ID A0A419SSH0_9FIRM Unreviewed; 498 AA.
AC A0A419SSH0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 03-MAY-2023, entry version 11.
DE RecName: Full=Metal-dependent carboxypeptidase {ECO:0000256|PIRNR:PIRNR006615};
DE EC=3.4.17.19 {ECO:0000256|PIRNR:PIRNR006615};
GN ORFNames=BET01_11185 {ECO:0000313|EMBL:RKD28102.1};
OS Lacrimispora algidixylanolytica.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Lacrimispora.
OX NCBI_TaxID=94868 {ECO:0000313|EMBL:RKD28102.1, ECO:0000313|Proteomes:UP000284277};
RN [1] {ECO:0000313|EMBL:RKD28102.1, ECO:0000313|Proteomes:UP000284277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SPL73 {ECO:0000313|EMBL:RKD28102.1,
RC ECO:0000313|Proteomes:UP000284277};
RA Poppleton D.I., Gribaldo S.;
RT "A new outlook on sporulation: Clostridium algidixylanolyticum.";
RL Submitted (AUG-2016) 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:RKD28102.1}.
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DR EMBL; MCIA01000035; RKD28102.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A419SSH0; -.
DR OrthoDB; 9772308at2; -.
DR Proteomes; UP000284277; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000284277};
KW Zinc {ECO:0000256|PIRSR:PIRSR006615-1}.
FT ACT_SITE 263
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-2"
FT BINDING 262
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT BINDING 266
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT BINDING 292
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
SQ SEQUENCE 498 AA; 58056 MW; A75960C0E33F0D9A CRC64;
MKKSYETLNS MLERSMALQT SLILFEWDNE TLAPEDAGSY TNRVIGVLSE EYYRIMTDDE
MGNAIEACEK EDNLSDLERA IVKAAREARE DLICIPSQEY RENAQLVADA VRIWTKAKKS
EDFDSFAPTL EKVIGFKKKF ASYRKKDDQK LYDVMLNEHE KDFNSELLDE FFSQLKKEIV
PLLKEITEHG KEIDVSFLTG GYPVEKQKEM AEFLAKYLGF DFKKGVLSES AHPFTTNLHN
HDVRITTSYH DRMDSSMFSV IHETGHGLYE LGIGDDITQT SAGQGTSMGV HESQSRFFEN
IIGRKAAFWE PIYGKLQELY PDKLSDIPLE QFVEAINKVE PSYIRTEADE LTYSLHIMIR
YEMEKMIVEE DIDLKKLPDI WADKYEEYLG VRPDKASKGI LQDIHWSQGM FGYFPSYALG
NAFGAQLYYH MQKEMDFDEL LRDEKIDVIR EYLRENIHRF GKLKTSRELL KDITGEDFNP
DYFIRYLKEK YRKLYGLS
//
