ID   CBPS_STRMP              Reviewed;         434 AA.
AC   P39041;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Zinc carboxypeptidase {ECO:0000250|UniProtKB:P18143};
DE            EC=3.4.17.18 {ECO:0000250|UniProtKB:P18143};
DE   Flags: Precursor;
OS   Saccharothrix mutabilis subsp. capreolus (Streptomyces capreolus).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharothrix.
OX   NCBI_TaxID=66854;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Thiara A.S., Cundliffe E.;
RL   Submitted (AUG-1993) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Carboxypeptidase that possesses the specificities of both
CC       mammalian Cpase A and B. Thus shows broad substrate specificity, being
CC       able to cleave Cbz-Gly-Leu, Cbz-Gly-Val, Cbz-Gly-Phe, Cbz-Gly-Lys and
CC       Bz-Gly-Arg in vitro. {ECO:0000250|UniProtKB:P18143}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Releases a C-terminal residue, which may be hydrophobic or
CC         positively charged.; EC=3.4.17.18;
CC         Evidence={ECO:0000250|UniProtKB:P18143};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P18143};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P18143};
CC   -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
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DR   EMBL; U00619; AAA73397.1; -; Unassigned_DNA.
DR   AlphaFoldDB; P39041; -.
DR   SMR; P39041; -.
DR   MEROPS; M14.007; -.
DR   PRIDE; P39041; -.
DR   BRENDA; 3.4.17.18; 5989.
DR   GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd03859; M14_CPT; 1.
DR   InterPro; IPR033810; Carboxypeptidase_T.
DR   InterPro; IPR000834; Peptidase_M14.
DR   Pfam; PF00246; Peptidase_M14; 1.
DR   PRINTS; PR00765; CRBOXYPTASEA.
DR   SMART; SM00631; Zn_pept; 1.
DR   PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
DR   PROSITE; PS00133; CARBOXYPEPT_ZN_2; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW   Signal; Zinc; Zymogen.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000255"
FT   PROPEP          34..114
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000004413"
FT   CHAIN           115..434
FT                   /note="Zinc carboxypeptidase"
FT                   /id="PRO_0000004414"
FT   REGION          270..295
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        388
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P00732"
FT   BINDING         183
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         186
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         315
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
SQ   SEQUENCE   434 AA;  48477 MW;  5C010AAB636EAC88 CRC64;
     MSPKRRRLMA AALGACVALV LPLHAGSAQP STAKTPERTV FEVTASTPEA RTRVARTGVD
     VLGQDGDKLT VVAEPRQQWA LRATGLRVEN LGDYDAQLQA LGKVDFTDPQ VGTQDFPSGY
     TGYHNFQETV TELNQTVTDH PNLVRLSSVG KSYQGRDLWM LKLSDNPAVD ENEPEVLFTC
     NMHAREHLTV EMCLRIIKQY TDGYATNPTI KNLVDSREIW IIPMVNPDGV EYDIATGSFR
     SWRKNRQPNS TAVGTDPNRN WGYQWGCCGG SSSSGSSETT AARRRSPPRR SPHPHFVNTR
     VVGGVQQIKT HIDWHTYSEL ILWPYGYTYN DTAPGLDAQQ ASAFSTLGRR MASLNGTRRQ
     QSSDLYITDG TINDWLWGVH KIWSYTFEMY PKSSSPGFYP RDTVIATQTQ RNDSAVELFL
     SYSDCVPRII GRTC