PTFB1_ECOLI
ID PTFB1_ECOLI Reviewed; 108 AA.
AC P69808; P76525; P78264;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
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; Synonyms=ypdH; OrderedLocusNames=b2387, JW5389;
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 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
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 STRUCTURE BY NMR.
RA Wu B., Yee A., Gutmanas A., Semest A., Arrowsmith C.H.;
RT "Solution structure of Enzyme IIB subunit of PTS system from Escherichia
RT coli K12, Northeast structural genomics consortium target ER315/Ontario
RT center for structural proteomics target ec0544.";
RL Submitted (JUN-2010) 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. 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}.
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DR EMBL; U00096; AAC75446.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16257.2; -; Genomic_DNA.
DR PIR; H65012; H65012.
DR RefSeq; NP_416888.1; NC_000913.3.
DR RefSeq; WP_000038456.1; NZ_STEB01000008.1.
DR PDB; 2KYR; NMR; -; A=1-108.
DR PDBsum; 2KYR; -.
DR AlphaFoldDB; P69808; -.
DR BMRB; P69808; -.
DR SMR; P69808; -.
DR BioGRID; 4260782; 10.
DR STRING; 511145.b2387; -.
DR TCDB; 4.A.2.1.11; the pts fructose-mannitol (fru) family.
DR jPOST; P69808; -.
DR PaxDb; P69808; -.
DR PRIDE; P69808; -.
DR EnsemblBacteria; AAC75446; AAC75446; b2387.
DR EnsemblBacteria; BAA16257; BAA16257; BAA16257.
DR GeneID; 66673742; -.
DR GeneID; 949087; -.
DR KEGG; ecj:JW5389; -.
DR KEGG; eco:b2387; -.
DR PATRIC; fig|1411691.4.peg.4341; -.
DR EchoBASE; EB3907; -.
DR eggNOG; COG1445; Bacteria.
DR HOGENOM; CLU_013155_2_1_6; -.
DR OMA; IAVCACP; -.
DR PhylomeDB; P69808; -.
DR BioCyc; EcoCyc:G7250-MON; -.
DR EvolutionaryTrace; P69808; -.
DR PRO; PR:P69808; -.
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: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..108
FT /note="PTS system fructose-like EIIB component 1"
FT /id="PRO_0000186700"
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"
FT STRAND 4..13
FT /evidence="ECO:0007829|PDB:2KYR"
FT HELIX 15..31
FT /evidence="ECO:0007829|PDB:2KYR"
FT STRAND 33..42
FT /evidence="ECO:0007829|PDB:2KYR"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:2KYR"
FT HELIX 52..57
FT /evidence="ECO:0007829|PDB:2KYR"
FT STRAND 59..67
FT /evidence="ECO:0007829|PDB:2KYR"
FT HELIX 72..75
FT /evidence="ECO:0007829|PDB:2KYR"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:2KYR"
FT HELIX 87..90
FT /evidence="ECO:0007829|PDB:2KYR"
FT HELIX 92..107
FT /evidence="ECO:0007829|PDB:2KYR"
SQ SEQUENCE 108 AA; 11735 MW; EADDEFB237FB72A9 CRC64;
MSKKLIALCA CPMGLAHTFM AAQALEEAAV EAGYEVKIET QGADGIQNRL TAQDIAEATI
IIHSVAVTPE DNERFESRDV YEITLQDAIK NAAGIIKEIE EMIASEQQ
