ID   A0A200JCL3_9ENTE        Unreviewed;       605 AA.
AC   A0A200JCL3;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN   ORFNames=A5889_000421 {ECO:0000313|EMBL:OUZ34946.1};
OS   Enterococcus sp. 9D6_DIV0238.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=1834192 {ECO:0000313|EMBL:OUZ34946.1, ECO:0000313|Proteomes:UP000196151};
RN   [1] {ECO:0000313|EMBL:OUZ34946.1, ECO:0000313|Proteomes:UP000196151}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9D6_DIV0238 {ECO:0000313|EMBL:OUZ34946.1,
RC   ECO:0000313|Proteomes:UP000196151};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genomic Center for Infectious Diseases;
RA   Earl A., Manson A., Schwartman J., Gilmore M., Abouelleil A., Cao P.,
RA   Chapman S., Cusick C., Shea T., Young S., Neafsey D., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Enterococcus sp. 9D6_DIV0238.";
RL   Submitted (MAY-2017) 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:OUZ34946.1}.
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DR   EMBL; NIBQ01000001; OUZ34946.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A200JCL3; -.
DR   Proteomes; UP000196151; 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:UP000196151};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT   DOMAIN          118..187
FT                   /note="Oligopeptidase F N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08439"
FT   DOMAIN          208..588
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   605 AA;  69758 MW;  8331E02728649C2D CRC64;
     MMSGAKQLPE RSTLPIEMTW DLTKIFKDDQ AFDDAYQVLT KELQEVEKYK GTLDQGSTAF
     LNSIEMLLKV YRQIEVIYVY AHLKNDQDTS NATYQALYSR ASSLFAQVSE AVAWFEPELL
     SLNDDLIWGY FAEKPELEIY RHFVENILNE RPHILSAEQE ALLAGASEIF GASSDTFSIL
     NNADLKFPVI EDENGEKVQL THGVYGQLME NIDRDVREKA FKALYSVYDQ FQNTFAQTLS
     SHVKAHNYKA KIRNYPSARA AALSSNHIPE SVYDTLLDVV NKHLPLLHRY VALRKRLLNL
     EELHMYDMYT PILGEASIKY SYEEAKEKAL AALKPMGEEY LTIVETAFND RWIDVIENQG
     KRSGAYSSGA YDTAPYILMN WHDSLDQLYT LVHEMGHSVH SYFTRNNQPY VYGDYSIFLA
     EIASTTNENI LTEHLLETET DPRIRAYVLN HYLDGFKGTI FRQTQFAEFE HFIHTEDAKG
     TPLTSEYLSE YYEQLNAKFY GPDVVKDPEI TLEWTRIPHF YYNYYVYQYA TGFSAASALA
     NKILAEEPQA LENYLTYLKS GSSDYPIEVM KKAGVDMTQP QYIEDAMKVF ETRLNELEKL
     VESME
//