ID   A0A0U5LJG6_9GAMM        Unreviewed;       680 AA.
AC   A0A0U5LJG6;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=oligopeptidase A {ECO:0000256|ARBA:ARBA00026100};
DE            EC=3.4.24.70 {ECO:0000256|ARBA:ARBA00026100};
GN   Name=prlC {ECO:0000313|EMBL:CUU22444.1};
GN   ORFNames=EM595_0207 {ECO:0000313|EMBL:CUU22444.1};
OS   Duffyella gerundensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Duffyella.
OX   NCBI_TaxID=1619313 {ECO:0000313|EMBL:CUU22444.1, ECO:0000313|Proteomes:UP000059419};
RN   [1] {ECO:0000313|Proteomes:UP000059419}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Blom J.;
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of oligopeptides, with broad specificity. Gly or
CC         Ala commonly occur as P1 or P1' residues, but more distant residues
CC         are also important, as is shown by the fact that Z-Gly-Pro-Gly-|-Gly-
CC         Pro-Ala is cleaved, but not Z-(Gly)(5).; EC=3.4.24.70;
CC         Evidence={ECO:0000256|ARBA:ARBA00024603};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU003435};
CC       Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC   -!- SIMILARITY: Belongs to the peptidase M3 family.
CC       {ECO:0000256|ARBA:ARBA00006040, ECO:0000256|RuleBase:RU003435}.
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DR   EMBL; LN907827; CUU22444.1; -; Genomic_DNA.
DR   RefSeq; WP_067426963.1; NZ_LN907827.1.
DR   AlphaFoldDB; A0A0U5LJG6; -.
DR   STRING; 1619313.EM595_0207; -.
DR   KEGG; ege:EM595_0207; -.
DR   PATRIC; fig|1619313.3.peg.214; -.
DR   OrthoDB; 9773538at2; -.
DR   Proteomes; UP000059419; Chromosome 1.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd06456; M3A_DCP; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 1.10.1370.10; Neurolysin, domain 3; 1.
DR   InterPro; IPR034005; M3A_DCP.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR024077; Neurolysin/TOP_dom2.
DR   InterPro; IPR024080; Neurolysin/TOP_N.
DR   InterPro; IPR045666; OpdA_N.
DR   InterPro; IPR045090; Pept_M3A_M3B.
DR   InterPro; IPR001567; Pept_M3A_M3B_dom.
DR   PANTHER; PTHR43660; DIPEPTIDYL CARBOXYPEPTIDASE; 1.
DR   PANTHER; PTHR43660:SF1; DIPEPTIDYL CARBOXYPEPTIDASE; 1.
DR   Pfam; PF01432; Peptidase_M3; 1.
DR   Pfam; PF19310; TOP_N; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003435};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU003435};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU003435};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW   Reference proteome {ECO:0000313|Proteomes:UP000059419};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN          31..148
FT                   /note="Oligopeptidase A N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF19310"
FT   DOMAIN          222..677
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   680 AA;  76743 MW;  5366EF82C539D526 CRC64;
     MTNPLLQSFT LPPFSDIKPE HVVPAVTAAL DECRQMVEKV VAQGAPYTWD NLVQPLAEVD
     DRLGRIFSPV SHLNSVKNSP ELREVYEQTL PLLSEYGTWV GQHEGLYQAY RNLKEGEHYA
     TLSLAQKKAV DNALRDFELS GIGLSKEKQK RYGEIAARLS ELGSTYSNNV LDATMGWSKL
     ITDVSELSGM PESALDAAKA QAEAKEQQGW LLTLDIPSYL PVMTYCDNQA LREEMYRAYA
     TRASDQGPNA GKWDNSEVMA EELALRHELA QLLGFDSYAD KSLATKMAEN PAQVTDFLTD
     LAKRARPQAE KELAQLQAFA QKEHGISELQ PWDLTYYGEK QKQHLYTISD EQLRPYFPEE
     RAVNGLFEVV KRIYGITAKE RKDVDVYHPD VRFFDLFDES GELRGSFYLD LYARENKRGG
     AWMDDCVGMM RLADGSLQKP VAYLTCNFNR PLNGKPALFT HDEVTTLFHE FGHGLHHMLT
     GIDTPGVSGI SGVPWDAVEL PSQFMENWCW EPEALAFISG HYETGEPLPQ ALLDKMLAAK
     NYQAALFILR QLEFGLFDFR LHAEFDPAKG AQILEMLKAI KKLVAVVPSP EWGRFPHAFS
     HIFAGGYAAG YYSYLWADVL AADAYSRFRE EGIFNRETGQ SFLDNILTRG GSEEPMELFK
     RFRGREPQLD AMLDHYGIEG
//