ID   CHEB1_XANC8             Reviewed;         352 AA.
AC   Q4UWU6;
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 1;
DE            EC=3.1.1.61;
GN   Name=cheB1; OrderedLocusNames=XC_1409;
OS   Xanthomonas campestris pv. campestris (strain 8004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=314565;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15899963; DOI=10.1101/gr.3378705;
RA   Qian W., Jia Y., Ren S.-X., He Y.-Q., Feng J.-X., Lu L.-F., Sun Q.,
RA   Ying G., Tang D.-J., Tang H., Wu W., Hao P., Wang L., Jiang B.-L.,
RA   Zeng S., Gu W.-Y., Lu G., Rong L., Tian Y., Yao Z., Fu G., Chen B.,
RA   Fang R., Qiang B., Chen Z., Zhao G.-P., Tang J.-L., He C.;
RT   "Comparative and functional genomic analyses of the pathogenicity of
RT   phytopathogen Xanthomonas campestris pv. campestris.";
RL   Genome Res. 15:757-767(2005).
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; CP000050; AAY48477.1; -; Genomic_DNA.
DR   RefSeq; YP_242497.2; -.
DR   GeneID; 3382346; -.
DR   GenomeReviews; CP000050_GR; XC_1409.
DR   KEGG; xcb:XC_1409; -.
DR   HOGENOM; Q4UWU6; -.
DR   OMA; Q4UWU6; CAVAVKE.
DR   BioCyc; XCAM314565:XC_1409-MON; -.
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    352       Chemotaxis response regulator protein-
FT                                glutamate methylesterase 1.
FT                                /FTId=PRO_0000225490.
FT   DOMAIN        1    116       Response regulatory.
FT   DOMAIN      162    352       CheB-type methylesterase.
FT   ACT_SITE    174    174       By similarity.
FT   ACT_SITE    200    200       By similarity.
FT   ACT_SITE    296    296       By similarity.
FT   MOD_RES      50     50       4-aspartylphosphate (By similarity).
SQ   SEQUENCE   352 AA;  37298 MW;  5C2AE933B83FFE84 CRC64;
     MVVDDSAVVR QVLVGVLNEA PGIEVIATAA DPLLAIEKMR QQWPDVIVLD VEMPRMDGIT
     FLRKIMSERP TPVVICSTLT EKGARVTMDA LAAGAVAVVT KPRLGLKQFL TDSADELVAT
     VRSAARANVK RLAARVTAAP LEAEVKHTAD VILPAQTGRA LAQTTERIVA IGTSTGGTQA
     LEEVLTALPR VCPGIVIVQH MPEKFTAAFA ARLNGLCQIA VKEAANNDRV MPGRALIAPG
     GKHLLLRRSG AQYFVEVLEG PPVNRHRPSV DVLFRSAARA AGSNALGIIM TGMGDDGAAG
     LLEMRQAGAR TIAQDEHTSI VFGMPKEAIK RGGADRILPL GAMAREIVTQ LQ
//