ID   Y517_MYCBO              Reviewed;         308 AA.
AC   P66802; A0A1R3XWL0; Q11169; X2BF63;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Putative hydrolase Mb0517c;
DE            EC=3.1.-.-;
GN   OrderedLocusNames=BQ2027_MB0517C;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. SerB family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=SIT99113.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; LT708304; SIT99113.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; P66802; -.
DR   SMR; P66802; -.
DR   PATRIC; fig|233413.5.peg.563; -.
DR   Proteomes; UP000001419; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006385; HAD_hydro_SerB1.
DR   InterPro; IPR023214; HAD_sf.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR01490; HAD-SF-IB-hyp1; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Metal-binding.
FT   CHAIN           1..308
FT                   /note="Putative hydrolase Mb0517c"
FT                   /id="PRO_0000156894"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        62
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        64
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255"
FT   BINDING         62
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         64
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         237
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   308 AA;  32673 MW;  EA722C653C3A88DC CRC64;
     MMVSSHLGSP DQAGHVDLAS PADPPPPDAS ASHSPVDMPA PVAAAGSDRQ PPIDLTAAAF
     FDVDNTLVQG SSAVHFGRGL AARHYFTYRD VLGFLYAQAK FQLLGKENSN DVAAGRRKAL
     AFIEGRSVAE LVALGEEIYD EIIADKIWDG TRELTQMHLD AGQQVWLITA TPYELAATIA
     RRLGLTGALG TVAESVDGIF TGRLVGEILH GTGKAHAVRS LAIREGLNLK RCTAYSDSYN
     DVPMLSLVGT AVAINPDARL RSLARERGWE IRDFRIARKA ARIGVPSALA LGAAGGALAA
     LASRRQSR