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 02-SEP-2026, entry version 145. 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; Thermoproteota; 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}. 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; 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 FunCoup; P80092; 13. DR STRING; 273057.SSO1355; -. DR MEROPS; M20.008; -. DR PaxDb; 273057-SSO1355; -. DR EnsemblBacteria; AAK41591; AAK41591; SSO1355. DR GeneID; 1454370; -. 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 PhylomeDB; P80092; -. DR BRENDA; 3.4.17.B1; 6163. DR Proteomes; UP000001974; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro. DR CDD; cd08021; M20_Acy1_YhaA-like; 1. DR FunFam; 3.30.70.360:FF:000014; N-acyl-L-amino acid amidohydrolase; 1. DR Gene3D; 3.30.70.360; -; 1. DR Gene3D; 3.40.630.10; Zn peptidases; 1. DR InterPro; IPR017439; Amidohydrolase. DR InterPro; IPR036264; Bact_exopeptidase_dim_dom. DR InterPro; IPR002933; Peptidase_M20. DR InterPro; IPR011650; Peptidase_M20_dimer. DR InterPro; IPR053493; Thermostable_CP. DR NCBIfam; TIGR01891; amidohydrolases; 1. DR NCBIfam; NF040868; carboxypep_CpsA; 1. DR PANTHER; PTHR11014:SF63; METALLOPEPTIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G09600)-RELATED; 1. DR PANTHER; PTHR11014; PEPTIDASE M20 FAMILY MEMBER; 1. DR Pfam; PF07687; M20_dimer; 1. DR Pfam; PF01546; Peptidase_M20; 1. DR PIRSF; PIRSF005962; Pept_M20D_amidohydro; 1. DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1. DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 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 //