00099. CheB_methylest.
[Tree]
InterProIPR011006. CheY-like.
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.
PfamPF01339. CheB_methylest. 1 hit.
PF00072. Response_reg. 1 hit.
[Graphical view]
PIRSFPIRSF000876. RR_chemtxs_CheB. 1 hit.
SMARTSM00448. REC. 1 hit.
[Graphical view]
PROSITEPS50122. CHEB. 1 hit.
PS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCHEB1_BURTA
AccessionPrimary (citable) accession number: Q2STS8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: January 24, 2006
Last modified: January 19, 2010
This is version 34 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