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 27-MAR-2024, entry version 134.
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; Spirochaetota; Spirochaetia; Spirochaetales; Borreliaceae;
OC 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 PaxDb; 224326-BB_0248; -.
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 OrthoDB; 9766487at2; -.
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 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; 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
//
