ID A0A428JPC3_9RHOB Unreviewed; 492 AA.
AC A0A428JPC3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 03-MAY-2023, entry version 9.
DE RecName: Full=Metal-dependent carboxypeptidase {ECO:0000256|PIRNR:PIRNR006615};
DE EC=3.4.17.19 {ECO:0000256|PIRNR:PIRNR006615};
GN ORFNames=EJA01_06660 {ECO:0000313|EMBL:RSK35072.1};
OS Rhodovulum robiginosum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodovulum.
OX NCBI_TaxID=68292 {ECO:0000313|EMBL:RSK35072.1, ECO:0000313|Proteomes:UP000275159};
RN [1] {ECO:0000313|EMBL:RSK35072.1, ECO:0000313|Proteomes:UP000275159}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12329 {ECO:0000313|EMBL:RSK35072.1,
RC ECO:0000313|Proteomes:UP000275159};
RA Gupta D., Guzman M.S., Bose A.;
RT "Draft genome sequence of a marine photoferrotrophic bacterium, Rhodovulum
RT robiginosum.";
RL Submitted (DEC-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:RSK35072.1}.
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DR EMBL; RWGU01000044; RSK35072.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A428JPC3; -.
DR OrthoDB; 9772308at2; -.
DR Proteomes; UP000275159; 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:RSK35072.1}; 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:UP000275159};
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 492 AA; 54110 MW; 608A9F1D795D4593 CRC64;
MSAYDDLLDH HRETEALAEV MGRLGWDQET VMPRGGAQQR AEEMGALEGV LHRRRTDPRI
GAWLASIDEG GLGAAERAQL RHIRRSYSRA MRLPETLSAE LARVTSRAQG IWAEARAADD
VAHFLPTLTE VIRLKREEAA ALAEGGDLYD ALLDDYEPGA TGQGIAEMFD RMRPRLVSLR
ERIMGSGRDH PALSGRYGAE AQLTLAREIA THFGYDWRHG RLDSSVHPFT SGSGTDVRIT
TRVDEAEPLG CLYSTLHEVG HGAYEQGIDP AFHLTPVGHG VSMGVHESQS RIYENQLGRS
AAFCGWLYAR FGEVFGQAGA ADAQAFYAAV NRVHSGYIRT EADEVHYNLH IMLRFDLERD
LIAGRLEAAD LEEAWNTRFA ADFGVAVDRP ANGVLQDVHW SVGLFGYFPT YTLGNVYAGC
LYQALRAAVP DLDAGLARGH AEPATDWLRA HVQRPGGLYA PAEVIERACG FAPHEGPLLD
YLDTKFGAVY GL
//
