ID   A0A1E5LAV9_9BACI        Unreviewed;       636 AA.
AC   A0A1E5LAV9;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, 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=BFG57_06185 {ECO:0000313|EMBL:OEH91203.1};
OS   Bacillus solimangrovi.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1305675 {ECO:0000313|EMBL:OEH91203.1, ECO:0000313|Proteomes:UP000095209};
RN   [1] {ECO:0000313|EMBL:OEH91203.1, ECO:0000313|Proteomes:UP000095209}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GH2-4 {ECO:0000313|EMBL:OEH91203.1,
RC   ECO:0000313|Proteomes:UP000095209};
RA   Lim S., Kim B.-C.;
RT   "Genome of Bacillus solimangrovi GH2-4.";
RL   Submitted (AUG-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:OEH91203.1}.
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DR   EMBL; MJEH01000063; OEH91203.1; -; Genomic_DNA.
DR   RefSeq; WP_069718719.1; NZ_MJEH01000063.1.
DR   AlphaFoldDB; A0A1E5LAV9; -.
DR   STRING; 1305675.BFG57_06185; -.
DR   OrthoDB; 9766487at2; -.
DR   Proteomes; UP000095209; 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:UP000095209};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT   DOMAIN          152..215
FT                   /note="Oligopeptidase F N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08439"
FT   DOMAIN          240..621
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   636 AA;  72353 MW;  9E5988AA25B55175 CRC64;
     MKKKILSSLT AVAIATSVIS TPGIPLNPVK VEAAQDALKP TYETRSEIPD EFKWKLDHIY
     ETKAAWEADV KKVEQMANDF TAHQGKISKS QDSLVKALNS YSDLMRLTDK VYVYANMSFD
     VNSTNPDLQE LADKAGNVLT LVSEKTSWFA PEVAAMQANK LEKYLKSDEM KPYAMFVGDI
     IREKEHTLST ELEKLLAQIS PLSSNPEDVY GALMTNIKFP MIKDETGKDI QLSRSNFISY
     MESENRNVRK AAFEGFYSTM EKYQDTFAQT ISGNVKAHNI NANVRNYDSA LEASLSANNV
     PVEVYDNLVK TVNDNLPLLH RYMELKKKLL EVDELHMYDI YTPIVDYQAD YIPYSKAKEM
     VKNGLKPLGP EVQSIIDKSF NEGWVDVYST PDKRSGAYQW GAYDTHPYML LNYQGTLDDT
     YTIAHEVGHA LQSHYTNAKQ PYMTSNYPIF TAEVASTLNE ALMFKEMYNN AKTKEEKLYL
     LNQYLENFRG TLFRQTQFAE FEKAIHDMDK AGESLNAEAL KKLYRDINAK YYGKTMISDE
     EIAMEWARVP HFYYNFYVYQ YATSFAASQA LSKQVMEEGD VAVKRITENF LSAGSSDAPL
     EVLKAAGVDM STAKPIEDAM KVFEQTLDEM EKLLEE
//