ID A0A151AU75_9CLOT Unreviewed; 501 AA.
AC A0A151AU75;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Metal-dependent carboxypeptidase {ECO:0000256|PIRNR:PIRNR006615};
DE EC=3.4.17.19 {ECO:0000256|PIRNR:PIRNR006615};
GN Name=ypwA {ECO:0000313|EMBL:KYH31151.1};
GN ORFNames=CLTEP_24310 {ECO:0000313|EMBL:KYH31151.1};
OS Clostridium tepidiprofundi DSM 19306.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121338 {ECO:0000313|EMBL:KYH31151.1, ECO:0000313|Proteomes:UP000075531};
RN [1] {ECO:0000313|EMBL:KYH31151.1, ECO:0000313|Proteomes:UP000075531}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19306 {ECO:0000313|EMBL:KYH31151.1,
RC ECO:0000313|Proteomes:UP000075531};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Clostridium tepidiprofundi DSM 19306.";
RL Submitted (FEB-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:KYH31151.1}.
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DR EMBL; LTBA01000050; KYH31151.1; -; Genomic_DNA.
DR RefSeq; WP_066827036.1; NZ_LTBA01000050.1.
DR AlphaFoldDB; A0A151AU75; -.
DR STRING; 1121338.CLTEP_24310; -.
DR PATRIC; fig|1121338.3.peg.2513; -.
DR OrthoDB; 9772308at2; -.
DR Proteomes; UP000075531; 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:KYH31151.1};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR006615, ECO:0000313|EMBL:KYH31151.1};
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:UP000075531};
KW Zinc {ECO:0000256|PIRSR:PIRSR006615-1}.
FT ACT_SITE 267
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-2"
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 270
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT BINDING 296
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
SQ SEQUENCE 501 AA; 58669 MW; BF3571F33820B736 CRC64;
MNNEAQNKMK EFKEYINKIE YLNSAASLLY WDMSVNMPKK GVEYRGKVLG HLTAEIYKLE
TSDTMKEYLE YFSKIDDLDE VHKSMIKSLK KNYELSKKIP EEKFKEYTIL TTQAEAAWED
AYAKSDFSLF QPYLEKIVAF NKEFVEYWGY KGNKYNTLLD KFEEGITVDK LDNIFSELRE
ALVKLLDKIK NSNVKIDESI FKNNFSKEKQ EQLSKLILEK MGYDFEAGRL DESIHPFTIG
FNRKDVRITT NYCDKDLRPA LFSSIHEGGH AIYDQDISEE LYGTGLGDGA SMGVHESQSR
FYENILGRSK EFWTYFYTEV KKIFQEFKDV SLEDFYRGMN VVEPSLIRVD ADELTYSLHV
IIRYEIEKGL INGDIEVENL PEVWNAKYKE YLGIEPSNDK EGVLQDNHWA GGMIGYFPSY
ALGNIYGAQF FNKMKQDIPD IFKQIEKGNF EVIHEWLKEN IHKYGAVYTP SELIKKVTGE
ELTAKYFIEY LNNKYSKIYN L
//
