ID   CHEB2_BURMA             Reviewed;         342 AA.
AC   Q4V2X4;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   16-JUN-2009, entry version 34.
DE   RecName: Full=Chemotaxis response regulator protein-glutamate methylesterase 2;
DE            EC=3.1.1.61;
GN   Name=cheB2; OrderedLocusNames=BMAA0221.1;
OS   Burkholderia mallei (Pseudomonas mallei).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=13373;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23344;
RX   PubMed=15377793; DOI=10.1073/pnas.0403306101;
RA   Nierman W.C., DeShazer D., Kim H.S., Tettelin H., Nelson K.E.,
RA   Feldblyum T.V., Ulrich R.L., Ronning C.M., Brinkac L.M.,
RA   Daugherty S.C., Davidsen T.D., DeBoy R.T., Dimitrov G., Dodson R.J.,
RA   Durkin A.S., Gwinn M.L., Haft D.H., Khouri H.M., Kolonay J.F.,
RA   Madupu R., Mohammoud Y., Nelson W.C., Radune D., Romero C.M.,
RA   Sarria S., Selengut J., Shamblin C., Sullivan S.A., White O., Yu Y.,
RA   Zafar N., Zhou L., Fraser C.M.;
RT   "Structural flexibility in the Burkholderia mallei genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14246-14251(2004).
CC   -!- FUNCTION: Involved in the modulation of the chemotaxis system;
CC       catalyzes the demethylation of specific methylglutamate residues
CC       introduced into the chemoreceptors (methyl-accepting chemotaxis
CC       proteins) by cheR (By similarity).
CC   -!- CATALYTIC ACTIVITY: Protein L-glutamate O(5)-methyl ester + H(2)O
CC       = protein L-glutamate + methanol.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- DOMAIN: The N-terminal regulatory domain inhibits the activity of
CC       the C-terminal effector domain.
CC   -!- PTM: Phosphorylated by cheA. Phosphorylation suppresses the
CC       inhibitory activity of the N-terminal domain (By similarity).
CC   -!- SIMILARITY: Contains 1 cheB-type methylesterase domain.
CC   -!- SIMILARITY: Contains 1 response regulatory domain.
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DR   EMBL; CP000011; AAY59282.1; -; Genomic_DNA.
DR   RefSeq; YP_338317.1; -.
DR   GeneID; 3704284; -.
DR   GenomeReviews; CP000011_GR; BMAA0221.1.
DR   KEGG; bma:BMAA0221.1; -.
DR   TIGR; BMAA0221.1; -.
DR   HOGENOM; Q4V2X4; -.
DR   OMA; Q4V2X4; EAMGHGA.
DR   BioCyc; BMAL243160:BMA_A0221.1-MON; -.
DR   BRENDA; 3.1.1.61; 260531.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008984; F:protein-glutamate methylesterase activity; IEA:HAMAP.
DR   GO; GO:0000156; F:two-component response regulator activity; IEA:InterPro.
DR   GO; GO:0006935; P:chemotaxis; IEA:HAMAP.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro.
DR   GO; GO:0007606; P:sensory perception of chemical stimulus; IEA:HAMAP.
DR   GO; GO:0000160; P:two-component signal transduction system (p...; IEA:HAMAP.
DR   HAMAP; MF_00099; -; 1.
DR   InterPro; IPR008248; Sig_transdc_resp-reg_CheB.
DR   InterPro; IPR000673; Sig_transdc_resp-reg_Me-estase.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   Gene3D; G3DSA:3.40.50.180; Chemotax_RR_pGlu_Me-esterase; 1.
DR   Pfam; PF01339; CheB_methylest; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PIRSF; PIRSF000876; RR_chemtxs_CheB; 1.
DR   ProDom; PD005328; CheB_methylest; 1.
DR   ProDom; PD000039; Response_reg; 1.
DR   SMART; SM00448; REC; 1.
DR   PROSITE; PS50122; CHEB; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   3: Inferred from homology;
KW   Chemotaxis; Complete proteome; Cytoplasm; Hydrolase; Phosphoprotein.
FT   CHAIN         1    342       Chemotaxis response regulator protein-
FT                                glutamate methylesterase 2.
FT                                /FTId=PRO_0000225444.
FT   DOMAIN        2    119       Response regulatory.
FT   DOMAIN      144    337       CheB-type methylesterase.
FT   ACT_SITE    159    159       By similarity.
FT   ACT_SITE    186    186       By similarity.
FT   ACT_SITE    279    279       By similarity.
FT   MOD_RES      53     53       4-aspartylphosphate (By similarity).
SQ   SEQUENCE   342 AA;  36134 MW;  E7BA20EC1E01B7DB CRC64;
     MNIGIVNDLP LAVEALRRTI ALRPEHRVLW VATDGAQALD FCVAQPPDLV LMDLVMPRID
     GVSATRSIME RSPCAILIVT ANVGANASYV YEAMGAGALD AVDTPTLEQG GSADPSQPLL
     AKIDQIGRLL ATRMPLAAPA AAAPAPQGAL PPLVAIGASA GGPTALTALL RRLPDDFPAA
     LVIVQHVDQA FAIGMAQWLD GYSPLPVRIA RQGSVPQAGE VLLAATNDHL HLTSRGVLAY
     TRRPEETPYR PSVDVFFHSV VDHWKGEAIG VLLTGMGRDG ALGLKAMRTK GHYTIAQDEA
     TSAVYGMPKA AAAIGAASAV LPLERIADQL ISLVQRNRQR WR
//