ID   MEC_MYCBO               Reviewed;         146 AA.
AC   P64814; A0A1R3XY19; Q10645; X2BHM6;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=CysO-cysteine peptidase;
DE            EC=3.13.1.6 {ECO:0000250|UniProtKB:P9WHS1};
DE   AltName: Full=Metallocarboxypeptidase Mec;
GN   Name=mec; OrderedLocusNames=BQ2027_MB1369;
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   -!- FUNCTION: Protease that hydrolyzes the covalent CysO-cysteine adduct
CC       synthesized by CysM to release L-cysteine and regenerate CysO.
CC       {ECO:0000250|UniProtKB:P9WHS1}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[CysO sulfur-carrier protein]-Gly-NH-CH2-C(O)-S-L-Cys + H2O =
CC         [CysO sulfur-carrier protein]-C-terminal Gly-Gly + H(+) + L-cysteine;
CC         Xref=Rhea:RHEA:48732, Rhea:RHEA-COMP:12207, Rhea:RHEA-COMP:12212,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:35235,
CC         ChEBI:CHEBI:90778, ChEBI:CHEBI:90783; EC=3.13.1.6;
CC         Evidence={ECO:0000250|UniProtKB:P9WHS1};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P9WHS1};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis.
CC   -!- SIMILARITY: Belongs to the peptidase M67A family. {ECO:0000305}.
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DR   EMBL; LT708304; SIT99972.1; -; Genomic_DNA.
DR   RefSeq; NP_855023.1; NC_002945.3.
DR   RefSeq; WP_003898830.1; NC_002945.4.
DR   AlphaFoldDB; P64814; -.
DR   SMR; P64814; -.
DR   EnsemblBacteria; SIT99972; SIT99972; BQ2027_MB1369.
DR   GeneID; 45425312; -.
DR   PATRIC; fig|233413.5.peg.1501; -.
DR   OMA; GAHYVLV; -.
DR   UniPathway; UPA00136; -.
DR   Proteomes; UP000001419; Chromosome.
DR   GO; GO:0070122; F:isopeptidase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0140492; F:metal-dependent deubiquitinase activity; IEA:InterPro.
DR   GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR028090; JAB_dom_prok.
DR   InterPro; IPR000555; JAMM/MPN+_dom.
DR   InterPro; IPR037518; MPN.
DR   Pfam; PF14464; Prok-JAB; 1.
DR   SMART; SM00232; JAB_MPN; 1.
DR   PROSITE; PS50249; MPN; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cysteine biosynthesis; Hydrolase; Metal-binding;
KW   Metalloprotease; Protease; Zinc.
FT   CHAIN           1..146
FT                   /note="CysO-cysteine peptidase"
FT                   /id="PRO_0000014096"
FT   DOMAIN          11..134
FT                   /note="MPN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   MOTIF           88..101
FT                   /note="JAMM motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         88
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         90
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         101
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
SQ   SEQUENCE   146 AA;  16530 MW;  333945ED84CF2D5E CRC64;
     MLLRKGTVYV LVIRADLVNA MVAHARRDHP DEACGVLAGP EGSDRPERHI PMTNAERSPT
     FYRLDSGEQL KVWRAMEDAD EVPVVIYHSH TATEAYPSRT DVKLATEPDA HYVLVSTRDP
     HRHELRSYRI VDGAVTEEPV NVVEQY