ID   U7VFG1_9FUSO            Unreviewed;       654 AA.
AC   U7VFG1;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN   ORFNames=HMPREF0202_00591 {ECO:0000313|EMBL:ERT69563.1};
OS   Cetobacterium somerae ATCC BAA-474.
OC   Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC   Cetobacterium.
OX   NCBI_TaxID=1319815 {ECO:0000313|EMBL:ERT69563.1, ECO:0000313|Proteomes:UP000017081};
RN   [1] {ECO:0000313|EMBL:ERT69563.1, ECO:0000313|Proteomes:UP000017081}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-474 {ECO:0000313|EMBL:ERT69563.1,
RC   ECO:0000313|Proteomes:UP000017081};
RA   Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA   O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA   Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL   Submitted (AUG-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:ERT69563.1}.
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DR   EMBL; AXZF01000019; ERT69563.1; -; Genomic_DNA.
DR   AlphaFoldDB; U7VFG1; -.
DR   STRING; 1319815.HMPREF0202_00591; -.
DR   PATRIC; fig|1319815.3.peg.567; -.
DR   eggNOG; COG1164; Bacteria.
DR   HOGENOM; CLU_021290_2_0_0; -.
DR   Proteomes; UP000017081; 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:UP000017081};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT   DOMAIN          157..225
FT                   /note="Oligopeptidase F N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08439"
FT   DOMAIN          250..630
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   654 AA;  75702 MW;  22530BFC4083F252 CRC64;
     MKKFIVLILM ANLAFAGKYF YEKKSSQSQN TLIKPLPEIK KEDFSMLKNR DEIAQQYKWD
     LNDIYPNWNQ WEADLVKLKE LMAEIPKYQG EISKNPKTFV EFIDLEEKIS RLLDKIYLYP
     YLQRDLDSTN EVASVKLQEI ESIYANYSIS SSWITPEILT IPKETMVTWI NENPTLEPNR
     FPLMEIYRLQ EHVLSADKEK LLSYFGQYLG VPSDIYSELS TSDIKWNDVE LSDGSKTTVT
     NGVYSKVIST NRNQEDRKKV FEALYNSFNI NKNTYASIYK SILQRDFATA QSRNYKSSLE
     KALNPKNIPL DVYTSLIEST KENTAPLKRY IALRKNALNL SDYHYYDNSV NIVDYNKEFT
     YEEAKNTVLE SVKPLGEDYY NGLNTALSEG WLDVYETPNK RSGAYSLNIY DVHPYMLLNY
     NGTMDAVFTL AHELGHTMHS MLSTKNQPYP ISSYTIFVAE VASTFNERLL LDNMLRNTTD
     PKEKIALIEQ AIGGIVGTYY IQSLFADYEY QAHQIVENGG AITPEVLNNI MENLFKDYFG
     TELTMDELQK IIWARIPHFY NSPYYVYQYA TSFASSANLY DRITNTKYTP QEREKAKNEY
     LTLLKSGGND HPMNQLKKAG VDLSKKDAFN AVATEFNRLL DLLEEELKKE KGDI
//