ID Q72GY3_THET2 Unreviewed; 510 AA. AC Q72GY3; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 25-APR-2018, entry version 80. DE RecName: Full=Metal-dependent carboxypeptidase {ECO:0000256|PIRNR:PIRNR006615}; DE EC=3.4.17.19 {ECO:0000256|PIRNR:PIRNR006615}; GN OrderedLocusNames=TT_C1715 {ECO:0000313|EMBL:AAS82057.1}; OS Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039). OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; OC Thermus. OX NCBI_TaxID=262724 {ECO:0000313|EMBL:AAS82057.1, ECO:0000313|Proteomes:UP000000592}; RN [1] {ECO:0000313|EMBL:AAS82057.1, ECO:0000313|Proteomes:UP000000592} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HB27 / ATCC BAA-163 / DSM 7039 RC {ECO:0000313|Proteomes:UP000000592}; RX PubMed=15064768; DOI=10.1038/nbt956; RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., RA Liesegang H., Johann A., Lienard T., Gohl O., Martinez-Arias R., RA Jacobi C., Starkuviene V., Schlenczeck S., Dencker S., Huber R., RA Klenk H.-P., Overbeek R., Kramer W., Merkl R., Gottschalk G., RA Fritz H.-J.; RT "The genome sequence of the extreme thermophile Thermus RT thermophilus."; RL Nat. Biotechnol. 22:547-553(2004). RN [2] {ECO:0000213|PDB:3HOA} RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1-509. RX PubMed=19544567; DOI=10.1002/prot.22478; RA Lee M.M., Isaza C.E., White J.D., Chen R.P., Liang G.F., He H.T., RA Chan S.I., Chan M.K.; RT "Insight into the substrate length restriction of M32 RT carboxypeptidases: characterization of two distinct subfamilies."; RL Proteins 77:647-657(2009). CC -!- FUNCTION: Broad specificity carboxypetidase that releases amino CC acids sequentially from the C-terminus, including neutral, CC aromatic, polar and basic residues. CC {ECO:0000256|PIRNR:PIRNR006615}. CC -!- CATALYTIC ACTIVITY: Release of a C-terminal amino acid with broad CC specificity, except for -Pro. {ECO:0000256|PIRNR:PIRNR006615}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR006615-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR006615- CC 1}; CC -!- SIMILARITY: Belongs to the peptidase M32 family. CC {ECO:0000256|PIRNR:PIRNR006615}. 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; AE017221; AAS82057.1; -; Genomic_DNA. DR RefSeq; WP_011174078.1; NC_005835.1. DR PDB; 3HOA; X-ray; 2.10 A; A/B=1-509. DR PDBsum; 3HOA; -. DR ProteinModelPortal; Q72GY3; -. DR SMR; Q72GY3; -. DR STRING; 262724.TTC1715; -. DR EnsemblBacteria; AAS82057; AAS82057; TT_C1715. DR KEGG; tth:TT_C1715; -. DR eggNOG; ENOG4105CTD; Bacteria. DR eggNOG; COG2317; LUCA. DR KO; K01299; -. DR OMA; EFGHALY; -. DR EvolutionaryTrace; Q72GY3; -. DR Proteomes; UP000000592; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:UniProtKB-UniRule. DR CDD; cd06460; M32_Taq; 1. DR InterPro; IPR001333; Peptidase_M32_Taq. DR PANTHER; PTHR34217; PTHR34217; 1. DR Pfam; PF02074; Peptidase_M32; 1. DR PIRSF; PIRSF006615; Zn_crbxpep_Taq; 1. DR PRINTS; PR00998; CRBOXYPTASET. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3HOA}; KW Carboxypeptidase {ECO:0000256|PIRNR:PIRNR006615, KW ECO:0000313|EMBL:AAS82057.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000592}; KW Hydrolase {ECO:0000256|PIRNR:PIRNR006615, KW ECO:0000313|EMBL:AAS82057.1}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR006615, KW ECO:0000256|PIRSR:PIRSR006615-1}; KW Metalloprotease {ECO:0000256|PIRNR:PIRNR006615}; KW Protease {ECO:0000256|PIRNR:PIRNR006615}; KW Zinc {ECO:0000256|PIRSR:PIRSR006615-1}. FT METAL 276 276 Zinc; catalytic. {ECO:0000256|PIRSR: FT PIRSR006615-1}. FT METAL 280 280 Zinc; catalytic. {ECO:0000256|PIRSR: FT PIRSR006615-1}. FT METAL 306 306 Zinc; catalytic. {ECO:0000256|PIRSR: FT PIRSR006615-1}. SQ SEQUENCE 510 AA; 58014 MW; 6EE48D42AA2FA379 CRC64; MTPEAAYQNL LEFQRETAYL ASLGALAAWD QRTMIPKKGH EHRARQMAAL ARLLHQRMTD PRIGEWLEKV EGSPLVQDPL SDAAVNVREW RQAYERARAI PERLAVELAQ AESEAESFWE EARPRDDWRG FLPYLKRVYA LTKEKAEVLF ALPPAPGDPP YGELYDALLD GYEPGMRARE LLPLFAELKE GLKGLLDRIL GSGKRPDTSI LHRPYPVEAQ RRFALELLSA CGYDLEAGRL DPTAHPFEIA IGPGDVRITT RYYEDFFNAG IFGTLHEMGH ALYEQGLPKE HWGTPRGDAV SLGVHESQSR TWENLVGRSL GFWERFFPRA REVFASLGDV SLEDFHFAVN AVEPSLIRVE ADEVTYNLHI LVRLELELAL FRGELSPEDL PEAWAEKYRD HLGVAPKDYK DGVMQDVHWA GGLFGYFPTY TLGNLYAAQF FQKAEAELGP LEPRFARGEF QPFLDWTRAR IHAEGSRFRP RVLVERVTGE APSARPFLAY LEKKYAALYG //