ID   Y415_BORBU              Reviewed;         375 AA.
AC   O51376;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-MAY-2022, entry version 126.
DE   RecName: Full=Probable protein-glutamate methylesterase BB_0415;
DE            EC=3.1.1.61;
GN   OrderedLocusNames=BB_0415;
OS   Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS   (Borrelia burgdorferi).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=224326;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX   PubMed=9403685; DOI=10.1038/37551;
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA   Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA   Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA   van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA   Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA   Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA   Smith H.O., Venter J.C.;
RT   "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL   Nature 390:580-586(1997).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-L-glutamate 5-O-methyl ester + H2O = H(+) + L-
CC         glutamyl-[protein] + methanol; Xref=Rhea:RHEA:23236, Rhea:RHEA-
CC         COMP:10208, Rhea:RHEA-COMP:10311, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17790, ChEBI:CHEBI:29973,
CC         ChEBI:CHEBI:82795; EC=3.1.1.61;
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DR   EMBL; AE000783; AAC66789.1; -; Genomic_DNA.
DR   PIR; F70151; F70151.
DR   RefSeq; NP_212549.1; NC_001318.1.
DR   RefSeq; WP_002657881.1; NC_001318.1.
DR   AlphaFoldDB; O51376; -.
DR   SMR; O51376; -.
DR   STRING; 224326.BB_0415; -.
DR   EnsemblBacteria; AAC66789; AAC66789; BB_0415.
DR   GeneID; 56567843; -.
DR   KEGG; bbu:BB_0415; -.
DR   PATRIC; fig|224326.49.peg.809; -.
DR   HOGENOM; CLU_000445_51_0_12; -.
DR   OMA; YGMPMAV; -.
DR   Proteomes; UP000001807; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro.
DR   GO; GO:0008984; F:protein-glutamate methylesterase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR   CDD; cd16432; CheB_Rec; 1.
DR   Gene3D; 3.40.50.180; -; 1.
DR   InterPro; IPR008248; CheB-like.
DR   InterPro; IPR035909; CheB_C.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR000673; Sig_transdc_resp-reg_Me-estase.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   Pfam; PF01339; CheB_methylest; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PIRSF; PIRSF000876; RR_chemtxs_CheB; 1.
DR   SUPFAM; SSF52172; SSF52172; 1.
DR   SUPFAM; SSF52738; SSF52738; 1.
DR   PROSITE; PS50122; CHEB; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..375
FT                   /note="Probable protein-glutamate methylesterase BB_0415"
FT                   /id="PRO_0000158060"
FT   DOMAIN          6..120
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   DOMAIN          183..375
FT                   /note="CheB-type methylesterase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00050"
FT   ACT_SITE        195
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00050"
FT   ACT_SITE        221
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00050"
FT   ACT_SITE        317
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00050"
SQ   SEQUENCE   375 AA;  41609 MW;  76F94AAFC98D09C0 CRC64;
     METKISVLII EYFAVKRKLI SDLINSSPKL QVIATASNSK FATNKLKKHK PEVILMNLEE
     NNIKDILFLE EKNSLNKTIP IVVTSSNQNL INIAASKGAD DLILVSKNKK SHEIKKEQII
     NSLLAYGSIS IKNKIACNKD MKTKNYERAN FILNHKNDIS SLNQLEEHAK EKTLNEKEIK
     KLKLRKFDII AIGVSAGGPV ALKSILPEIP ESFPPIIIVQ HMPKGFTEEF AKNLNNLCKI
     SVKETTNNEI LKQGYAYISS GGYHTKIKKI DGNYQIKTLD GKHINGHKPS IGVLFQSIAE
     IAKDKAIAII MTGMGNDGSR EIGDIKKAGG LTIAQDKESS MVFGMPKIAI KENNIDYIVP
     LSHMVKLLKA ILINS