ID   A0A0M0KFQ9_9BACI        Unreviewed;       617 AA.
AC   A0A0M0KFQ9;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN   ORFNames=AMD01_23085 {ECO:0000313|EMBL:KOO37407.1};
OS   Priestia koreensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Priestia.
OX   NCBI_TaxID=284581 {ECO:0000313|EMBL:KOO37407.1, ECO:0000313|Proteomes:UP000037558};
RN   [1] {ECO:0000313|Proteomes:UP000037558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16467 {ECO:0000313|Proteomes:UP000037558};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA   Shi H., Pan Z., Liu X.;
RT   "Fjat-14210 dsm16467.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Has oligopeptidase activity and degrades a variety of small
CC       bioactive peptides. {ECO:0000256|RuleBase:RU368091}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU368091};
CC       Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU368091};
CC   -!- SIMILARITY: Belongs to the peptidase M3B family.
CC       {ECO:0000256|RuleBase:RU368091}.
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:KOO37407.1}.
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DR   EMBL; LILC01000037; KOO37407.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M0KFQ9; -.
DR   STRING; 284581.AMD01_23085; -.
DR   PATRIC; fig|284581.3.peg.3477; -.
DR   Proteomes; UP000037558; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd09608; M3B_PepF; 1.
DR   Gene3D; 1.10.1370.20; Oligoendopeptidase f, C-terminal domain; 1.
DR   Gene3D; 1.20.140.70; Oligopeptidase f, N-terminal domain; 1.
DR   Gene3D; 1.10.287.830; putative peptidase helix hairpin domain like; 1.
DR   InterPro; IPR013647; OligopepF_N_dom.
DR   InterPro; IPR042088; OligoPept_F_C.
DR   InterPro; IPR045090; Pept_M3A_M3B.
DR   InterPro; IPR001567; Pept_M3A_M3B_dom.
DR   InterPro; IPR004438; Peptidase_M3B.
DR   NCBIfam; TIGR00181; pepF; 1.
DR   PANTHER; PTHR11804:SF79; MITOCHONDRIAL INTERMEDIATE PEPTIDASE; 1.
DR   PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR   Pfam; PF01432; Peptidase_M3; 1.
DR   Pfam; PF08439; Peptidase_M3_N; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368091};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU368091};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU368091};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU368091};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037558};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT   DOMAIN          135..195
FT                   /note="Oligopeptidase F N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08439"
FT   DOMAIN          222..603
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   617 AA;  70872 MW;  67059526B0AD0109 CRC64;
     MATVCLLLQV GATTSNGAEV NPQYENRSDI PSQYTWKLEE IYPNQKAWDK DVKSVVSQAD
     QFYHYKGTLS KSASHLKNIL EQYSTIMRKH DKIYIYASLK LHTNSSNAKL QSSTDQADHM
     SMNVMEKTSW LYTDISKLPM KKLKTYIDDP QLSAYKYVLE EMLRTKEHTL PEKMEELLLK
     TAPIASVPES TFTMLEKDIP FPSFMAASKT ALPLNRFNYS TYMESSDRVI REKAFQTYYH
     TLKQYQDTFA QTLGGQVKAS NAYAKIRHYP NAIAASLDSN NIPVRVYGGL IQSVHRGLPL
     LHRYMAVKKQ LLHVSPMHMY DLRAPLSKKD NQYVSFEEAK KRVIDGLSIW GEDYTDVLTK
     AFNERWIDVY STQDKHGGAY QWGSYDTHPY VLLNYRGTND DISTIAHELG HAMQSYYTKK
     AQPYLTAGYP TFLAEIASTM NEQLLWHDTY KKAKTKEEKI ALLCDRLEGF RTTLFRQTQF
     AEFEKIIHEK DQQGESLNAE AMSKVYLELN KKYYGPSIVS DPEIAVEWAK IPHLYNNFYV
     YQYATSFAAS IDLTEQILKE GRPAINRIHH HLLTAGGSEN PLSVLKKSGV DMSTDQPIRE
     AMKAFDETLT ELENLLK
//