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
//