ID   I0K247_9BACT            Unreviewed;       709 AA.
AC   I0K247;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=oligopeptidase A {ECO:0000256|ARBA:ARBA00026100};
DE            EC=3.4.24.70 {ECO:0000256|ARBA:ARBA00026100};
GN   ORFNames=FAES_0186 {ECO:0000313|EMBL:CCG98200.1};
OS   Fibrella aestuarina BUZ 2.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC   Fibrella.
OX   NCBI_TaxID=1166018 {ECO:0000313|EMBL:CCG98200.1, ECO:0000313|Proteomes:UP000011058};
RN   [1] {ECO:0000313|EMBL:CCG98200.1, ECO:0000313|Proteomes:UP000011058}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BUZ 2T {ECO:0000313|Proteomes:UP000011058};
RX   PubMed=22689241; DOI=10.1128/JB.00550-12;
RA   Filippini M., Qi W., Blom J., Goesmann A., Smits T.H., Bagheri H.C.;
RT   "Genome Sequence of Fibrella aestuarina BUZ 2T, a Filamentous Marine
RT   Bacterium.";
RL   J. Bacteriol. 194:3555-3555(2012).
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; HE796683; CCG98200.1; -; Genomic_DNA.
DR   RefSeq; WP_015329300.1; NC_020054.1.
DR   AlphaFoldDB; I0K247; -.
DR   KEGG; fae:FAES_0186; -.
DR   PATRIC; fig|1166018.3.peg.188; -.
DR   eggNOG; COG0339; Bacteria.
DR   HOGENOM; CLU_001805_4_0_10; -.
DR   OrthoDB; 9773538at2; -.
DR   Proteomes; UP000011058; Chromosome.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd06456; M3A_DCP; 1.
DR   Gene3D; 1.10.1370.40; -; 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; 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   Carboxypeptidase {ECO:0000313|EMBL:CCG98200.1};
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:UP000011058};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN          60..178
FT                   /note="Oligopeptidase A N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF19310"
FT   DOMAIN          253..704
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   709 AA;  79746 MW;  6B910FCF5F89F31F CRC64;
     MKVTLLLALP VVMTALISGR PALDPPAGNP FFSAYTTPFG VPPFDQIKPE HFEPAIDEGI
     KQQTAEIATI TQQKAAPTFA NTVEALEASG DLLRRVNTVL GNLNGANTND QLQKIAQTVA
     PKLAKHSDDI MLNPVLFSRV KAVYEQRSKL NLSGDQQRLL EKMYKNFVRN GAALTAEKQE
     RLRKINGELS VLTLKFGQNL LAENNAYTLV IDKQDDLSGL PASVVATAAE EAKRRKLDGK
     WVFTLQNPSI MPFLQYADNR KLREQLLRAY LERGNHNDER DNKAIMANMV ALRAEKAQLL
     GYDNHAAYVL EESMAQTPAK VAELLNQLWT ATVPVAKQEA KELQAIMDKD PAAGGAKLAS
     WDWRYYAEKL RKEKYALDEQ ELRPYFPLEG VREGIFMLTG RLYGLKFERR TDIPVYHEEA
     TVYEVKEADG RHIGLIYMDF FPRSSKRGGA WMTSYRRQEV ENGKKITPVV SIVCNFSKPT
     GNVPALLTQN EVSTFFHEFG HALHGLLSNV HYGSQSGTSV PRDFVELPSQ IMENWAVEPE
     MLKLFAKHYQ TGAVIPDALV DKIKQSSLFN QGFETSEYLA ASLLDMSYHT LKPGQTPTDV
     LAFEKQAMDK IGLIDQIPPR YRSTYFQHIF SGGYSAGYYS YIWSAVLDAD AFEVFKQKGL
     FDPKSAQSFR KNVLERGGTE DPMTLYRKFR GAEPDIKPLL RRRGLLKAI
//