ID CBPX2_SULSO Reviewed; 393 AA. AC P58156; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 29-MAY-2013, entry version 77. DE RecName: Full=Thermostable carboxypeptidase 2; DE EC=3.4.17.-; GN Name=cpsA2; Synonyms=cpsA-2; OrderedLocusNames=SSO1952; OS Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / OS P2). OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae; OC Sulfolobus. 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., RA Awayez M.J., Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., RA De Moors A., Erauso G., Fletcher C., Gordon P.M.K., RA Heikamp-de Jong I., Jeffries A.C., Kozera C.J., Medina N., Peng X., RA Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C., Tolstrup N., RA 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 CC extent, aliphatic amino acids (By similarity). CC -!- COFACTOR: Zinc (By similarity). CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SIMILARITY: Belongs to the peptidase M20 family. 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; NP_343354.1; NC_002754.1. DR ProteinModelPortal; P58156; -. DR STRING; 273057.SSO1952; -. DR MEROPS; M20.008; -. DR EnsemblBacteria; AAK42144; AAK42144; SSO1952. DR GeneID; 1453471; -. DR KEGG; sso:SSO1952; -. DR eggNOG; COG1473; -. DR HOGENOM; HOG000241404; -. DR KO; K13048; -. DR OMA; NHSSKFT; -. DR ProtClustDB; CLSK785363; -. DR BioCyc; SSOL273057:GCH2-1829-MONOMER; -. DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW. 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 Gene3D; 3.30.70.360; -; 1. DR InterPro; IPR017439; Amidohydrolase. 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; Peptidase_M20_dimer; 1. DR TIGRFAMs; TIGR01891; amidohydrolases; 1. PE 3: Inferred from homology; KW Carboxypeptidase; Complete proteome; Hydrolase; Metal-binding; KW Metalloprotease; Protease; Reference proteome; Zinc. FT CHAIN 1 393 Thermostable carboxypeptidase 2. FT /FTId=PRO_0000061948. FT ACT_SITE 302 302 Proton donor (Potential). FT ACT_SITE 373 373 Nucleophile (Potential). FT METAL 104 104 Zinc (Potential). FT METAL 109 109 Zinc (Potential). FT METAL 245 245 Zinc (Potential). 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 //