ID D6GSG9_FILAD Unreviewed; 604 AA.
AC D6GSG9;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN Name=pepF {ECO:0000313|EMBL:EFE28610.1};
GN OrderedLocusNames=HMPREF0389_00527 {ECO:0000313|EMBL:EFE28610.1};
OS Filifactor alocis (strain ATCC 35896 / CCUG 47790 / D40 B5) (Fusobacterium
OS alocis).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Filifactor.
OX NCBI_TaxID=546269 {ECO:0000313|EMBL:EFE28610.1, ECO:0000313|Proteomes:UP000007468};
RN [1] {ECO:0000313|Proteomes:UP000007468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35896 / D40 B5 {ECO:0000313|Proteomes:UP000007468};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Earl A., Feldgarden M., Young S.K., Gargeya S., Zeng Q.,
RA Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z., Freedman E.,
RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D.,
RA Howarth C., Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., White J., Yandava C., Izard J.,
RA Blanton J.M., Baranova O.V., Tanner A.C., Dewhirst F.E., Haas B.,
RA Nusbaum C., Birren B.;
RT "The genome sequence of Filifactor alocis strain ATCC 35896.";
RL Submitted (DEC-2010) 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}.
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DR EMBL; CP002390; EFE28610.1; -; Genomic_DNA.
DR RefSeq; WP_014261785.1; NC_016630.1.
DR AlphaFoldDB; D6GSG9; -.
DR STRING; 546269.HMPREF0389_00527; -.
DR KEGG; faa:HMPREF0389_00527; -.
DR PATRIC; fig|546269.5.peg.121; -.
DR eggNOG; COG1164; Bacteria.
DR OrthoDB; 9766487at2; -.
DR Proteomes; UP000007468; 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; 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 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000007468};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT DOMAIN 115..181
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 202..584
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
FT COILED 102..129
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 604 AA; 70572 MW; ACEF83F6FEA14BB8 CRC64;
MMEVMKKRDE TPEYLKWDIS RLYKKESDYE EDLKKCEQMS VDIEKKYKNK IVSPDTAICA
IREYNEFLEL NDVISHYATL SVSVDMTDAQ HQKRESYYYS KAAEIQTRLK FLEKEIVSLD
AQILEKVKEK APEYRVYIED IMLKKEYMLD DSVEEALATL SPVLHSSIKG YETTKIADIE
FESFVVRGKE YPNSYVLYEN MYQYNPDFEI RRKSFQSFSN GLKKYQNTTA FYYQNHIQKE
KIISAMRGFS SVFDYLLLDQ KVTKEMYHRQ IDLIMKELAP YMQKYAALLK KIYHLDKITF
ADLKIPVDKE IVPRITIEES KKYVREALSV LGEEYVDLIM SSYEERWVDF AQNIGKSTGG
FCATPYGKHS FILLSWTGLL SEVFTLVHEL GHAGHFTLNQ RENSYLNQEP SLYFVEAPST
MNELLLTNYL LKDVGVDKRM KRWVLSNMIS NTYFHNFVTH LLEAAYQREV YKRVDRGESL
QAEDLSMIKK NVLQEFWGED VEITDGAELT WMRQPHYYMG LYSYTYSAGL TIGTQMSNRI
KEEGFSAAQD WIKVLKAGGT KNPVELAQMA GIDITTDKPL LDTIHFIGSA IKEIIQLTEE
LEKN
//
