ID M5VDM4_9LEPT Unreviewed; 510 AA.
AC M5VDM4;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Carboxypeptidase Taq M32 metallopeptidase {ECO:0000313|EMBL:EMI66278.1};
DE Flags: Fragment;
GN ORFNames=LEP1GSC076_0311 {ECO:0000313|EMBL:EMI66278.1};
OS Leptospira sp. Fiocruz LV4135.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1193013 {ECO:0000313|EMBL:EMI66278.1, ECO:0000313|Proteomes:UP000011956};
RN [1] {ECO:0000313|EMBL:EMI66278.1, ECO:0000313|Proteomes:UP000011956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fiocruz LV4135 {ECO:0000313|EMBL:EMI66278.1,
RC ECO:0000313|Proteomes:UP000011956};
RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA Sanka R., DePew J., Ko A.I., Reis M.G., Ribeiro G.S., Wunder E.Jr.,
RA Vinetz J.M., Sutton G.G., Nierman W.C., Fouts D.E.;
RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:EMI66278.1}.
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DR EMBL; AOHI01000053; EMI66278.1; -; Genomic_DNA.
DR AlphaFoldDB; M5VDM4; -.
DR Proteomes; UP000011956; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
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 4: Predicted;
KW Carboxypeptidase {ECO:0000313|EMBL:EMI66278.1};
KW Hydrolase {ECO:0000313|EMBL:EMI66278.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR006615-1};
KW Protease {ECO:0000313|EMBL:EMI66278.1};
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"
FT NON_TER 510
FT /evidence="ECO:0000313|EMBL:EMI66278.1"
SQ SEQUENCE 510 AA; 59053 MW; 10DF9931CC01658A 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 YYPIFLDTLN
IKESELSFSK LFSYINQSSA SLIRVEADQI TYNLHIILRF EIERELINGK IQVSELPEVW
NSKMKEIFGI TVPSDKEGVL QDVHWSGGAF GYFPTYTLGN IYSAQLFQAF SKENSDFQLE
VREKKNFSSL LNWLKKNVHW KGKFYSAKDL
//
