ID   CBPX2_SACS2             Reviewed;         393 AA.
AC   P58156;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Thermostable carboxypeptidase 2;
DE            EC=3.4.17.-;
GN   Name=cpsA2; Synonyms=cpsA-2; OrderedLocusNames=SSO1952;
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 [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).
CC   -!- FUNCTION: Can release basic, acidic, aromatic, and, to a lesser extent,
CC       aliphatic amino acids. {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M20 family. {ECO:0000305}.
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DR   EMBL; AE006641; AAK42144.1; -; Genomic_DNA.
DR   PIR; A99361; A99361.
DR   RefSeq; WP_009991759.1; NC_002754.1.
DR   AlphaFoldDB; P58156; -.
DR   SMR; P58156; -.
DR   STRING; 273057.SSO1952; -.
DR   MEROPS; M20.008; -.
DR   EnsemblBacteria; AAK42144; AAK42144; SSO1952.
DR   GeneID; 44130746; -.
DR   KEGG; sso:SSO1952; -.
DR   PATRIC; fig|273057.12.peg.2026; -.
DR   eggNOG; arCOG01108; Archaea.
DR   HOGENOM; CLU_023257_0_1_2; -.
DR   InParanoid; P58156; -.
DR   OMA; RAHACGH; -.
DR   PhylomeDB; P58156; -.
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   3: Inferred from homology;
KW   Carboxypeptidase; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW   Reference proteome; Zinc.
FT   CHAIN           1..393
FT                   /note="Thermostable carboxypeptidase 2"
FT                   /id="PRO_0000061948"
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"
SQ   SEQUENCE   393 AA;  42993 MW;  AFBDE9F0A3469B63 CRC64;
     MDLVEKLKND VKEIEDWIIQ IRRKIHENPE LSYKEYSTSK LVAETLRKLG IEVEEGVGLP
     TAVVGKIRGN KPGKTVALRA DMDALPVEET SDVEFKSKVK GVMHACGHDT HVAMLLGGAY
     LLVKNKDLIS GEIRLIFQPA EEDGGLGGAK PMIEAGVMNG VDYVFGIHIS SSYPSGVFAT
     RKGPIMATPD AFKIVVHGKG GHGSAPHETI DPIFISLQIA NAIYGITARQ IDPVQPFVIS
     ITTIHSGTKD NIIPDDAEMQ GTIRSLDENV RSKAKDYMRR IVSSICGIYG ATCEVKFMED
     VYPITVNNPE VTDEVMKILS SISTVVETEP VLGAEDFSRF LQKAPGMYFF LGTRNEKKGC
     IYPNHSSKFC VDEDVLKLGA LAHALLAIKF SNK