ID   PTFB1_ECOL6             Reviewed;         108 AA.
AC   P69809; P76525; P78264;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=PTS system fructose-like EIIB component 1 {ECO:0000250|UniProtKB:P20966};
DE            EC=2.7.1.202 {ECO:0000250|UniProtKB:P20966};
DE   AltName: Full=Fructose-like phosphotransferase enzyme IIB component 1 {ECO:0000250|UniProtKB:P20966};
GN   Name=fryB; OrderedLocusNames=c2926;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase
CC       system (sugar PTS), a major carbohydrate active transport system,
CC       catalyzes the phosphorylation of incoming sugar substrates
CC       concomitantly with their translocation across the cell membrane. The
CC       enzyme II FryABC PTS system is involved in fructose transport.
CC       {ECO:0000250|UniProtKB:P20966}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-fructose(out) + N(pros)-phospho-L-histidyl-[protein] = D-
CC         fructose 1-phosphate(in) + L-histidyl-[protein];
CC         Xref=Rhea:RHEA:49252, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:9746,
CC         ChEBI:CHEBI:29979, ChEBI:CHEBI:37721, ChEBI:CHEBI:58674,
CC         ChEBI:CHEBI:64837; EC=2.7.1.202;
CC         Evidence={ECO:0000250|UniProtKB:P20966};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- DOMAIN: The PTS EIIB type-2 domain is phosphorylated by phospho-EIIA on
CC       a cysteinyl residue. Then, it transfers the phosphoryl group to the
CC       sugar substrate concomitantly with the sugar uptake processed by the
CC       PTS EIIC type-2 domain. {ECO:0000255|PROSITE-ProRule:PRU00422}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN81376.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE014075; AAN81376.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000038456.1; NC_004431.1.
DR   AlphaFoldDB; P69809; -.
DR   BMRB; P69809; -.
DR   SMR; P69809; -.
DR   STRING; 199310.c2926; -.
DR   EnsemblBacteria; AAN81376; AAN81376; c2926.
DR   GeneID; 66673742; -.
DR   KEGG; ecc:c2926; -.
DR   eggNOG; COG1445; Bacteria.
DR   HOGENOM; CLU_013155_2_1_6; -.
DR   OMA; IAVCACP; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0022877; F:protein-N(PI)-phosphohistidine-fructose phosphotransferase system transporter activity; IEA:InterPro.
DR   GO; GO:0090582; F:protein-phosphocysteine-D-fructose-phosphotransferase system transporter activity; ISS:UniProtKB.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; ISS:UniProtKB.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd05569; PTS_IIB_fructose; 1.
DR   InterPro; IPR036095; PTS_EIIB-like_sf.
DR   InterPro; IPR013011; PTS_EIIB_2.
DR   InterPro; IPR003501; PTS_EIIB_2/3.
DR   InterPro; IPR003353; PTS_IIB_fruc.
DR   Pfam; PF02302; PTS_IIB; 1.
DR   SUPFAM; SSF52794; SSF52794; 1.
DR   TIGRFAMs; TIGR00829; FRU; 1.
DR   PROSITE; PS51099; PTS_EIIB_TYPE_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Kinase; Phosphoprotein; Phosphotransferase system;
KW   Sugar transport; Transferase; Transport.
FT   CHAIN           1..108
FT                   /note="PTS system fructose-like EIIB component 1"
FT                   /id="PRO_0000186701"
FT   DOMAIN          1..104
FT                   /note="PTS EIIB type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00422"
FT   ACT_SITE        11
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P20966, ECO:0000305"
FT   MOD_RES         11
FT                   /note="Phosphocysteine; by EIIA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00422"
SQ   SEQUENCE   108 AA;  11735 MW;  EADDEFB237FB72A9 CRC64;
     MSKKLIALCA CPMGLAHTFM AAQALEEAAV EAGYEVKIET QGADGIQNRL TAQDIAEATI
     IIHSVAVTPE DNERFESRDV YEITLQDAIK NAAGIIKEIE EMIASEQQ