ID   F5LM21_9BACL            Unreviewed;       633 AA.
AC   F5LM21;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN   Name=pepF {ECO:0000313|EMBL:EGL16584.1};
GN   ORFNames=HMPREF9413_5858 {ECO:0000313|EMBL:EGL16584.1};
OS   Paenibacillus sp. HGF7.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=944559 {ECO:0000313|EMBL:EGL16584.1, ECO:0000313|Proteomes:UP000003445};
RN   [1] {ECO:0000313|EMBL:EGL16584.1, ECO:0000313|Proteomes:UP000003445}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HGF7 {ECO:0000313|EMBL:EGL16584.1,
RC   ECO:0000313|Proteomes:UP000003445};
RA   Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
RL   Submitted (FEB-2011) 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:EGL16584.1}.
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DR   EMBL; AFDH01000092; EGL16584.1; -; Genomic_DNA.
DR   AlphaFoldDB; F5LM21; -.
DR   OrthoDB; 9766487at2; -.
DR   Proteomes; UP000003445; 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:UP000003445};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..633
FT                   /note="Oligoendopeptidase F"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038893087"
FT   DOMAIN          150..218
FT                   /note="Oligopeptidase F N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08439"
FT   DOMAIN          239..619
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   633 AA;  72510 MW;  F450B4CB7AAE182C CRC64;
     MRLLPIALMA GLLVSTLVPG SGAHPAANPK SSVRRVPMNQ IPVRKDVPAE HRWKLEDLFA
     NQEAWNKEYN ETKEALGKIG QFHGKLSDPA AVKQCFELED DISLHTERLY VYSNMKHHED
     MTDPTYQALS DKAQKLSVEV SQALSFISPE IVSLSEEQLK ALVENKDLAP YKTTLEEMIR
     QKPHVLSKEE EALLAMAGNM SGAPSNIFGM INNADMKFPK VKNENGEEAE LTHGSYIQFL
     ESRDREVREQ AFKAVYETYA KQKNTIAATL SSNINKNIFY SQARKYPSVL EMSLFGDNIK
     PEVYTNLIET IHESLPLLQR YMKLRKKLLK LDELHMYDLF VPLVDDLKMK VTYDEAKETI
     KESLAPLGKS YVETLEKGYN DGWIDIYENQ NKRSGAYSWG AYGTHPYVLL NHKENLNSMF
     TLAHEMGHAI HSYLSDENQP YRDAQYTIFL AEVASTLNEA LLMDYLLKHT DDPKKKLYLL
     TYYADQFRTT VFRQTMFAEF EKITHEKMEK GESLTAQEFS KIYYDLNTLY HGKEMVVDKD
     IEMEWARIPH FYNSFYVYKY ATGFSAATSF SKQILDEGQP AVERYLGFLK SGGSDYSINI
     LKKAGVDMST PEPIKQAMSV FASVLDQMEE LTK
//