ID   A0A0L0QTY7_VIRPA        Unreviewed;       606 AA.
AC   A0A0L0QTY7;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN   ORFNames=AFK71_04070 {ECO:0000313|EMBL:KNE21987.1};
OS   Virgibacillus pantothenticus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX   NCBI_TaxID=1473 {ECO:0000313|EMBL:KNE21987.1, ECO:0000313|Proteomes:UP000036780};
RN   [1] {ECO:0000313|Proteomes:UP000036780}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26 {ECO:0000313|Proteomes:UP000036780};
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-10053 dsm26.";
RL   Submitted (JUL-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:KNE21987.1}.
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DR   EMBL; LGTO01000004; KNE21987.1; -; Genomic_DNA.
DR   RefSeq; WP_050350270.1; NZ_LGTO01000004.1.
DR   AlphaFoldDB; A0A0L0QTY7; -.
DR   GeneID; 66869728; -.
DR   PATRIC; fig|1473.5.peg.3770; -.
DR   OrthoDB; 9766487at2; -.
DR   Proteomes; UP000036780; 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; cd09609; 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   InterPro; IPR034009; M3B_PepF_4.
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; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR   PANTHER; PTHR11804:SF45; SIMILAR TO OLIGOENDOPEPTIDASE; 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:UP000036780};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT   DOMAIN          114..183
FT                   /note="Oligopeptidase F N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08439"
FT   DOMAIN          209..585
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   606 AA;  68827 MW;  89BF817003D3B7AC CRC64;
     MVKRQKRSEV PEKLIWDLTD LFSTHTDWEN ELQAIQQDVE QFSSYKGELG KEASTLHQCM
     EAYETFQKRV IRVATYANLR NSTDGTDPTR QQDSAKVAQA LAKIQAQLSF IQSEILEIPT
     ETIGEFVKQH PALATYRKML ADLIEKKPYT LSPQIEELLA ALSEVHNAPY MIYQRSKSSD
     MVFASISDEQ GNELPMSAAL YEDRYELTAD NTARRNAYHS FVQTLQQYQH TYAAIYATEV
     TKQVVMAQQR HYDNVTDMLL HPQQVTTDMY HNQLDVIQTE LAPHMQRFAR LKQEQLGLDE
     LYMCDLKAPL DPSFNPVTTY EEATATIIEA LGVMGEDYQQ VMKQAIENRW IDLADNVGKA
     TGAFCSSPYG VHPYILITWT DTMRGAFVLA HELGHAGHFY FAGKAQTLFN TRPSTYFIEA
     PSTLNELLLA HHLLAKTDDE RMKRWIITQL LGTYYHNFVT HLLEAEFQRR VYTLAESGTP
     LTAKVLSEQK IEALANFWGD TVTIDEGAGL TWMRQPHYYM GLYPYTYSAG LTVSTAVAQT
     IQKEGAPAAK RWIEVLESGG TLKPLDLIQK AGVDMSTPDA IKQAVAFVGS LVDQLETSYR
     EEKQER
//