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Q2WAJ8 (CHEB1_MAGSA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 50. 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 1

EC=3.1.1.61
Gene names
Name:cheB1
Ordered Locus Names:amb0323
OrganismMagnetospirillum magneticum (strain AMB-1 / ATCC 700264) [Complete proteome] [HAMAP]
Taxonomic identifier342108 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeMagnetospirillum

Protein attributes

Sequence length381 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.

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 – 381381Chemotaxis response regulator protein-glutamate methylesterase 1 HAMAP MF_00099
PRO_0000264286

Regions

Domain14 – 132119Response regulatory
Domain188 – 381194CheB-type methylesterase

Sites

Active site1991 By similarity
Active site2271 By similarity
Active site3231 By similarity

Amino acid modifications

Modified residue6514-aspartylphosphate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2WAJ8 [UniParc].

Last modified January 10, 2006. Version 1.
Checksum: BC671434000D5289

FASTA38139,765
        10         20         30         40         50         60 
MAIDSPSPAT DSIRVMLVDD SAVVRGLVTR ILEGEAGIQV VASVGNGQMA LASLERNEID 

        70         80         90        100        110        120 
VVILDIEMPV MDGLTALPKL LQIDPGLKVI MQSTLTLKGA DVSLRAMQMG AADYIPKPTS 

       130        140        150        160        170        180 
TRDLAGGVDF KSELVTKIRA LGQARRAGAR PARPGGPPAT RPVIASTSPR TPVPIHPPGP 

       190        200        210        220        230        240 
LQLRSNTPEP PDIIAIGSST GGPQALFTVL GTMKAGTVRQ PIVITQHMPA TFTTILAEHI 

       250        260        270        280        290        300 
GRVSGWEARE AQDGEAIRGG RVYIAPGDFH MVVETKGTDK VLRLNKNPPE NFCRPAVDPM 

       310        320        330        340        350        360 
LRSIAAAYGK RVLACILTGM GADGMKGGQA VVASGGTVIA QDEASSVVWG MPGAAATAGI 

       370        380 
CSAVLPLPEI APWIMKLAAR R 

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References

[1]"Complete genome sequence of the facultative anaerobic magnetotactic bacterium Magnetospirillum sp. strain AMB-1."
Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.
DNA Res. 12:157-166(2005) [PubMed: 16303747] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AMB-1 / ATCC 700264.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP007255 Genomic DNA. Translation: BAE49127.1.
RefSeqYP_419686.1. NC_007626.1.

3D structure databases

ProteinModelPortalQ2WAJ8.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2WAJ8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3806085.
GenomeReviewsGene locus amb0323 in contig AP007255_GR.
KEGGmag:amb0323.
NMPDRfig|342108.5.peg.322.
PATRIC22434916. VBIMagMag129836_0329.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2201.
HOGENOMHBG705324.
OMALISRWVE.
PhylomeDBQ2WAJ8.
ProtClustDBPRK00742.

Enzyme and pathway databases

BioCycMMAG342108:AMB0323-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 nameCHEB1_MAGSA
AccessionPrimary (citable) accession number: Q2WAJ8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: January 10, 2006
Last modified: January 25, 2012
This is version 50 of the entry and version 1 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