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Database: UniProt
Entry: Q8XKE7_CLOPE
LinkDB: Q8XKE7_CLOPE
Original site: Q8XKE7_CLOPE 
ID   Q8XKE7_CLOPE            Unreviewed;       599 AA.
AC   Q8XKE7;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 107.
DE   RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN   Name=pepF {ECO:0000313|EMBL:BAB81159.1};
OS   Clostridium perfringens (strain 13 / Type A).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195102 {ECO:0000313|EMBL:BAB81159.1, ECO:0000313|Proteomes:UP000000818};
RN   [1] {ECO:0000313|EMBL:BAB81159.1, ECO:0000313|Proteomes:UP000000818}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13 / Type A {ECO:0000313|Proteomes:UP000000818};
RX   PubMed=11792842; DOI=10.1073/pnas.022493799;
RA   Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA   Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT   "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT   eater.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
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}.
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DR   EMBL; BA000016; BAB81159.1; -; Genomic_DNA.
DR   RefSeq; WP_011010455.1; NC_003366.1.
DR   AlphaFoldDB; Q8XKE7; -.
DR   SMR; Q8XKE7; -.
DR   STRING; 195102.gene:10490717; -.
DR   KEGG; cpe:CPE1453; -.
DR   HOGENOM; CLU_021290_2_0_9; -.
DR   Proteomes; UP000000818; Chromosome.
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:UP000000818};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT   DOMAIN          116..185
FT                   /note="Oligopeptidase F N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08439"
FT   DOMAIN          207..585
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   599 AA;  69581 MW;  BAC7501015AF1A4A CRC64;
     MSEVKKLRIR DEIPESDKWR IDKIYETPAK WNEELNKLKE EAPKLKDFEG KLGNKEDLKA
     FLLLNEKLSR KLGKLYVYAH MRSHEDTSNP EMQSLVNKID PYSAEFSSYT AYFVPEILSL
     KEGTIENFIN EDKDLKQYKI YFEMILNEKP HILSKEVESV LASVSDCLGA PESIYSMLTN
     SDMTFGEIVD ESSRKVELTE GNYISFIKSK DRKVREAAFK LLFGTYKKYE NTLATSLTSS
     IKNFVFESKT RKYNSSLEAS LKPNNIPVEV YYNALKTVDE NMDALHRYVR IKKKLLNLEE
     IHMYDLYVPV IECKKEHLEY KDAISLVEEG LKPLGKEYLD IFNEGINEGW IDVYENKGKR
     SGAYSWGSYD TMPYVLLNYN YELNDASTLA HEMGHSIHSY YTRKTQPYIY GDYSLFCAEV
     ASTTNEILLI HHLIEKETDK NKKLYLINQE LEQIRTTVFR QLMFAEFELK THEAIENGES
     LTSEVLCKMW KDINIKYFGE DMNVDEEISI EWARIPHFYS DFYVYQYATG YAAASSFANS
     ILSKGEEAVE KYKGFLKAGG SMYPIDTLKM AGVDMTTSKP LKDTLDRFNE LLDMLEEII
//
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