ID   CHEB2_LEPIC             Reviewed;         193 AA.
AC   P62642; Q72QQ2;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Putative protein-glutamate methylesterase/protein-glutamine glutaminase {ECO:0000305};
DE            EC=3.1.1.61 {ECO:0000250};
DE            EC=3.5.1.44 {ECO:0000250};
GN   Name=cheB2; OrderedLocusNames=LIC_12061;
OS   Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni
OS   (strain Fiocruz L1-130).
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=267671;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fiocruz L1-130;
RX   PubMed=15028702; DOI=10.1128/jb.186.7.2164-2172.2004;
RA   Nascimento A.L.T.O., Ko A.I., Martins E.A.L., Monteiro-Vitorello C.B.,
RA   Ho P.L., Haake D.A., Verjovski-Almeida S., Hartskeerl R.A., Marques M.V.,
RA   Oliveira M.C., Menck C.F.M., Leite L.C.C., Carrer H., Coutinho L.L.,
RA   Degrave W.M., Dellagostin O.A., El-Dorry H., Ferro E.S., Ferro M.I.T.,
RA   Furlan L.R., Gamberini M., Giglioti E.A., Goes-Neto A., Goldman G.H.,
RA   Goldman M.H.S., Harakava R., Jeronimo S.M.B., Junqueira-de-Azevedo I.L.M.,
RA   Kimura E.T., Kuramae E.E., Lemos E.G.M., Lemos M.V.F., Marino C.L.,
RA   Nunes L.R., de Oliveira R.C., Pereira G.G., Reis M.S., Schriefer A.,
RA   Siqueira W.J., Sommer P., Tsai S.M., Simpson A.J.G., Ferro J.A.,
RA   Camargo L.E.A., Kitajima J.P., Setubal J.C., Van Sluys M.A.;
RT   "Comparative genomics of two Leptospira interrogans serovars reveals novel
RT   insights into physiology and pathogenesis.";
RL   J. Bacteriol. 186:2164-2172(2004).
CC   -!- FUNCTION: May be involved in chemotaxis. {ECO:0000250}.
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; Evidence={ECO:0000250};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+);
CC         Xref=Rhea:RHEA:16441, Rhea:RHEA-COMP:10207, Rhea:RHEA-COMP:10208,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29973,
CC         ChEBI:CHEBI:30011; EC=3.5.1.44; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CheB family. {ECO:0000305}.
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DR   EMBL; AE016823; AAS70632.1; -; Genomic_DNA.
DR   RefSeq; WP_001105137.1; NC_005823.1.
DR   AlphaFoldDB; P62642; -.
DR   SMR; P62642; -.
DR   PaxDb; P62642; -.
DR   EnsemblBacteria; AAS70632; AAS70632; LIC_12061.
DR   GeneID; 61141947; -.
DR   KEGG; lic:LIC_12061; -.
DR   HOGENOM; CLU_000445_51_2_12; -.
DR   OMA; PGYHLSV; -.
DR   Proteomes; UP000007037; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0050568; F:protein-glutamine glutaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.180; -; 1.
DR   InterPro; IPR035909; CheB_C.
DR   InterPro; IPR000673; Sig_transdc_resp-reg_Me-estase.
DR   Pfam; PF01339; CheB_methylest; 1.
DR   SUPFAM; SSF52738; SSF52738; 1.
DR   PROSITE; PS50122; CHEB; 1.
PE   3: Inferred from homology;
KW   Chemotaxis; Cytoplasm; Hydrolase.
FT   CHAIN           1..193
FT                   /note="Putative protein-glutamate methylesterase/protein-
FT                   glutamine glutaminase"
FT                   /id="PRO_0000158000"
FT   DOMAIN          1..179
FT                   /note="CheB-type methylesterase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00050"
FT   ACT_SITE        11
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00050"
FT   ACT_SITE        38
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00050"
FT   ACT_SITE        131
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00050"
SQ   SEQUENCE   193 AA;  21292 MW;  1F1DB67891BE90BC CRC64;
     MNYEAIVIGV SAGGINAMKT ILPTLPTQFG IPIVIVQHIG ARSDGEWFRI LEKLCNIKIK
     EAEEKEEIKS GMVYVAPPNY HLLIEKDKTF SFSIGERVNF SRPSIDVLFE TASEVYEDKL
     IGVILTGANS DGAQGLKKIK ENGGLAVVQD PLTAEIALMP RSAIEATSVD YVLSLEKIAE
     LFIRLDQNNL EQR