ID   Y367_BORBU              Reviewed;          92 AA.
AC   O51340;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-MAY-2022, entry version 110.
DE   RecName: Full=Putative phosphotransferase enzyme IIB component BB_0367;
DE            EC=2.7.1.-;
DE   AltName: Full=Putative PTS system EIIB component;
GN   OrderedLocusNames=BB_0367;
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   -!- FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase
CC       system (PTS), a major carbohydrate active -transport system, catalyzes
CC       the phosphorylation of incoming sugar substrates concomitant with their
CC       translocation across the cell membrane. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- DOMAIN: The EIIB domain is phosphorylated by phospho-EIIA on a
CC       cysteinyl or histidyl residue, depending on the transported sugar.
CC       Then, it transfers the phosphoryl group to the sugar substrate
CC       concomitantly with the sugar uptake processed by the EIIC domain.
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DR   EMBL; AE000783; AAC66754.1; -; Genomic_DNA.
DR   PIR; F70145; F70145.
DR   RefSeq; NP_212501.1; NC_001318.1.
DR   RefSeq; WP_002657824.1; NC_001318.1.
DR   AlphaFoldDB; O51340; -.
DR   SMR; O51340; -.
DR   STRING; 224326.BB_0367; -.
DR   PRIDE; O51340; -.
DR   EnsemblBacteria; AAC66754; AAC66754; BB_0367.
DR   GeneID; 56567795; -.
DR   KEGG; bbu:BB_0367; -.
DR   PATRIC; fig|224326.49.peg.762; -.
DR   HOGENOM; CLU_2407420_0_0_12; -.
DR   OMA; VMNFEII; -.
DR   Proteomes; UP000001807; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1360.60; -; 1.
DR   InterPro; IPR036878; Glu_permease_IIB.
DR   InterPro; IPR018113; PTrfase_EIIB_Cys.
DR   InterPro; IPR001996; PTS_IIB_1.
DR   Pfam; PF00367; PTS_EIIB; 1.
DR   SUPFAM; SSF55604; SSF55604; 1.
DR   PROSITE; PS51098; PTS_EIIB_TYPE_1; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Phosphoprotein; Phosphotransferase system; Reference proteome;
KW   Transferase.
FT   CHAIN           1..92
FT                   /note="Putative phosphotransferase enzyme IIB component
FT                   BB_0367"
FT                   /id="PRO_0000174395"
FT   DOMAIN          10..92
FT                   /note="PTS EIIB type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
SQ   SEQUENCE   92 AA;  10636 MW;  14311F946490B934 CRC64;
     MADLEKINKI KVAEHIVECF GGIKNIKNID KDLTRIKILV DSNSLVKRDD LTKNDNIIGT
     IKSNELTEVV INFEIIEDVY NKILYMMNEQ KQ