ID   A0A1S2R073_9BACI        Unreviewed;       605 AA.
AC   A0A1S2R073;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN   ORFNames=BIV60_18560 {ECO:0000313|EMBL:OIK11156.1};
OS   Bacillus sp. MUM 116.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1678002 {ECO:0000313|EMBL:OIK11156.1, ECO:0000313|Proteomes:UP000180019};
RN   [1] {ECO:0000313|EMBL:OIK11156.1, ECO:0000313|Proteomes:UP000180019}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MUM 116 {ECO:0000313|EMBL:OIK11156.1,
RC   ECO:0000313|Proteomes:UP000180019};
RA   Lee L.-H., Ser H.-L.;
RT   "Genome sequence of Bacillus sp. MUM 116.";
RL   Submitted (OCT-2016) 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:OIK11156.1}.
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DR   EMBL; MLYR01000081; OIK11156.1; -; Genomic_DNA.
DR   RefSeq; WP_071357198.1; NZ_MLYR01000081.1.
DR   AlphaFoldDB; A0A1S2R073; -.
DR   STRING; 1678002.BIV60_18560; -.
DR   OrthoDB; 9766487at2; -.
DR   Proteomes; UP000180019; 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:UP000180019};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT   DOMAIN          120..189
FT                   /note="Oligopeptidase F N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08439"
FT   DOMAIN          210..590
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   605 AA;  69555 MW;  C6E6EE6630647AFC CRC64;
     MANETAVKTL PARSEILVEE TWKLEDIFAN DETWEKEFQE VKTQIPGIKE FVGKLGESAE
     TLYKALQAQD QILERLGKLF AYSHMRYDQD TTNSFYQGLD DRIKNLYSQA GSALAFIVPE
     LLSIDENKLK GFLSEKPELK LYEHAIEEIN LQRPHVLSAE EEALLAEAGE VMDASSNTFG
     MLNNADLEFP SIKDENGEEI EITHGRYIRF LESSDQRVRS DAFKAVYETY GNFRNTFAST
     LSGNVKKDNF NARIRKYHSA RQAALTANNI PESVYDNLVN TVNEQLPLLH RYVKLRKKVL
     GLKELHMYDL YTPLVKDVKM EIKYNEAKDI VLKGLAPLGE EYGKVLEEGF ENRWIDVHEN
     KGKRSGAYSS GSYGTNPYIL LNWQDNVNNL FTLAHELGHS VHSYYTRKSQ PYPYGNYSIF
     VAEVASTCNE ALLNDHLLKT IDDEQKRIYL LNHYLEGFRG TVFRQTMFAE FEHLIHQKLQ
     NNEALTADLL TKEYYKLNKK YFGEEDIVID EEIGLEWSRI PHFYYNYYVY QYATGFSAAT
     ALSKQILEEG EPAVKRYIEF LSAGSSDYPI EVLKKAGVDM TSSQPVKDAC KVFEEKLNEL
     EQLLS
//