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Reviewed, UniProtKB/Swiss-Prot Q7NZB3 (CHEB2_CHRVO)

Last modified November 3, 2009. Version 43. 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 of group 2 operon
    EC=3.1.1.61
Gene names
Name: cheB2
Ordered Locus Names: CV_1009
OrganismChromobacterium violaceum [Complete proteome] [HAMAP]
Taxonomic identifier536 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeChromobacterium

Protein attributes

Sequence length356 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 – 356356Chemotaxis response regulator protein-glutamate methylesterase of group 2 operon HAMAP MF_00099
PRO_0000157987

Regions

Domain4 – 121118Response regulatory
Domain169 – 356188CheB-type methylesterase

Sites

Active site1811 By similarity
Active site2071 By similarity
Active site3031 By similarity

Amino acid modifications

Modified residue5514-aspartylphosphate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7NZB3-1 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: EBB79A3D8664E9FC

FASTA35637,923
        10         20         30         40         50         60 
MSIKVLIVDD SAVVRQVLSQ VFTAASGIEV MDVANDPYMA MDKMKARWPD VIVLDVEMPR 

        70         80         90        100        110        120 
MDGITFLKQL MASRPTPVVI CSSLTQKGTD ISMQAMAAGA VEVIAKPVSG VKGFLEESSH 

       130        140        150        160        170        180 
ELVMAVRSAA AARMNRVRVM PSASGNPLET RPKLSADAIL SAPTGSNVFA TTERIIAIGT 

       190        200        210        220        230        240 
STGGTQALEA VLTQLPRTCP GLAIVQHMPE KFTRSFADRL NSLSQIEVKE ADNGDRILPG 

       250        260        270        280        290        300 
RALIAPGGKH MMVKRSGAYY QVEVVDGPLV SRHKPSVDVL FRSAAKFAGK NALGIIMTGM 

       310        320        330        340        350 
GDDGAKGLKE MHDCGAKTIA QDEESCVVFG MPKEAIKLGA ADEVMPLELI AKAICR 

« Hide

References

« Hide 'large scale' references
[1]"The complete genome sequence of Chromobacterium violaceum reveals remarkable and exploitable bacterial adaptability."
Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T., Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R., Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F., Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S., Belo A. expand/collapse author list , van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M., Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R., Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J., Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F., Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M., Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.
Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003) [PubMed: 14500782] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 12472 / DSM 30191 / IFO 12614 / JCM 1249 / NCIB 9131.
[2]"Chemotaxis and flagellar genes of Chromobacterium violaceum."
Pereira M., Parente J.A., Bataus L.A.M., Cardoso D.D.P., Soares R.B.A., Soares C.M.A.
Genet. Mol. Res. 3:92-101(2004) [PubMed: 15100991] [Abstract]
Cited for: DISCUSSION OF CHEMOTAXIS GENOMIC COMPLEXITY.
Strain: ATCC 12472 / DSM 30191 / IFO 12614 / JCM 1249 / NCIB 9131.

Cross-references

Sequence databases

AE016825 Genomic DNA. Translation: AAQ58683.1.
RefSeqNP_900679.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID2550627.
GenomeReviewsGene locus CV_1009 in contig AE016825_GR.
KEGGcvi:CV_1009.
NMPDRfig|243365.1.peg.1009.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ7NZB3.
OMACAVAVKE.

Enzyme and pathway databases

BioCycCVIO243365:CV_1009-MON.
BRENDA3.1.1.61. 415.

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 nameCHEB2_CHRVO
AccessionPrimary (citable) accession number: Q7NZB3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: December 15, 2003
Last modified: November 3, 2009
This is version 43 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