ID   CHEB1_RHOS4             Reviewed;         369 AA.
AC   Q3J653;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   16-JUN-2009, entry version 26.
DE   RecName: Full=Chemotaxis response regulator protein-glutamate methylesterase 1;
DE            EC=3.1.1.61;
GN   Name=cheB1; OrderedLocusNames=RHOS4_01630; ORFNames=RSP_1588;
OS   Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM
OS   158).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=272943;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA   Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J.,
RA   Kaplan S.;
RT   "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000143; ABA77731.1; -; Genomic_DNA.
DR   RefSeq; YP_351632.1; -.
DR   GeneID; 3718577; -.
DR   GenomeReviews; CP000143_GR; RHOS4_01630.
DR   KEGG; rsp:RSP_1588; -.
DR   NMPDR; fig|272943.3.peg.384; -.
DR   HOGENOM; Q3J653; -.
DR   OMA; Q3J653; VMCSSLT.
DR   BioCyc; RSPH272943:RSP_1588-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    369       Chemotaxis response regulator protein-
FT                                glutamate methylesterase 1.
FT                                /FTId=PRO_0000225481.
FT   DOMAIN       11    128       Response regulatory.
FT   DOMAIN      170    363       CheB-type methylesterase.
FT   ACT_SITE    183    183       By similarity.
FT   ACT_SITE    209    209       By similarity.
FT   ACT_SITE    305    305       By similarity.
FT   MOD_RES      62     62       4-aspartylphosphate (By similarity).
SQ   SEQUENCE   369 AA;  39605 MW;  304F844CA7EB83C7 CRC64;
     MTTHAAAPST RVLIVDDSAA ARAMFKVIVE SDPALQVMAA VPDAFAAARA MRTELPDVIL
     LDLELPGMDG LTFLRKIMQQ HPIPVVVCSS HVGAGTEAMV SALELGAREV ISKPAARNDL
     ERQEASIRIC DAIRAATETT RRRSQPEPRP LAPGPKLTAD EILPARPPRP VPETMPVVCI
     GASTGGTEAL RDVLTALPAS APPIVIVQHM PRGFTAAFAR RLDSLCAIEV LEAEDEMQVM
     PGRAIIAQGD RHLLLRRRNQ GYRVSVLDGA YVCRHRPSVD VLFRSAAQEA GGNALGVIMT
     GMGDDGARCM AEMRAAGAET IAQNEESCVV YGMPREAVAH GGVGKVEPLD RLAARIMEFG
     RRHTERTVR
//