ID D7N8V2_9FIRM Unreviewed; 595 AA.
AC D7N8V2;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 24-JAN-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:EFI41317.1};
GN ORFNames=HMPREF0629_01375 {ECO:0000313|EMBL:EFI41317.1};
OS Peptoniphilus sp. oral taxon 386 str. F0131.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Peptoniphilus.
OX NCBI_TaxID=575609 {ECO:0000313|EMBL:EFI41317.1, ECO:0000313|Proteomes:UP000004712};
RN [1] {ECO:0000313|EMBL:EFI41317.1, ECO:0000313|Proteomes:UP000004712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0131 {ECO:0000313|EMBL:EFI41317.1,
RC ECO:0000313|Proteomes:UP000004712};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J., Yandava C.,
RA Izard J., Baranova O.V., Blanton J.M., Tanner A.C., Dewhirst F.E., Haas B.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Peptoniphilus sp. oral taxon 386 strain F0131.";
RL Submitted (FEB-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; GL349423; EFI41317.1; -; Genomic_DNA.
DR RefSeq; WP_009222647.1; NZ_GL349423.1.
DR AlphaFoldDB; D7N8V2; -.
DR STRING; 575609.HMPREF0629_01375; -.
DR eggNOG; COG1164; Bacteria.
DR HOGENOM; CLU_021290_1_1_9; -.
DR Proteomes; UP000004712; 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; 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 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:UP000004712};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT DOMAIN 113..179
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 200..581
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 595 AA; 68707 MW; 17EE3E6C56BF203D CRC64;
MEALKNRSEI DESLKWDLSR IFKSEDEYNT KLNEMIKLSD ELVKFKGNIK NSEDLLNSIK
IYEKIMEAQN LTSNYASLSY SVDLTDEESR IRIQKFDNIE NNLMEKISFY ENEILSLDVE
IIEETINSSD KYKMYLKTIL KNKEHILSEK EEKVIATLAP SIAGPYKTYE DSKASDMTFD
DFVVGDKTYA NSFVLYENFY CYDTNEEVRR KAYESFSKGL DRYKNTFASV YINHVTNEKQ
IATLRGFDSV IDYLLFNQGV DRKLYDRQID LMTEKLAPHM RKYAKLIKKF YNIDKMTFAD
LKVPIDAEFV PKITIEESKD YVKDALSVMG EEYLDVAMSS YSNRWIDFAN NIGKSTGGFC
ASPYKCDSFI LLSFTEQLNE VYTLVHEIGH GVHFHNAQAN NSVLEEEPSL YFIESPSTIN
ELLLSNSLLK KATDDRFKRF VYAAQIGNTY YHNCVTHLLE AAYQREVYRL VDAGEPLTEK
TLTKITKEVH EKFWADAVEI DDYAALTWMR QPHYYMGLYS YTYSAGLSIA TEVAKRIMKD
GKVAADAWID ALCKGGSLEI IDLCKVAGVD ITKEDFILNT IDYIGDIIDK IEELM
//
