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UniProtKB/Swiss-Prot entry P32154


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PTFLB_ECOLI
Primary accession number P32154
Secondary accession number Q2M8J6
Integrated into Swiss-Prot on October 1, 1993
Sequence was last modified on April 27, 2001 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 79)
Name and origin of the protein
Protein name Fructose-like PTS system EIIBC component
Synonyms None
Includes Fructose-like phosphotransferase enzyme IIB component
     (EC 2.7.1.69)
     (PTS system fructose-like EIIB component)
Fructose-like permease IIC component
     (PTS system fructose-like EIIC component)
Gene name
Name: frvB
Synonyms: yiiJ
OrderedLocusNames: b3899, JW5562
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1093/nar/21.15.3391; PubMed=8346018 [NCBI, ExPASy, EBI, Israel, Japan]
Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
"Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes.";
Nucleic Acids Res. 21:3391-3398(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[4]
DISCUSSION OF SEQUENCE.
PubMed=8019415 [NCBI, ExPASy, EBI, Israel, Japan]
Reizer J., Michotey V., Reizer A., Saier M.H. Jr.;
"Novel phosphotransferase system genes revealed by bacterial genome analysis: unique, putative fructose- and glucoside-specific systems.";
Protein Sci. 3:440-450(1994).
[5]
SUBCELLULAR LOCATION.
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.1109730; PubMed=15919996 [NCBI, ExPASy, EBI, Israel, Japan]
Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
"Global topology analysis of the Escherichia coli inner membrane proteome.";
Science 308:1321-1323(2005).
Comments
  • FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane (By similarity).
  • CATALYTIC ACTIVITY: Protein EIIB N(pi)-phospho-L-histidine/cysteine + sugar = protein EIIB + sugar phosphate.
  • SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
  • DOMAIN: The EIIB domain is phosphorylated by phospho-EIIA on a cysteinyl or histidyl residue, depending on the transported sugar. Then, it transfers the phosphoryl group to the sugar substrate concomitantly with the sugar uptake processed by the EIIC domain.
  • DOMAIN: The EIIC domain forms the PTS system translocation channel and contains the specific substrate-binding site.
  • SIMILARITY: Contains 1 PTS EIIB type-2 domain.
  • SIMILARITY: Contains 1 PTS EIIC type-2 domain.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
L19201; AAB03032.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC76881.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE77410.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq AP_003909.1; -.
NP_418335.4; -.
3D structure databases
ModBase P32154.
Enzyme and pathway databases
BioCyc EcoCyc:FRVB-MON; -.
Organism-specific databases
EchoBASE EB1809; -.
EcoGene EG11863; frvB.
Ontologies
GO
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from InterPro).
GO:0005886; Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0016301; Molecular function: kinase activity (inferred from electronic annotation from UniProtKB-KW).
GO:0008982; Molecular function: protein-N(PI)-phosphohistidine-sugar phosphotransferase activity (inferred from electronic annotation from InterPro).
GO:0005351; Molecular function: sugar:hydrogen symporter activity (inferred from electronic annotation from InterPro).
GO:0009401; Biological process: phosphoenolpyruvate-dependent sugar phosphotransferase system (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR013011; PTS_EIIB_2.
IPR003352; PTS_EIIC.
IPR013014; PTS_EIIC_2.
IPR003353; PTS_IIB_fruc.
IPR006327; PTS_IIC_fruc.
Graphical view of domain structure.
Pfam PF02378; PTS_EIIC; 1.
PF02379; PTS_IIB_fruc; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR00829; FRU; 1.
TIGR01427; PTS_IIC_fructo; 1.
PROSITE PS51099; PTS_EIIB_TYPE_2; 1.
PS51104; PTS_EIIC_TYPE_2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P32154.
ProtoNet P32154.
Genome annotation databases
GeneID 948390; -.
GenomeReviews U00096_GR; b3899.
AP009048_GR; JW5562.
KEGG ecj:JW5562; -.
eco:b3899; -.
Phylogenomic databases
HOGENOM P32154; -.
Genome annotation databases
CMR P32154; b3899.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cell inner membrane; Cell membrane; Complete proteome; Kinase; Membrane; Phosphotransferase system; Sugar transport; Transferase; Transmembrane; Transport.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   483  483     Fructose-like PTS system EIIBC component. PRO_0000186499
TRANSMEM   132   152  21     Potential. 
TRANSMEM   180   200  21     Potential. 
TRANSMEM   204   224  21     Potential. 
TRANSMEM   227   247  21     Potential. 
TRANSMEM   264   284  21     Potential. 
TRANSMEM   303   323  21     Potential. 
TRANSMEM   344   364  21     Potential. 
TRANSMEM   380   400  21     Potential. 
TRANSMEM   402   422  21     Potential. 
TRANSMEM   442   462  21     Potential. 
DOMAIN   1   105  105     PTS EIIB type-2. 
DOMAIN   128   475  348     PTS EIIC type-2. 
ACT_SITE   13    13        Phosphocysteine intermediate; for EIIB activity (By similarity). 
Sequence information
Length: 483 AA [This is the length of the unprocessed precursor] Molecular weight: 51120 Da [This is the MW of the unprocessed precursor] CRC64: 9B982ECDCBA1E1A4 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MESSLRIVAI TNCPAGIAHT YMVAEALEQK ARSLGHTIKV ETQGSSGVEN RLSSEEIAAA 

        70         80         90        100        110        120 
DYVILATGRG LSGDDRARFA GKKVYEIAIS QALKNIDQIF SELPTNSQLF AADSGVKLGK 

       130        140        150        160        170        180 
QEVQSGSVMS HLMAGVSAAL PFVIGGGILV ALANMLVQFG LPYTDMSKGA PSFTWVVESI 

       190        200        210        220        230        240 
GYLGFTFMIP IMGAYIASSI ADKPAFAPAF LVCYLANDKA LLGTQSGAGF LGAVVLGLAI 

       250        260        270        280        290        300 
GYFVFWFRKV RLGKALQPLL GSMLIPFVTL LVFGVLTYYV IGPVMSDLMG GLLHFLNTIP 

       310        320        330        340        350        360 
PSMKFAAAFL VGAMLAFDMG GPINKTAWFF CFSLLEKHIY DWYAIVGVVA LMPPVAAGLA 

       370        380        390        400        410        420 
TFIAPKLFTR QEKEAASSAI VVGATVATEP AIPYALAAPL PMITANTLAG GITGVLVIAF 

       430        440        450        460        470        480 
GIKRLAPGLG IFDPLIGLMS PVGSFYLVLA IGLALNISFI IVLKGLWLRR KAKAAQQELV 


HEH 

P32154 in FASTA format

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View entry in raw text format (no links)
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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