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Database: UniProt
Entry: M3E4C7_LEPIR
LinkDB: M3E4C7_LEPIR
Original site: M3E4C7_LEPIR 
ID   M3E4C7_LEPIR            Unreviewed;       278 AA.
AC   M3E4C7;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=protein-glutamate methylesterase {ECO:0000256|ARBA:ARBA00039140};
DE            EC=3.1.1.61 {ECO:0000256|ARBA:ARBA00039140};
GN   ORFNames=LEP1GSC067_1049 {ECO:0000313|EMBL:EMF41895.1};
OS   Leptospira interrogans serovar Lora str. TE 1992.
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=1193028 {ECO:0000313|EMBL:EMF41895.1, ECO:0000313|Proteomes:UP000011754};
RN   [1] {ECO:0000313|EMBL:EMF41895.1, ECO:0000313|Proteomes:UP000011754}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TE 1992 {ECO:0000313|EMBL:EMF41895.1,
RC   ECO:0000313|Proteomes:UP000011754};
RA   Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA   Sanka R., DePew J., Purushe J., Hartskeerl R.A., Ahmed A.,
RA   van der Linden H., Goris M.G.A., Vinetz J.M., Sutton G.G., Nierman W.C.,
RA   Fouts D.E.;
RL   Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
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;
CC         Evidence={ECO:0000256|ARBA:ARBA00000941};
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00169}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EMF41895.1}.
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DR   EMBL; AKWW02000051; EMF41895.1; -; Genomic_DNA.
DR   AlphaFoldDB; M3E4C7; -.
DR   Proteomes; UP000011754; Unassembled WGS sequence.
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:InterPro.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-UniRule.
DR   CDD; cd16432; CheB_Rec; 1.
DR   Gene3D; 3.40.50.180; Methylesterase CheB, C-terminal domain; 1.
DR   InterPro; IPR035909; CheB_C.
DR   InterPro; IPR000673; Sig_transdc_resp-reg_Me-estase.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR42872; PROTEIN-GLUTAMATE METHYLESTERASE/PROTEIN-GLUTAMINE GLUTAMINASE; 1.
DR   PANTHER; PTHR42872:SF6; PROTEIN-GLUTAMATE METHYLESTERASE/PROTEIN-GLUTAMINE GLUTAMINASE; 1.
DR   Pfam; PF01339; CheB_methylest; 1.
DR   SUPFAM; SSF52738; Methylesterase CheB, C-terminal domain; 1.
DR   PROSITE; PS50122; CHEB; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Chemotaxis {ECO:0000256|PROSITE-ProRule:PRU00050};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU00050}.
FT   DOMAIN          1..51
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          90..278
FT                   /note="CheB-type methylesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50122"
FT   ACT_SITE        102
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT   ACT_SITE        128
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT   ACT_SITE        224
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ   SEQUENCE   278 AA;  30182 MW;  F91C87FD06B7E0D3 CRC64;
     MSEKPTPVII CSSLAEKESE TAVLAMKLGA VDIIEKPKVG LKNFLEESEI LFIDSVRAAS
     NARVKTHSFQ NDDSKFLENH KQPKTDFSKI DTTDKLIAIG TSTGGTQALE FILTQLNIHC
     PGIVIVQHMP EKFTEAFANR LNQVCKIQVK EAKDGDRVQL GSAYIAPGNK HMEIYLSGAQ
     FHIRVLDGPL VNRHRPSVDT LFHSVAKAAG KNAKGIIMTG MGNDGANGLL KMKQSGAHTI
     AQDEASCVVF GMPKEAILKG AVNTILPLSK IVGEVQYF
//
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