ID   W2C167_9FIRM            Unreviewed;       599 AA.
AC   W2C167;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN   Name=pepF {ECO:0000313|EMBL:ETK00171.1};
GN   ORFNames=HMPREF0378_1393 {ECO:0000313|EMBL:ETK00171.1};
OS   Eubacterium nodatum ATCC 33099.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales;
OC   Eubacteriales Family XIII. Incertae Sedis.
OX   NCBI_TaxID=1161902 {ECO:0000313|EMBL:ETK00171.1, ECO:0000313|Proteomes:UP000018868};
RN   [1] {ECO:0000313|EMBL:ETK00171.1, ECO:0000313|Proteomes:UP000018868}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33099 {ECO:0000313|EMBL:ETK00171.1,
RC   ECO:0000313|Proteomes:UP000018868};
RA   Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA   Methe B., Sutton G., Nelson K.E.;
RL   Submitted (DEC-2013) 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:ETK00171.1}.
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DR   EMBL; AZKM01000006; ETK00171.1; -; Genomic_DNA.
DR   AlphaFoldDB; W2C167; -.
DR   STRING; 1161902.HMPREF0378_1393; -.
DR   PATRIC; fig|1161902.3.peg.262; -.
DR   eggNOG; COG1164; Bacteria.
DR   OrthoDB; 9766487at2; -.
DR   Proteomes; UP000018868; 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:UP000018868};
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          206..586
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   599 AA;  68654 MW;  CD022869604FC12D CRC64;
     MGNKKLKTRN EIAPEFKWRL EKMYSDDGDW EKDLSDAESL AADFSKFKGH LGESPSILAD
     ALETGDKIEL KLERAFVYAR MKLDEDNRVA KHQAMHDRSK QSIAKISAAL SFITPELISL
     PGETLLSYLE REPRLQVYEH MFHNLLRQKD HVLSSDEETL MAQIGEVLGA TDTIFTMLND
     ADMKFGKITD ENGEKVTLTH GNYINFMRSH NRKVREDAYK CCYTSYKNLI NTLAANYSYN
     VKTDVVTSKI RKYPSSRNAA LSGGNISEEV YDNLVSAVHD ALPAMHEYIE LRKKILGVDE
     LKMHDVYVPL VELPERYIPF EDAVSISMQG LAPLGKEYLT QFKSGIDSGW VDIYENEGKT
     SGAYSFGSYD SDPFVLMNYN NRLEDVFTLV HEMGHSMNSY YTRKHQPFVY GDHSIFTAEV
     ASTVNESLLM KHLLSTEKDD KMHKHILNMY IEAFRTTLFR QTMFAEFEHK SHKYVEEGGS
     LTAEWLNKTY DDLNTLYFGP ALTHDDLIQY EWSRIPHFYR SFYVYQYATG YSAATAISKL
     ILENGEEAKN AYIEFLKCGT NDYPVELLKI AGVDMASKEP VDKAMETFKN LVDELKGLF
//