ID   A0A344PGC9_9RHOB        Unreviewed;       497 AA.
AC   A0A344PGC9;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=Metal-dependent carboxypeptidase {ECO:0000256|PIRNR:PIRNR006615};
DE            EC=3.4.17.19 {ECO:0000256|PIRNR:PIRNR006615};
GN   ORFNames=DRW48_00820 {ECO:0000313|EMBL:AXC48434.1};
OS   Paracoccus suum.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=2259340 {ECO:0000313|EMBL:AXC48434.1, ECO:0000313|Proteomes:UP000252023};
RN   [1] {ECO:0000313|Proteomes:UP000252023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC2-6 {ECO:0000313|Proteomes:UP000252023};
RA   Heo J., Kim S.-J., Kwon S.-W.;
RT   "Genome sequencing of Paracoccus sp. SC2-6.";
RL   Submitted (JUL-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}.
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DR   EMBL; CP030918; AXC48434.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A344PGC9; -.
DR   KEGG; pars:DRW48_00820; -.
DR   OrthoDB; 9772308at2; -.
DR   Proteomes; UP000252023; 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:AXC48434.1}; 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:UP000252023};
KW   Zinc {ECO:0000256|PIRSR:PIRSR006615-1}.
FT   ACT_SITE        254
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006615-2"
FT   BINDING         253
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
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         292
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
SQ   SEQUENCE   497 AA;  55750 MW;  670AAB84E3CE3AAB CRC64;
     MGQVNDLLNA KSVLSWDARV MMPRGGAETR AKQVATLSVL ARDTLVADET RRLLDAAQAE
     IQSKDADSVE ATVCAQVREA LDYHDRIPAE LIRRRTEMGS IGQEIWAEAR AKDDFAMFAP
     LLADTVALNR EMAEHIGYAE HPYDALMYRF EPGETVASLQ PLFGRLREAL RPLLQTVMSR
     TAPDVEFLRR PFPVDEQLAF GRTMAQRLGY DLDRGRLDTT VHPFEVSFTR NDVRITSRTN
     ENWMPMCLFG CLHEAGHALY EQNCDPAFTR TPLATDLVGL YAVAGVSFGA HESQSRLFEN
     HVGRSRAFWE ANFGTARDAF PEQLADVDAE AFWRGVNRVA PGLIRVEADE LSYDFHIMLR
     VDIEAGLIDG SLKVEDLPEI WNARIRQDLG LEVPNNRMGV LQDVHWSSGQ IGTFCNYTIG
     NVMAGQLYEA ATKDADVAAG VAAADYGPLL GWMVKNVHQH GRRYERNELL RRATGRTLDP
     EPYIAQLTQK YSEIYGI
//