ID   Y118_BORBU              Reviewed;         433 AA.
AC   O51145;
DT   15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2012, sequence version 2.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Putative zinc metalloprotease BB_0118;
DE            EC=3.4.24.-;
GN   OrderedLocusNames=BB_0118;
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:0000305};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M50B family. {ECO:0000305}.
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DR   EMBL; AE000783; AAC66514.2; -; Genomic_DNA.
DR   PIR; F70114; F70114.
DR   RefSeq; NP_212252.2; NC_001318.1.
DR   RefSeq; WP_010889688.1; NC_001318.1.
DR   AlphaFoldDB; O51145; -.
DR   SMR; O51145; -.
DR   STRING; 224326.BB_0118; -.
DR   PRIDE; O51145; -.
DR   EnsemblBacteria; AAC66514; AAC66514; BB_0118.
DR   KEGG; bbu:BB_0118; -.
DR   PATRIC; fig|224326.49.peg.516; -.
DR   HOGENOM; CLU_025778_0_0_12; -.
DR   Proteomes; UP000001807; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; 2.30.42.10; -; 2.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR041489; PDZ_6.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR004387; Pept_M50_Zn.
DR   InterPro; IPR008915; Peptidase_M50.
DR   PANTHER; PTHR42837; PTHR42837; 2.
DR   Pfam; PF17820; PDZ_6; 1.
DR   Pfam; PF02163; Peptidase_M50; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; SSF50156; 2.
DR   TIGRFAMs; TIGR00054; TIGR00054; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Hydrolase; Membrane; Metal-binding;
KW   Metalloprotease; Protease; Reference proteome; Transmembrane;
KW   Transmembrane helix; Zinc.
FT   CHAIN           1..433
FT                   /note="Putative zinc metalloprotease BB_0118"
FT                   /id="PRO_0000088431"
FT   TRANSMEM        98..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        334..356
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        366..388
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        401..423
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          193..265
FT                   /note="PDZ"
FT   ACT_SITE        18
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         17
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         21
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   433 AA;  49238 MW;  CD623F67971C39FF CRC64;
     MYILFSVLAL SFIIFIHELG HFLFAKLFKV KVEVFSVGIG PSILKFKINN TEYRLSPILL
     GGYCKLKGFD HLEKELKANK ELEADKDSLF GISHFKKILI YFAGPLFNLI FSFIVFIFIS
     MAGVIYFDYS SRVSILNKDS LLKDKFRDGD VILKVNDKKI KYFSDLRKFI PEEKSTVMFD
     VLREKENITF KETVSLQDFL KEIGPWADLV IADVVSNSPA KIAGMKPGDE IISIDNVILK
     NKRDLDYFLK NLNSDVVEIK FSRNGEIFSS KLVFHDKNKM IGIYFSPPLK RVVKVENVSS
     AIKNSFFKVV SALQDILYSI FLLMTNFLNA SKSVSGPVGI VGILSSSYSL GILYWINSIS
     FLSLILAGMN LFFIVIPIFD GGQIFISFIE LLRGKRFKAK TIYSFYSFGI FFGLFLFGLG
     LFNDLKGLLN IFN