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Database: UniProt
Entry: R5CKE9_9FIRM
LinkDB: R5CKE9_9FIRM
Original site: R5CKE9_9FIRM 
ID   R5CKE9_9FIRM            Unreviewed;       609 AA.
AC   R5CKE9;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN   ORFNames=BN785_01769 {ECO:0000313|EMBL:CCX65247.1};
OS   Firmicutes bacterium CAG:791.
OC   Bacteria; Bacillota.
OX   NCBI_TaxID=1262993 {ECO:0000313|EMBL:CCX65247.1, ECO:0000313|Proteomes:UP000018038};
RN   [1] {ECO:0000313|EMBL:CCX65247.1, ECO:0000313|Proteomes:UP000018038}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:791 {ECO:0000313|Proteomes:UP000018038};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:CCX65247.1}.
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DR   EMBL; CAWT010000128; CCX65247.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5CKE9; -.
DR   STRING; 1262993.BN785_01769; -.
DR   Proteomes; UP000018038; 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; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR   PANTHER; PTHR11804:SF84; SACCHAROLYSIN; 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:UP000018038};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT   DOMAIN          111..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"
FT   COILED          577..604
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   609 AA;  69169 MW;  960AE5320526DB58 CRC64;
     MEQERSQMNP KDQWDLSTLY ENDEAFEQDL ARMDADTDAA AAFEGKLRDA ETIAKFYQAM
     TALQRRMNNL LTYAMLRQSE DTRAPKAQEL MAKGMNKAVL AESRCSFAEP EILALSEEKL
     KEIADAKELL PYRFLLQELL DEKPHVLSAE AEQLLAGFSE VLEAPKTIAD SLMDADLSFD
     SVKDREGNER ELSQANFILL EQSEDRTLRE NAFRSFYKGY ASHGNTLAAT YSGIVKSFAA
     QARARHYESS RAMALAGEHI PASVYDGLVE SVRRHMPSMH RYVQLRKKLL GLDELHYYDV
     YVPLTQGLSA QDSWSYEEAK SLVLEGLSPL GREYTDQVRK AFDDRWIDVY PNAGKRGGAF
     SSGTYDSNPF ILMSYTGDYE SVSTIAHEMG HSMHTWYSKN HQPSYYADYT LFVAEVASTV
     NENLLVEDLL KKTSDPTQRL FLLNQYLEGF KATVYRQTMF AEFERDAHAM AERGEALTPQ
     ALNNLYRKLI EDYFGPELVL DEEVACEWSR IPHFYRPFYV YKYATSYAAA VALSEKILKE
     GDQAVKPYLE FLSMGGSTYP LEELAHAGVD MTTTEPIDAA LEKFDRILDE AEQCAEELKA
     AAAETPRQR
//
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