ID   PTFLB_ECOLI             Reviewed;         483 AA.
AC   P32154; Q2M8J6;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 2.
DT   04-NOV-2026, entry version 179.
DE   RecName: Full=Fructose-like PTS system EIIBC component {ECO:0000305|PubMed:8019415};
DE   Includes:
DE     RecName: Full=PTS system fructose-like EIIB component {ECO:0000305|PubMed:8019415};
DE              EC=2.7.1.202 {ECO:0000250|UniProtKB:P20966};
DE     AltName: Full=Fructose-like phosphotransferase enzyme IIB component {ECO:0000305|PubMed:8019415};
DE   Includes:
DE     RecName: Full=PTS system fructose-like EIIC component {ECO:0000305|PubMed:8019415};
DE     AltName: Full=Fructose-like permease IIC component {ECO:0000305|PubMed:8019415};
GN   Name=frvB {ECO:0000303|PubMed:8019415}; Synonyms=yiiJ;
GN   OrderedLocusNames=b3899, JW5562;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=8346018; DOI=10.1093/nar/21.15.3391;
RA   Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
RT   "Analysis of the Escherichia coli genome. III. DNA sequence of the region
RT   from 87.2 to 89.2 minutes.";
RL   Nucleic Acids Res. 21:3391-3398(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   FUNCTION, AND DISCUSSION OF SEQUENCE.
RX   PubMed=8019415; DOI=10.1002/pro.5560030309;
RA   Reizer J., Michotey V., Reizer A., Saier M.H. Jr.;
RT   "Novel phosphotransferase system genes revealed by bacterial genome
RT   analysis: unique, putative fructose- and glucoside-specific systems.";
RL   Protein Sci. 3:440-450(1994).
RN   [5]
RP   SUBCELLULAR LOCATION.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=15919996; DOI=10.1126/science.1109730;
RA   Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT   "Global topology analysis of the Escherichia coli inner membrane
RT   proteome.";
RL   Science 308:1321-1323(2005).
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 FrvAB PTS system is involved in fructose transport.
CC       {ECO:0000305|PubMed:8019415}.
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: Cell inner membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00427, ECO:0000305|PubMed:15919996}; Multi-pass membrane
CC       protein {ECO:0000255|PROSITE-ProRule:PRU00427}.
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   -!- DOMAIN: The EIIC type-2 domain forms the PTS system translocation
CC       channel and contains the specific substrate-binding site.
CC       {ECO:0000255|PROSITE-ProRule:PRU00427}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB03032.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; L19201; AAB03032.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U00096; AAC76881.2; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77410.1; -; Genomic_DNA.
DR   RefSeq; NP_418335.4; NC_000913.3.
DR   RefSeq; WP_000446023.1; NZ_CP009789.1.
DR   AlphaFoldDB; P32154; -.
DR   SMR; P32154; -.
DR   BioGRID; 4259396; 17.
DR   ComplexPortal; CPX-5979; Frv fructose-like enzyme II complex.
DR   FunCoup; P32154; 83.
DR   STRING; 511145.b3899; -.
DR   TCDB; 4.A.2.1.25; the pts fructose-mannitol (fru) family.
DR   PaxDb; 511145-b3899; -.
DR   EnsemblBacteria; AAC76881; AAC76881; b3899.
DR   GeneID; 75174139; -.
DR   GeneID; 948390; -.
DR   KEGG; ecj:JW5562; -.
DR   KEGG; eco:b3899; -.
DR   KEGG; ecoc:C3026_21080; -.
DR   PATRIC; fig|1411691.4.peg.2808; -.
DR   EchoBASE; EB1809; -.
DR   eggNOG; COG1299; Bacteria.
DR   eggNOG; COG1445; Bacteria.
DR   HOGENOM; CLU_013155_0_0_6; -.
DR   InParanoid; P32154; -.
DR   OMA; DWYAIIG; -.
DR   OrthoDB; 9782569at2; -.
DR   PhylomeDB; P32154; -.
DR   BioCyc; EcoCyc:FRVB-MONOMER; -.
DR   BioCyc; MetaCyc:FRVB-MONOMER; -.
DR   PRO; PR:P32154; -.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR   GO; GO:1902495; C:transmembrane transporter complex; NAS:ComplexPortal.
DR   GO; GO:0005351; F:carbohydrate:proton symporter activity; IEA:InterPro.
