ID   PTFB2_ECOL6             Reviewed;         106 AA.
AC   P69817; P32673;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=PTS system fructose-like EIIB component 2 {ECO:0000250|UniProtKB:P20966};
DE            EC=2.7.1.202 {ECO:0000250|UniProtKB:P20966};
DE   AltName: Full=Fructose-like phosphotransferase enzyme IIB componet 2 {ECO:0000250|UniProtKB:P20966};
GN   Name=frwB; OrderedLocusNames=c4908;
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 FrwABC 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}.
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DR   EMBL; AE014075; AAN83336.1; -; Genomic_DNA.
DR   RefSeq; WP_000161265.1; NC_004431.1.
DR   AlphaFoldDB; P69817; -.
DR   SMR; P69817; -.
DR   STRING; 199310.c4908; -.
DR   EnsemblBacteria; AAN83336; AAN83336; c4908.
DR   GeneID; 67417533; -.
DR   KEGG; ecc:c4908; -.
DR   eggNOG; COG1445; Bacteria.
DR   HOGENOM; CLU_013155_2_1_6; -.
DR   OMA; TPHDIAQ; -.
DR   BioCyc; ECOL199310:C4908-MON; -.
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..106
FT                   /note="PTS system fructose-like EIIB component 2"
FT                   /id="PRO_0000186502"
FT   DOMAIN          1..103
FT                   /note="PTS EIIB type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00422"
FT   ACT_SITE        10
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P20966, ECO:0000305"
FT   MOD_RES         10
FT                   /note="Phosphocysteine; by EIIA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00422"
SQ   SEQUENCE   106 AA;  11248 MW;  F712189F18489D3D CRC64;
     MTKIIAVTAC PSGVAHTYMA AEALESAAKA KGWEVKVETQ GSIGLENELT AEDVASADMV
     ILTKDIGIKF EERFAGKTIV RVNISDAVKR ADAIMSKIEA HLAQTA