ID   G8NBN4_9DEIN            Unreviewed;       511 AA.
AC   G8NBN4;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=Metal-dependent carboxypeptidase {ECO:0000256|PIRNR:PIRNR006615};
DE            EC=3.4.17.19 {ECO:0000256|PIRNR:PIRNR006615};
GN   ORFNames=TCCBUS3UF1_20730 {ECO:0000313|EMBL:AEV17111.1};
OS   Thermus sp. CCB_US3_UF1.
OC   Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=1111069 {ECO:0000313|EMBL:AEV17111.1, ECO:0000313|Proteomes:UP000005635};
RN   [1] {ECO:0000313|EMBL:AEV17111.1, ECO:0000313|Proteomes:UP000005635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCB_US3_UF1 {ECO:0000313|EMBL:AEV17111.1,
RC   ECO:0000313|Proteomes:UP000005635};
RA   Teh B.S., Abdul Rahman A.Y., Saito J.A., Hou S., Alam M.;
RT   "Complete genome sequence of thermophilic Thermus sp. CCB_US3_UF1.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP003126; AEV17111.1; -; Genomic_DNA.
DR   RefSeq; WP_014516460.1; NC_017278.1.
DR   AlphaFoldDB; G8NBN4; -.
DR   STRING; 1111069.TCCBUS3UF1_20730; -.
DR   MEROPS; M32.001; -.
DR   KEGG; thc:TCCBUS3UF1_20730; -.
DR   PATRIC; fig|1111069.3.peg.2038; -.
DR   eggNOG; COG2317; Bacteria.
DR   HOGENOM; CLU_032916_1_1_0; -.
DR   OrthoDB; 9772308at2; -.
DR   Proteomes; UP000005635; 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   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000256|PIRNR:PIRNR006615,
KW   ECO:0000313|EMBL:AEV17111.1}; Hydrolase {ECO:0000256|PIRNR:PIRNR006615};
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   511 AA;  57825 MW;  87A592A3147DA269 CRC64;
     MTPEAAYQNL LEFQRETAYL ASLGALAAWD QRTMIPKKGH AHRAKQMAAL AKLLHGRMTD
     PRIGEWLERV EGSHLVQDPF SDAAVNVREW RQAYERARAI PERLAVELAE AESESESYWE
     EARPKDDWQG FLPYLKRVFS LTREKAEILY ALPVPQGDPP YGEPYDALLE GYEPGMRAAE
     LLLLFAQLRQ GLAGLLDRIL GSPKRPDTTL LHRSYPKEAQ RAFALELLQA CGYDLEAGRL
     DPTAHPFEIS IGPGDVRITT RYFQDFFNAG IFGTLHEMGH ALYEQGLPPE HWGTPRGEAV
     SLGVHESQSR TWENLVGRSL GFWERFFPRA QAHFPSLEGV GLEDFHFAVN AVAPSLIRVE
     ADEVTYNLHI LVRLELELAL FRGELSLEDL PGAWAEKYRA YLGVAPRDYK DGVMQDVHWS
     GGLFGYFPTY TLGNLYAAQF FAKAEEELGD LEGLFRLGEF RPFLDWTRRK IHAEGSRFRP
     KALVERVTGA PPSAGPFLAY LEGKYRALYA L
//