PTFB2_ECOLI
ID PTFB2_ECOLI Reviewed; 106 AA.
AC P69816; P32673; Q2M8P5;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
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 component 2 {ECO:0000250|UniProtKB:P20966};
GN Name=frwB; Synonyms=yijK; OrderedLocusNames=b3950, JW3922;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(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=7773398; DOI=10.1099/13500872-141-4-961;
RA Reizer J., Reizer A., Saier M.H. Jr.;
RT "Novel phosphotransferase system genes revealed by bacterial genome
RT analysis -- a gene cluster encoding a unique Enzyme I and the proteins of a
RT fructose-like permease system.";
RL Microbiology 141:961-971(1995).
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, ECO:0000305|PubMed:7773398}.
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; U00006; AAC43056.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76932.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77361.1; -; Genomic_DNA.
DR PIR; A65202; A65202.
DR RefSeq; NP_418385.1; NC_000913.3.
DR RefSeq; WP_000161265.1; NZ_STEB01000037.1.
DR AlphaFoldDB; P69816; -.
DR SMR; P69816; -.
DR BioGRID; 4262059; 13.
DR BioGRID; 852744; 3.
DR ComplexPortal; CPX-5994; Frw fuctose-like enzyme II complex.
DR IntAct; P69816; 4.
DR STRING; 511145.b3950; -.
DR TCDB; 4.A.2.1.10; the pts fructose-mannitol (fru) family.
DR PaxDb; P69816; -.
DR PRIDE; P69816; -.
DR EnsemblBacteria; AAC76932; AAC76932; b3950.
DR EnsemblBacteria; BAE77361; BAE77361; BAE77361.
DR GeneID; 67417533; -.
DR GeneID; 948447; -.
DR KEGG; ecj:JW3922; -.
DR KEGG; eco:b3950; -.
DR PATRIC; fig|1411691.4.peg.2755; -.
DR EchoBASE; EB1853; -.
DR eggNOG; COG1445; Bacteria.
DR HOGENOM; CLU_013155_2_1_6; -.
DR OMA; TPHDIAQ; -.
DR PhylomeDB; P69816; -.
DR BioCyc; EcoCyc:FRWB-MON; -.
DR BioCyc; MetaCyc:FRWB-MON; -.
DR PRO; PR:P69816; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:1902495; C:transmembrane transporter complex; IC:ComplexPortal.
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:0090563; F:protein-phosphocysteine-sugar phosphotransferase activity; IBA:GO_Central.
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 Reference proteome; Sugar transport; Transferase; Transport.
FT CHAIN 1..106
FT /note="PTS system fructose-like EIIB component 2"
FT /id="PRO_0000186501"
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
