ID   CHEB2_LEPIN             Reviewed;         193 AA.
AC   Q8F5D8;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 104.
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=LA_1744;
OS   Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain
OS   56601).
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=189518;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=56601;
RX   PubMed=12712204; DOI=10.1038/nature01597;
RA   Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X.,
RA   Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X.,
RA   Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., Zhang Y., Zhu G.-F.,
RA   Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y.,
RA   Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I.,
RA   Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.;
RT   "Unique physiological and pathogenic features of Leptospira interrogans
RT   revealed by whole-genome sequencing.";
RL   Nature 422:888-893(2003).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN48943.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE010300; AAN48943.2; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_711925.2; NC_004342.2.
DR   RefSeq; WP_001105137.1; NC_004342.2.
DR   AlphaFoldDB; Q8F5D8; -.
DR   SMR; Q8F5D8; -.
DR   STRING; 189518.LA_1744; -.
DR   EnsemblBacteria; AAN48943; AAN48943; LA_1744.
DR   GeneID; 61141947; -.
DR   KEGG; lil:LA_1744; -.
DR   PATRIC; fig|189518.3.peg.1735; -.
DR   HOGENOM; CLU_000445_51_2_12; -.
DR   InParanoid; Q8F5D8; -.
DR   OMA; PGYHLSV; -.
DR   Proteomes; UP000001408; 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; Reference proteome.
FT   CHAIN           1..193
FT                   /note="Putative protein-glutamate methylesterase/protein-
FT                   glutamine glutaminase"
FT                   /id="PRO_0000158003"
FT   DOMAIN          1..189
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