ID   K6DHI8_9BACI            Unreviewed;       607 AA.
AC   K6DHI8;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN   ORFNames=BABA_12500 {ECO:0000313|EMBL:EKN67553.1};
OS   Neobacillus bataviensis LMG 21833.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX   NCBI_TaxID=1117379 {ECO:0000313|EMBL:EKN67553.1, ECO:0000313|Proteomes:UP000006316};
RN   [1] {ECO:0000313|EMBL:EKN67553.1, ECO:0000313|Proteomes:UP000006316}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21833T {ECO:0000313|Proteomes:UP000006316};
RX   PubMed=23087684;
RA   Heylen K., Keltjens J.;
RT   "Redundancy and modularity in membrane-associated dissimilatory nitrate
RT   reduction in Bacillus.";
RL   Front. Microbiol. 3:371-371(2012).
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:EKN67553.1}.
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DR   EMBL; AJLS01000074; EKN67553.1; -; Genomic_DNA.
DR   RefSeq; WP_007085513.1; NZ_AJLS01000074.1.
DR   AlphaFoldDB; K6DHI8; -.
DR   STRING; 1117379.BABA_12500; -.
DR   PATRIC; fig|1117379.3.peg.2598; -.
DR   eggNOG; COG1164; Bacteria.
DR   OrthoDB; 9766487at2; -.
DR   Proteomes; UP000006316; 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   Gene3D; 1.10.287.830; putative peptidase helix hairpin domain like; 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:UP000006316};
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          212..589
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   607 AA;  68914 MW;  D09FA19A5589C793 CRC64;
     MKKTVEKRLT RLEVPEEQTW NLNDLFPSDE AWETECELIE KQILGFNRFK GTLHTGAKAL
     LDCLSAQEQL SMRIIKAWTF ANLKQSADGA DPINQATSAK FSALRTKSFA ALSFINSEIL
     TLEEGKVAKY LEEEPELMAF KKNLEELLET KKHKLSPETE EALAALGDLQ GAPYQIYQMS
     KLADMDFAPI QDADGNEWPV SFALFENRYE FSADTEIRRK AYNSFVSSLL QYKNTMAATY
     AAEVNKQVTL ARLRKYESAT HMLLEPQQVS IDMYNNQIDT IFTELAPHMR RFAQLKKKVL
     GLDQMLFCDL KAPLDPDFNP ETTYEEASQV ILESLKVMGP EYCEIIERGF NERWVDLADN
     VGKSTGAFCS SPYGAHPYIL ITWQDNMRGC FTLAHEFGHA GHFFLANKYQ RIMNVRPSMY
     FVEAPSTLNE MLLGQHLLAK NEDKQMRRWV ILQLLGTYFH NFVTHLLEAE YQRRVYALAE
     EGKALTAKTL SEVTGAVLAE FWGDTVEIDE GAGLTWMRQP HYYMGLYPYT YSAGLTASTA
     VAQLIQEEGQ PAVDRWLEVL RAGGTMKPLE LLKHAGVDMS KPDPIKKAVA YVGSLIDELE
     RSYEIGA
//