ID Q72GY3_THET2 Unreviewed; 510 AA. AC Q72GY3; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 28-JUN-2023, entry version 98. 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 ATCC BAA-163 / DSM 7039 / HB27). OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; 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=ATCC BAA-163 / DSM 7039 / HB27 RC {ECO:0000313|Proteomes:UP000000592}; RX PubMed=15064768; DOI=10.1038/nbt956; RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H., RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C., RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P., RA Overbeek R., Kramer W., Merkl R., Gottschalk G., Fritz H.-J.; RT "The genome sequence of the extreme thermophile Thermus thermophilus."; RL Nat. Biotechnol. 22:547-553(2004). RN [2] {ECO:0007829|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 carboxypeptidases: RT characterization of two distinct subfamilies."; RL Proteins 77:647-657(2009). CC -!- FUNCTION: Broad specificity carboxypetidase that releases amino acids CC sequentially from the C-terminus, including neutral, aromatic, polar CC and basic residues. {ECO:0000256|PIRNR:PIRNR006615}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Release of a C-terminal amino acid with broad specificity, CC except for -Pro.; EC=3.4.17.19; CC Evidence={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:PIRSR006615-1}; 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 AlphaFoldDB; Q72GY3; -. DR SMR; Q72GY3; -. DR STRING; 262724.TT_C1715; -. DR MEROPS; M32.001; -. DR EnsemblBacteria; AAS82057; AAS82057; TT_C1715. DR GeneID; 3168368; -. DR KEGG; tth:TT_C1715; -. DR eggNOG; COG2317; Bacteria. DR HOGENOM; CLU_032916_1_1_0; -. DR OMA; EFGHALY; -. DR OrthoDB; 9772308at2; -. 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 GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule. DR CDD; cd06460; M32_Taq; 1. DR Gene3D; 1.10.1370.30; -; 1. DR InterPro; IPR001333; Peptidase_M32_Taq. DR PANTHER; PTHR34217:SF1; CARBOXYPEPTIDASE 1; 1. DR PANTHER; PTHR34217; METAL-DEPENDENT CARBOXYPEPTIDASE; 1. DR Pfam; PF02074; Peptidase_M32; 1. DR PIRSF; PIRSF006615; Zn_crbxpep_Taq; 1. DR PRINTS; PR00998; CRBOXYPTASET. DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:3HOA}; KW Carboxypeptidase {ECO:0000256|PIRNR:PIRNR006615, KW ECO:0000313|EMBL:AAS82057.1}; KW Hydrolase {ECO:0000256|PIRNR:PIRNR006615, 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 ACT_SITE 277 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR006615-2" FT BINDING 276 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1" FT BINDING 280 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1" FT BINDING 306 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR: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 //