ID A0A2T5BT82_9RHOB Unreviewed; 490 AA.
AC A0A2T5BT82;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Metal-dependent carboxypeptidase {ECO:0000256|PIRNR:PIRNR006615};
DE EC=3.4.17.19 {ECO:0000256|PIRNR:PIRNR006615};
GN ORFNames=C8N32_10517 {ECO:0000313|EMBL:PTN02647.1};
OS Rhodovulum imhoffii.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodovulum.
OX NCBI_TaxID=365340 {ECO:0000313|EMBL:PTN02647.1, ECO:0000313|Proteomes:UP000243859};
RN [1] {ECO:0000313|EMBL:PTN02647.1, ECO:0000313|Proteomes:UP000243859}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18064 {ECO:0000313|EMBL:PTN02647.1,
RC ECO:0000313|Proteomes:UP000243859};
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 -!- 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 -!- 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:PTN02647.1}.
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DR EMBL; QAAA01000005; PTN02647.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T5BT82; -.
DR OrthoDB; 9772308at2; -.
DR Proteomes; UP000243859; Unassembled WGS sequence.
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:PTN02647.1}; 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 Reference proteome {ECO:0000313|Proteomes:UP000243859};
KW Zinc {ECO:0000256|PIRSR:PIRSR006615-1}.
FT ACT_SITE 258
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-2"
FT BINDING 257
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT BINDING 261
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT BINDING 287
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
SQ SEQUENCE 490 AA; 54565 MW; 69693AED3151102F CRC64;
MTAYDDLLAH ERETQALSQV MGRLGWDQET MMPRGAAQQR AEEMGALETV LHARRTEPRI
GEWLNAIDEA ALDAVGRAQL RHIRRSYARA TRLPRTLSAE IAHVTSRSQG IWAEARAADD
VGHFLPVFRE VVRLKREEAA ALAEGREAYD ALLDDYEPGA TADSIAGMFD RMRPRLVQLR
ERIMGTERGQ PGLSGHFDGA IQIDLSREIA TRFGYDWRHG RLDRSVHPFT SGSGADVRIT
TRVDEKEPLG CLYSVLHEVG HGAYEQAIDP AYALTPLGEG ASMGVHESQS RIYENQLGRS
RAFTGWLYGR MADLFGVTGG AEAFYAAVNR VHAGFIRTEA DEVHYNLHIM MRFDLERDLI
LGKLEPEDLE EAWNVRFVTD FGVAVDRPSN GVLQDVHWPV GLFGYFPTYT LGNVYAGCLH
LAMRAALPSL DADLAQGEVT AVTSWLRDTV QRHGGLYLPA DVIEHACGFP PTEKPLLDYL
EAKYSALYGV
//
