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Database: UniProt
Entry: A0A2T6KCL6_9RHOB
LinkDB: A0A2T6KCL6_9RHOB
Original site: A0A2T6KCL6_9RHOB 
ID   A0A2T6KCL6_9RHOB        Unreviewed;       458 AA.
AC   A0A2T6KCL6;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=Carboxypeptidase Taq {ECO:0000313|EMBL:PUB12713.1};
GN   ORFNames=C8N45_10921 {ECO:0000313|EMBL:PUB12713.1};
OS   Yoonia sediminilitoris.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Yoonia.
OX   NCBI_TaxID=1286148 {ECO:0000313|EMBL:PUB12713.1, ECO:0000313|Proteomes:UP000244523};
RN   [1] {ECO:0000313|EMBL:PUB12713.1, ECO:0000313|Proteomes:UP000244523}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 29955 {ECO:0000313|EMBL:PUB12713.1,
RC   ECO:0000313|Proteomes:UP000244523};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PUB12713.1}.
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DR   EMBL; QBUD01000009; PUB12713.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T6KCL6; -.
DR   Proteomes; UP000244523; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
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   4: Predicted;
KW   Carboxypeptidase {ECO:0000313|EMBL:PUB12713.1};
KW   Hydrolase {ECO:0000313|EMBL:PUB12713.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR006615-1};
KW   Protease {ECO:0000313|EMBL:PUB12713.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000244523};
KW   Zinc {ECO:0000256|PIRSR:PIRSR006615-1}.
FT   ACT_SITE        224
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006615-2"
FT   BINDING         223
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT   BINDING         227
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT   BINDING         253
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
SQ   SEQUENCE   458 AA;  49727 MW;  89349B7AB36F63A2 CRC64;
     MPAGATPQRA EEHGAMANIL HARRIDPRVG EWLAQAEAID EVAKANLRHI RRNFERTAKV
     PAKLATALAK TTSLAHGVWA RARADEDVAA FLPILQEVVD LRKEEAAAVA GNADPYDALL
     DDYEAGATGA QLAAMFDALR PRLVALRAAI LEQPAPAQLN QIFDEAGQLA LSHKLALAFG
     YDVQNGRIDQ AVHPFSSGSG LDVRITTRTS AHDPFGCFYS TVHEVGHAAY EQGIDAQHLL
     TPLGRGVSMG VHESQSRIYE NQLGRSRAFT GWLYGQMRDM FGDFGIADED AFFATVNRVS
     DGFIRTEADE VQYNLHVLLR FDLERALIAG DLAVGDLEAA WNDRFAADFG FAVDRPSNGV
     LQDVHWSEGL FGYFPTYSLG NVYAGCLHEA LRKAVPDLDS GLAKGDTSQA TGWLRDNLQK
     YGGLRTPVET ITHAAGGPPS EGPLLAYLED KFGAIYGL
//
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