ID   A0A0X3U1W1_9RHOB        Unreviewed;       489 AA.
AC   A0A0X3U1W1;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Metal-dependent carboxypeptidase {ECO:0000256|PIRNR:PIRNR006615};
DE            EC=3.4.17.19 {ECO:0000256|PIRNR:PIRNR006615};
GN   ORFNames=AVO44_01360 {ECO:0000313|EMBL:KUJ81957.1};
OS   Ruegeria profundi.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Ruegeria.
OX   NCBI_TaxID=1685378 {ECO:0000313|EMBL:KUJ81957.1, ECO:0000313|Proteomes:UP000053690};
RN   [1] {ECO:0000313|Proteomes:UP000053690}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZGT108 {ECO:0000313|Proteomes:UP000053690};
RA   Zhang G., Stingl U.;
RL   Submitted (DEC-2015) 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:KUJ81957.1}.
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DR   EMBL; LQBP01000001; KUJ81957.1; -; Genomic_DNA.
DR   RefSeq; WP_068331532.1; NZ_LQBP01000001.1.
DR   AlphaFoldDB; A0A0X3U1W1; -.
DR   STRING; 1685378.AVO44_01360; -.
DR   OrthoDB; 9772308at2; -.
DR   Proteomes; UP000053690; 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   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        255
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006615-2"
FT   BINDING         254
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT   BINDING         258
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT   BINDING         284
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
SQ   SEQUENCE   489 AA;  54029 MW;  F62580E29911FA0A CRC64;
     MSAYDELMAF QRETSALGQI AGRLGWDQET VMPRGAAPQR AEEMAAIEAV LHARRSDPRV
     AEWLEQADPQ DDAARAQLRD IRRTYERTVK VPADLAKAIA RVTSAAQGTW AQARADEDVA
     AFLPVLTEVV ALKREEGAAL AQGGDVYDAM VEDYEPYTTG AQISEIFDQM RPRLVALRAA
     VLEKPAPQVL AGKFDELTQM RLSQKLATTF GYDLNTGRMD KAVHPFSSGS GLDVRITTRT
     SETDPFNCFY STIHEVGHAA YEQGIDLAYA LTPLGQGVSM GVHESQSRIY ENQLGRSRAF
     TGWLYDQMID AFGEFGISDP DAFYATVNGV HNGYIRTEAD EVQYNLHIML RFDLERALMS
     GDLNVNDLET AWNDRFKADF GYAIDKPSNG CLQDVHWSVG LFGYFPTYSL GNVYAGCLHQ
     ALRAAVPDLD AQLATGDTSG ATGWLRENLQ RHGGLYTPRE TIQRACGMQA GPEPFLSYLE
     EKFGALYGL
//