CBPX1_SACS2
ID CBPX1_SACS2 Reviewed; 393 AA.
AC P80092;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Thermostable carboxypeptidase 1;
DE EC=3.4.17.-;
GN Name=cpsA1; Synonyms=cpsA, cpsA-1; OrderedLocusNames=SSO1355;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 5833 / MT-4;
RX PubMed=7559343; DOI=10.1128/jb.177.19.5561-5566.1995;
RA Colombo S., Toietta G., Zecca L., Vanoni M., Tortora P.;
RT "Molecular cloning, nucleotide sequence, and expression of a
RT carboxypeptidase-encoding gene from the archaebacterium Sulfolobus
RT solfataricus.";
RL J. Bacteriol. 177:5561-5566(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [3]
RP PROTEIN SEQUENCE OF 1-31.
RC STRAIN=DSM 5833 / MT-4;
RX PubMed=1597179; DOI=10.1111/j.1432-1033.1992.tb16934.x;
RA Colombo S., D'Auria S., Fusi P., Zecca L., Raia C.A., Tortora P.;
RT "Purification and characterization of a thermostable carboxypeptidase from
RT the extreme thermophilic archaebacterium Sulfolobus solfataricus.";
RL Eur. J. Biochem. 206:349-357(1992).
CC -!- FUNCTION: Can release basic, acidic, aromatic, and, to a lesser extent,
CC aliphatic amino acids.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC -!- SUBUNIT: Homotetramer.
CC -!- SIMILARITY: Belongs to the peptidase M20 family. {ECO:0000305}.
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DR EMBL; Z48497; CAA88397.1; -; Genomic_DNA.
DR EMBL; AE006641; AAK41591.1; -; Genomic_DNA.
DR PIR; H90291; H90291.
DR PIR; S23180; S23180.
DR RefSeq; WP_010923348.1; NC_002754.1.
DR AlphaFoldDB; P80092; -.
DR SMR; P80092; -.
DR STRING; 273057.SSO1355; -.
DR MEROPS; M20.008; -.
DR EnsemblBacteria; AAK41591; AAK41591; SSO1355.
DR GeneID; 27427725; -.
DR KEGG; sso:SSO1355; -.
DR PATRIC; fig|273057.12.peg.1361; -.
DR eggNOG; arCOG01108; Archaea.
DR HOGENOM; CLU_023257_0_1_2; -.
DR InParanoid; P80092; -.
DR OMA; ECSCANV; -.
DR PhylomeDB; P80092; -.
DR BRENDA; 3.4.17.B1; 6163.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR017439; Amidohydrolase.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR PANTHER; PTHR11014; PTHR11014; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF005962; Pept_M20D_amidohydro; 1.
DR SUPFAM; SSF55031; SSF55031; 1.
DR TIGRFAMs; TIGR01891; amidohydrolases; 1.
PE 1: Evidence at protein level;
KW Carboxypeptidase; Direct protein sequencing; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Zinc.
FT CHAIN 1..393
FT /note="Thermostable carboxypeptidase 1"
FT /id="PRO_0000061947"
FT ACT_SITE 302
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT ACT_SITE 373
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT BINDING 245
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT CONFLICT 12
FT /note="R -> K (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 17
FT /note="W -> R (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 28
FT /note="Y -> N (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 30
FT /note="E -> P (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 393 AA; 43069 MW; B4754EC5A8E9A9C8 CRC64;
MDLVEKLKND VREIEDWIIQ IRRKIHEYPE LSYKEYNTSK LVAETLRKLG VEVEEGVGLP
TAVVGKIRGS KPGKTVALRA DMDALPVEEN TDLEFKSKVK GVMHACGHDT HVAMLLGGAY
LLVKNKDLIS GEIRLIFQPA EEDGGLGGAK PMIEAGVMNG VDYVFGIHIS SSYPSGVFAT
RKGPIMATPD AFKIIVHGKG GHGSAPHETI DPIFISLQIA NAIYGITARQ IDPVQPFIIS
ITTIHSGTKD NIIPDDAEMQ GTIRSLDENV RSKAKDYMRR IVSSICGIYG ATCEVKFMED
VYPTTVNNPE VTDEVMKILS SISTVVETEP VLGAEDFSRF LQKAPGTYFF LGTRNEKKGC
IYPNHSSKFC VDEDVLKLGA LAHALLAVKF SNK
