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Entry: I4FP18_MICAE
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ID   I4FP18_MICAE            Unreviewed;       683 AA.
AC   I4FP18;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   24-JAN-2024, entry version 46.
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:CCH97393.1};
GN   ORFNames=MICAB_3240005 {ECO:0000313|EMBL:CCH97393.1};
OS   Microcystis aeruginosa PCC 9717.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Microcystaceae; Microcystis.
OX   NCBI_TaxID=1160286 {ECO:0000313|EMBL:CCH97393.1, ECO:0000313|Proteomes:UP000003172};
RN   [1] {ECO:0000313|EMBL:CCH97393.1, ECO:0000313|Proteomes:UP000003172}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9717 {ECO:0000313|EMBL:CCH97393.1,
RC   ECO:0000313|Proteomes:UP000003172};
RA   Genoscope - CEA;
RL   Submitted (APR-2012) 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}.
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:CCH97393.1}.
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DR   EMBL; CAII01000251; CCH97393.1; -; Genomic_DNA.
DR   RefSeq; WP_002759920.1; NZ_HE972705.1.
DR   AlphaFoldDB; I4FP18; -.
DR   HOGENOM; CLU_001805_4_1_3; -.
DR   Proteomes; UP000003172; Unassembled WGS sequence.
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; 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; PTHR11804:SF83; LD37516P; 1.
DR   PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 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   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN          29..151
FT                   /note="Oligopeptidase A N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF19310"
FT   DOMAIN          231..682
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   683 AA;  76877 MW;  81B2A5196A073B99 CRC64;
     MTNTSNPLLA GQGLPAFDQI QPGLIVPGMT QLLQELAREL TDLEAQIAPT WEKLVEPLTR
     IEERLSWSWG IIGHLMGVKN SPELRQAYET VQPQVVEFIS RLSQSKPIYE AFSSLRQGES
     WGQLDEAQQR IVEASLRDAQ LAGVGLVGEK KDRFNAIQLE LAEITTKFSN NLLDATKAFQ
     LKLTTPEDIA GLPPSLLSLA AQTARGQGET NASTETGPWV ITLDFPSYFP FMKYSDNREL
     REKLYKAYVS RADLGELDNN PLIDRILQLR QEQAHLLGYS TYAEVSLARK MANSVDEIEK
     LLDNLRQVSY KAAKQDLEAL KTFAGTDDLK HWDIAYWSEK QRQAKFNFSA EELRPYFPLP
     RVLEGIFSLA KRIFGVEIIA TDGKAPIWHP DVRYFQINDE KGEKIAYFYL DAYSRPAEKR
     GGAWMDVCIG RAKTGAEVRL PVAYLICNQT PPVDGNPSLM TFEEVTTLFH EFGHGLQHML
     TTVDYSGAAG INNVEWDAVE LPSQFMENWC YDRPTLMSMA KHYETGETLP EHYYQKLLLA
     KNYMSGSAML RQLHLSLVDL ELHHRYQPNG GETPKQVRQR LAATTTIIPP LPEDAFLCSF
     GHIFAGGYAA GYYSYKWAEV LSADAFAAFE EVGLDNEEAV KAIGRRFRDT VLAMGGSSHP
     MNVFKAFRGR EPSTEPLLRH SGL
//
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