DR   GO; GO:0022877; F:protein-N(PI)-phosphohistidine-fructose phosphotransferase system transporter activity; IEA:InterPro.
DR   GO; GO:0090563; F:protein-phosphocysteine-sugar phosphotransferase activity; IBA:GO_Central.
DR   GO; GO:1990539; P:fructose import across plasma membrane; NAS:ComplexPortal.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; ISA:EcoCyc.
DR   CDD; cd05569; PTS_IIB_fructose; 1.
DR   FunFam; 3.40.50.2300:FF:000014; PTS system fructose-like transporter subunit IIB; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   InterPro; IPR050864; Bacterial_PTS_Sugar_Transport.
DR   InterPro; IPR036095; PTS_EIIB-like_sf.
DR   InterPro; IPR013011; PTS_EIIB_2.
DR   InterPro; IPR003501; PTS_EIIB_2/3.
DR   InterPro; IPR003352; PTS_EIIC.
DR   InterPro; IPR013014; PTS_EIIC_2.
DR   InterPro; IPR003353; PTS_IIB_fruc.
DR   InterPro; IPR006327; PTS_IIC_fruc.
DR   NCBIfam; TIGR00829; FRU; 1.
DR   NCBIfam; NF008493; PRK11404.1; 1.
DR   NCBIfam; TIGR01427; PTS_IIC_fructo; 1.
DR   PANTHER; PTHR30505; FRUCTOSE-LIKE PERMEASE; 1.
DR   PANTHER; PTHR30505:SF0; FRUCTOSE-LIKE PTS SYSTEM EIIBC COMPONENT-RELATED; 1.
DR   Pfam; PF02378; PTS_EIIC; 1.
DR   Pfam; PF02302; PTS_IIB; 1.
DR   SUPFAM; SSF52794; PTS system IIB component-like; 1.
DR   PROSITE; PS51099; PTS_EIIB_TYPE_2; 1.
DR   PROSITE; PS51104; PTS_EIIC_TYPE_2; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Kinase; Membrane; Phosphoprotein;
KW   Phosphotransferase system; Reference proteome; Sugar transport;
KW   Transferase; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..483
FT                   /note="Fructose-like PTS system EIIBC component"
FT                   /id="PRO_0000186499"
FT   TRANSMEM        132..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT   TRANSMEM        180..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT   TRANSMEM        204..224
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT   TRANSMEM        227..247
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT   TRANSMEM        264..284
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT   TRANSMEM        303..323
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT   TRANSMEM        344..364
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT   TRANSMEM        380..400
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT   TRANSMEM        402..422
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT   TRANSMEM        442..462
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT   DOMAIN          1..105
FT                   /note="PTS EIIB type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00422"
FT   DOMAIN          128..475
FT                   /note="PTS EIIC type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT   ACT_SITE        13
FT                   /note="Phosphocysteine intermediate; for EIIB activity"
FT                   /evidence="ECO:0000250|UniProtKB:P20966, ECO:0000305"
FT   MOD_RES         13
FT                   /note="Phosphocysteine; by EIIA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00422"
SQ   SEQUENCE   483 AA;  51120 MW;  9B982ECDCBA1E1A4 CRC64;
     MESSLRIVAI TNCPAGIAHT YMVAEALEQK ARSLGHTIKV ETQGSSGVEN RLSSEEIAAA
     DYVILATGRG LSGDDRARFA GKKVYEIAIS QALKNIDQIF SELPTNSQLF AADSGVKLGK
     QEVQSGSVMS HLMAGVSAAL PFVIGGGILV ALANMLVQFG LPYTDMSKGA PSFTWVVESI
     GYLGFTFMIP IMGAYIASSI ADKPAFAPAF LVCYLANDKA LLGTQSGAGF LGAVVLGLAI
     GYFVFWFRKV RLGKALQPLL GSMLIPFVTL LVFGVLTYYV IGPVMSDLMG GLLHFLNTIP
     PSMKFAAAFL VGAMLAFDMG GPINKTAWFF CFSLLEKHIY DWYAIVGVVA LMPPVAAGLA
     TFIAPKLFTR QEKEAASSAI VVGATVATEP AIPYALAAPL PMITANTLAG GITGVLVIAF
     GIKRLAPGLG IFDPLIGLMS PVGSFYLVLA IGLALNISFI IVLKGLWLRR KAKAAQQELV
     HEH
//