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 29-SEP-2021, entry version 110. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE006641; AAK42144.1; -; Genomic_DNA. DR PIR; A99361; A99361. DR RefSeq; WP_009991759.1; NC_002754.1. 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 BioCyc; SSOL273057:G1FZF-2150-MONOMER; -. 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 InterPro; IPR017439; Amidohydrolase. DR InterPro; IPR036264; Bact_exopeptidase_dim_dom. DR InterPro; IPR002933; Peptidase_M20. DR InterPro; IPR011650; Peptidase_M20_dimer. 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 METAL 104 FT /note="Zinc" FT /evidence="ECO:0000255" FT METAL 109 FT /note="Zinc" FT /evidence="ECO:0000255" FT METAL 245 FT /note="Zinc" 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 //