PTFB3_ECOLI
ID PTFB3_ECOLI Reviewed; 113 AA.
AC P32676; Q2M8P8;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=PTS system fructose-like EIIB component 3 {ECO:0000250|UniProtKB:P20966};
DE EC=2.7.1.202 {ECO:0000250|UniProtKB:P20966};
DE AltName: Full=Fructose-like phosphotransferase enzyme IIB component 3 {ECO:0000250|UniProtKB:P20966};
GN Name=frwD; Synonyms=yijN; OrderedLocusNames=b3953, JW3925;
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).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS).
RA Kim M.S., Shin D.H., Lee J., Joo K., Park J., Lee D., Berry E.A.,
RA Jhon G.-J.;
RT "High-accuracy protein modeling and its application to molecular
RT replacement of crystallographic phasing.";
RL Submitted (JUN-2014) to the PDB data bank.
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.
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; AAC43059.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76935.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77358.1; -; Genomic_DNA.
DR PIR; D65202; D65202.
DR RefSeq; NP_418388.1; NC_000913.3.
DR RefSeq; WP_000323846.1; NZ_LN832404.1.
DR PDB; 4TN5; X-ray; 2.29 A; A/B=1-113.
DR PDBsum; 4TN5; -.
DR AlphaFoldDB; P32676; -.
DR SMR; P32676; -.
DR BioGRID; 4263010; 6.
DR BioGRID; 852748; 2.
DR ComplexPortal; CPX-5994; Frw fuctose-like enzyme II complex.
DR IntAct; P32676; 2.
DR STRING; 511145.b3953; -.
DR TCDB; 4.A.2.1.10; the pts fructose-mannitol (fru) family.
DR PaxDb; P32676; -.
DR PRIDE; P32676; -.
DR EnsemblBacteria; AAC76935; AAC76935; b3953.
DR EnsemblBacteria; BAE77358; BAE77358; BAE77358.
DR GeneID; 948452; -.
DR KEGG; ecj:JW3925; -.
DR KEGG; eco:b3953; -.
DR PATRIC; fig|1411691.4.peg.2752; -.
DR EchoBASE; EB1856; -.
DR eggNOG; COG1445; Bacteria.
DR HOGENOM; CLU_013155_2_2_6; -.
DR OMA; CISGVAH; -.
DR PhylomeDB; P32676; -.
DR BioCyc; EcoCyc:EG11912-MON; -.
DR PRO; PR:P32676; -.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Kinase; Phosphoprotein; Phosphotransferase system;
KW Reference proteome; Sugar transport; Transferase; Transport.
FT CHAIN 1..113
FT /note="PTS system fructose-like EIIB component 3"
FT /id="PRO_0000186505"
FT DOMAIN 1..100
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"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:4TN5"
FT TURN 13..17
FT /evidence="ECO:0007829|PDB:4TN5"
FT HELIX 18..30
FT /evidence="ECO:0007829|PDB:4TN5"
FT STRAND 34..41
FT /evidence="ECO:0007829|PDB:4TN5"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:4TN5"
FT HELIX 51..56
FT /evidence="ECO:0007829|PDB:4TN5"
FT STRAND 58..66
FT /evidence="ECO:0007829|PDB:4TN5"
FT HELIX 71..74
FT /evidence="ECO:0007829|PDB:4TN5"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:4TN5"
FT HELIX 84..89
FT /evidence="ECO:0007829|PDB:4TN5"
FT HELIX 92..103
FT /evidence="ECO:0007829|PDB:4TN5"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:4TN5"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:4TN5"
SQ SEQUENCE 113 AA; 12637 MW; 36252AB21DDB09EC CRC64;
MAYLVAVTAC VSGVAHTYMA AERLEKLCLL EKWGVSIETQ GALGTENRLA DEDIRRADVA
LLITDIELAG AERFEHCRYV QCSIYAFLRE PQRVMSAVRK VLSAPQQTHL ILE
