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Database: UniProt
Entry: M6YYJ2_9LEPT
LinkDB: M6YYJ2_9LEPT
Original site: M6YYJ2_9LEPT 
ID   M6YYJ2_9LEPT            Unreviewed;       507 AA.
AC   M6YYJ2;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=Metal-dependent carboxypeptidase {ECO:0000256|PIRNR:PIRNR006615};
DE            EC=3.4.17.19 {ECO:0000256|PIRNR:PIRNR006615};
GN   ORFNames=LEP1GSC120_2083 {ECO:0000313|EMBL:EMO98860.1};
OS   Leptospira santarosai str. 200702252.
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=1049977 {ECO:0000313|EMBL:EMO98860.1, ECO:0000313|Proteomes:UP000012145};
RN   [1] {ECO:0000313|EMBL:EMO98860.1, ECO:0000313|Proteomes:UP000012145}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=200702252 {ECO:0000313|EMBL:EMO98860.1,
RC   ECO:0000313|Proteomes:UP000012145};
RA   Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA   Sanka R., DePew J., Purushe J., Picardeau M., Werts C., Goarant C.,
RA   Vinetz J.M., Sutton G.G., Nierman W.C., Fouts D.E.;
RL   Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Broad specificity carboxypetidase that releases amino acids
CC       sequentially from the C-terminus, including neutral, aromatic, polar
CC       and basic residues. {ECO:0000256|PIRNR:PIRNR006615}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of a C-terminal amino acid with broad specificity,
CC         except for -Pro.; EC=3.4.17.19;
CC         Evidence={ECO:0000256|PIRNR:PIRNR006615};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR006615-1};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR006615-1};
CC   -!- SIMILARITY: Belongs to the peptidase M32 family.
CC       {ECO:0000256|PIRNR:PIRNR006615}.
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:EMO98860.1}.
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DR   EMBL; AHOA02000017; EMO98860.1; -; Genomic_DNA.
DR   AlphaFoldDB; M6YYJ2; -.
DR   MEROPS; M32.001; -.
DR   Proteomes; UP000012145; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule.
DR   CDD; cd06460; M32_Taq; 1.
DR   Gene3D; 1.10.1370.30; -; 1.
DR   InterPro; IPR001333; Peptidase_M32_Taq.
DR   PANTHER; PTHR34217:SF1; CARBOXYPEPTIDASE 1; 1.
DR   PANTHER; PTHR34217; METAL-DEPENDENT CARBOXYPEPTIDASE; 1.
DR   Pfam; PF02074; Peptidase_M32; 1.
DR   PIRSF; PIRSF006615; Zn_crbxpep_Taq; 1.
DR   PRINTS; PR00998; CRBOXYPTASET.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000256|PIRNR:PIRNR006615,
KW   ECO:0000313|EMBL:EMO98860.1}; Hydrolase {ECO:0000256|PIRNR:PIRNR006615};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR006615,
KW   ECO:0000256|PIRSR:PIRSR006615-1};
KW   Metalloprotease {ECO:0000256|PIRNR:PIRNR006615};
KW   Protease {ECO:0000256|PIRNR:PIRNR006615};
KW   Zinc {ECO:0000256|PIRSR:PIRSR006615-1}.
FT   ACT_SITE        301
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006615-2"
FT   BINDING         300
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT   BINDING         304
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT   BINDING         331
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
SQ   SEQUENCE   507 AA;  58602 MW;  FCB8188390EE57EF CRC64;
     MRKNHFFAVR LLVNLKEEFL LSIEMKEYEN LFTEPIRREL KSFTEYRIAY QEIWTLKNVL
     SVLQWDSEII LPEDGRAERG SQIGLLSGLI HSKYAGEDFY KLAEKAREEN EQKNLPGQTE
     RKIEFERLFQ NLDRSRRLPR ELVEEFSVTT SKAHSIWARA KKENRFADFS QILSKIVELS
     KKQAECYGYQ TEAYDALLES YEPGERAKNL DQLFFKLKNN LKPLIAKGKK VANPFLKEVP
     VFLQNELGKS LPGILGLSSS ISRLDASEHP FSTSLGSKDK RITTRYDLKD PLSSIFSILH
     ETGHSLYEVG ISEIDGGPSP LHDSVSLGIH ESQSRLWENQ VGRSKEFWEM YYPIFLNTLN
     IKESELSFSK LFSYINQSSA SLIRVEADQI TYNLHIILRF EIERELINGK IQVSELPEVW
     NSKMKEIFGI TVPSDKEGVL QDVHWSGGAF GYFPTYTLGN IYSAQLFQAF SKENSDFQLE
     VREKKDFSSL LNWLKKTFIG NYKANIT
//
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