ID A0A150FSF8_CLOPD Unreviewed; 630 AA.
AC A0A150FSF8;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN ORFNames=JWYL7_1628 {ECO:0000313|EMBL:KXZ40553.1};
OS [Clostridium] paradoxum JW-YL-7 = DSM 7308.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae.
OX NCBI_TaxID=1121328 {ECO:0000313|EMBL:KXZ40553.1, ECO:0000313|Proteomes:UP000092605};
RN [1] {ECO:0000313|EMBL:KXZ40553.1, ECO:0000313|Proteomes:UP000092605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JW-YL-7 {ECO:0000313|EMBL:KXZ40553.1,
RC ECO:0000313|Proteomes:UP000092605};
RA Utturkar S.M., Lancaster A., Poole F.L., Adams M.W., Brown S.D.;
RT "Draft genome sequence for Clostridium paradoxum JW-YL-7.";
RL Submitted (FEB-2016) 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:KXZ40553.1}.
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DR EMBL; LSFY01000001; KXZ40553.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150FSF8; -.
DR STRING; 1121328.JWYL7_1628; -.
DR PATRIC; fig|1121328.3.peg.1639; -.
DR OrthoDB; 9766487at2; -.
DR Proteomes; UP000092605; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|SAM:Phobius};
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 Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 145..214
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 235..615
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 630 AA; 73974 MW; A90465E7149BD1ED CRC64;
MNKKGYVVSK FIILTVLMGM LLFIFTISNI NTSIDVFKTI DSHEYTWDLT KIYKTDKDWE
RDYKRLEQMI PEIEKYKGRL SNSSKDMKNA LKHLEDMKRL NEKLYIYAHL KSDEDKSNDK
YIALKEKAKN INIKLQLSTN FIEGEILSIP KEKINKFMKE DDFLRDYDFY FKELFRLKDR
YLSVEEENII SLAGFMANTP SNIYDIFRNS ERNFGKIKDR DGNEITLTPA LYRSLMGSRD
RTLRKEAFEK EFESFNQNIN MLAANLAGEV GKNIFYSKAR KYNSSLEASL DRDNVSVKLY
ENIINTTSKN LKPLHRYISL RKEALGIDDK VYLYDMYIPI SNYPGRRIPF DEAKDILLDA
LKPLGQDYIK DLEVALNSRW IDVYERENKR TGAYSFGVYD TYPYVLLNYS DSFSDVSTLA
HEMGHAMHSY YTNKHQPYIK SNYSIFTAEV ASITNEALLF EYLIENASSK EEKIYLIENY
IDLIQSAIYT QVMYAEFEKI IHEKVESGNT LNASILNEIW ADLLRKYYGE DFGVHELSKI
WWSRIPHFYR NFYVYKYVIG CSGAIALSED ILKSEEAREK YLEFLKSGAS DYPINLLKKA
GVDMTSSKPL EKAFKKFEQL IDEFEKLLKE
//
