ID   PEPF_BORBU              Reviewed;         590 AA.
AC   O51264;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Oligoendopeptidase F homolog;
DE            EC=3.4.24.-;
GN   Name=pepF; OrderedLocusNames=BB_0248;
OS   Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS   (Borrelia burgdorferi).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=224326;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX   PubMed=9403685; DOI=10.1038/37551;
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA   Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA   Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA   van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA   Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA   Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA   Smith H.O., Venter J.C.;
RT   "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL   Nature 390:580-586(1997).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the peptidase M3B family. {ECO:0000305}.
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DR   EMBL; AE000783; AAB91498.1; -; Genomic_DNA.
DR   PIR; H70130; H70130.
DR   RefSeq; NP_212382.1; NC_001318.1.
DR   RefSeq; WP_010889716.1; NC_001318.1.
DR   AlphaFoldDB; O51264; -.
DR   SMR; O51264; -.
DR   STRING; 224326.BB_0248; -.
DR   PRIDE; O51264; -.
DR   EnsemblBacteria; AAB91498; AAB91498; BB_0248.
DR   KEGG; bbu:BB_0248; -.
DR   PATRIC; fig|224326.49.peg.647; -.
DR   HOGENOM; CLU_021290_2_0_12; -.
DR   OMA; YRQTMFA; -.
DR   Proteomes; UP000001807; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:CAFA.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1370.20; -; 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   PANTHER; PTHR11804; PTHR11804; 1.
DR   Pfam; PF01432; Peptidase_M3; 1.
DR   Pfam; PF08439; Peptidase_M3_N; 1.
DR   TIGRFAMs; TIGR00181; pepF; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW   Zinc.
FT   CHAIN           1..590
FT                   /note="Oligoendopeptidase F homolog"
FT                   /id="PRO_0000078166"
FT   ACT_SITE        382
FT                   /evidence="ECO:0000250"
FT   BINDING         381
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         385
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         388
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   590 AA;  69723 MW;  E401E692C85EF4C3 CRC64;
     MINRNEINEN DKWDLSFLFA NEEEYVKTIN AIEIKTKEFK KYEKLELNFD LFKETLNKYY
     EIMEDLEKVS YYAMLQLETD VTNKDSNKIY SICVNLATKV SNTTSYFMPK ILKTDEKKIQ
     AWINDPELKD KKIAIEKILR EKKHILSEQE EKILANYTPL YTSYQSIFSA LTNADMEFGE
     INKHPLTNST YTLFLQNEDQ KIRKEAFLRF YQKYKNNENT LANLIISDFK KNHFIAKTRR
     FQNTFSMQLF SNNIDKKVYT NLIETVNENL PVLNDYYEFR KKVLNQEYLY HYDVYVPLTK
     GIIFKNSFED ACEKILKSLE VLGNEYTKIL RNGLLKERWV DKYENTGKRS GAFSAGSYNG
     KPYILLNYKD ESIRDMFTLA HEAGHSMHSY FSIKNNPFPH YNYSIFEAEI ASIINEQILA
     EYLLKNETDT NKIKYIKLTQ IDDMISTFFR QTMFAEFEYI IHEMISKEEP VVKETLTETY
     MNLLKKYFGP SLKFDELSPL ECLRIPHFYS PFYVYQYATG IAAALSIYKG IKENKKDAVE
     NYIKFLKTGG SKYPLDSLNI TGVDLTKKAT IENTINIFKC RLEEIKKIFQ