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
//