CBPS_STRGR
ID CBPS_STRGR Reviewed; 451 AA.
AC P18143;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Zinc carboxypeptidase {ECO:0000303|PubMed:2118139};
DE EC=3.4.17.18 {ECO:0000269|PubMed:399};
DE AltName: Full=Cpase SG {ECO:0000303|PubMed:2118139};
DE Short=CPSG;
DE Flags: Precursor;
GN Name=scpD;
OS Streptomyces griseus.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1911;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=N2-3-11;
RA Roessler C., Piepersberg W.;
RL Submitted (APR-1992) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 124-451.
RC STRAIN=K-1;
RX PubMed=2118139; DOI=10.1093/oxfordjournals.jbchem.a123142;
RA Narahashi Y.;
RT "The amino acid sequence of zinc-carboxypeptidase from Streptomyces
RT griseus.";
RL J. Biochem. 107:879-886(1990).
RN [3]
RP PROTEIN SEQUENCE OF 124-171.
RA Strydom D.J., Bazzone T.J.;
RT "The amino-terminal sequence of Streptomyces griseus carboxypeptidase.";
RL J. Protein Chem. 4:141-149(1985).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP ACTIVITY REGULATION.
RC STRAIN=K-1;
RX PubMed=399; DOI=10.1016/s0021-9258(17)33946-7;
RA Seber J.F., Toomey T.P., Powell J.T., Brew K., Awad W.M. Jr.;
RT "Proteolytic enzymes of the K-1 strain of Streptomyces griseus obtained
RT from a commercial preparation (Pronase). Purification and characterization
RT of the carboxypeptidase.";
RL J. Biol. Chem. 251:204-208(1976).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND ACTIVITY
RP REGULATION.
RC STRAIN=K-1;
RX PubMed=410802;
RA Narahashi Y., Yoda K., Honda S.;
RT "Purification and specificity of carboxypeptidase from Streptomyces griseus
RT K-1.";
RL J. Biochem. 82:615-618(1977).
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:0000269|PubMed:399,
CC ECO:0000269|PubMed:410802}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Releases a C-terminal residue, which may be hydrophobic or
CC positively charged.; EC=3.4.17.18; Evidence={ECO:0000269|PubMed:399,
CC ECO:0000269|PubMed:410802};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:399};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:399};
CC -!- ACTIVITY REGULATION: In vitro, is completely inhibited by l,l0-
CC phenanthroline, and by isocaproic acid and Bz-Arg.
CC {ECO:0000269|PubMed:399, ECO:0000269|PubMed:410802}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7-8. {ECO:0000269|PubMed:399};
CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
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DR EMBL; X65719; CAA46635.1; -; Genomic_DNA.
DR PIR; S20723; S20723.
DR RefSeq; WP_003966921.1; NZ_UAVD01000027.1.
DR AlphaFoldDB; P18143; -.
DR SMR; P18143; -.
DR MEROPS; M14.007; -.
DR PRIDE; P18143; -.
DR GeneID; 6209349; -.
DR OMA; HQHAREH; -.
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 1: Evidence at protein level;
KW Carboxypeptidase; Direct protein sequencing; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Signal; Zinc; Zymogen.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT PROPEP 35..123
FT /note="Activation peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000004411"
FT CHAIN 124..451
FT /note="Zinc carboxypeptidase"
FT /id="PRO_0000004412"
FT ACT_SITE 400
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00732"
FT BINDING 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 327
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT CONFLICT 178
FT /note="T -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 451 AA; 48697 MW; 481EB570171730FE CRC64;
MRLVTARRPR PTKGRRNAAL TVLLALALAA PATAVATAGN AAPNAAVAAD ERTLQYEITG
RTTPAARTDI ARAGVSIDEV HDHGVVITAD AAQARKLRAR GHVLEALPAP DAAPRAADGV
SALDFPPADS RYHNYAEMNA AIDARIAANP SIMSKRVIGK TYQGRDVIAV KVSDNVATDE
AEPEVLFTAH QHAREHLTVE MALYLLRELG QGYGSDSRIT QAVNGRELWI VPDMNPDGGE
YDIASGSYRS WRKNRQPNAG SSAVGTDLNR NWAYKWGCCG GSSSSPSSET YRGAAAESAP
ETKVVADFVR SRVVGGKQQI TAAIDFHTYS ELVLWPFGYT YNDTAPGMTA DDRNAFAAVG
QKMAASNGYT AEQSSDLYIT DGSIDDWLWG SQKIFGYTFE MYPRSASGGG FYPPDEVIER
ETSRNRDAVL QLIENADCMY RSIGKEAQYC S
