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UniProtKB/Swiss-Prot entry P69788


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

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Entry information
Entry name PTGCB_ECO57
Primary accession number P69788
Secondary accession number P05053
Integrated into Swiss-Prot on August 13, 1987
Sequence was last modified on August 13, 1987 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 31)
Name and origin of the protein
Protein name PTS system glucose-specific EIICB component
Synonyms EIICB-Glc
EII-Glc
Includes Glucose permease IIC component
     (PTS system glucose-specific EIIC component)
Glucose-specific phosphotransferase enzyme IIB component
     (EC 2.7.1.69)
     (PTS system glucose-specific EIIB component)
Gene name
Name: ptsG
OrderedLocusNames: Z1740, ECs1479
From
Escherichia coli O157:H7 [TaxID: 83334] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
DOI=10.1038/35054089; PubMed=11206551 [NCBI, ExPASy, EBI, Israel, Japan]
Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R.;
"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
Nature 409:529-533(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
DOI=10.1093/dnares/8.1.11; PubMed=11258796 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S., Shiba T., Hattori M., Shinagawa H.;
"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12.";
DNA Res. 8:11-22(2001).
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. This system is involved in glucose transport. This enzyme is also a chemoreceptor monitoring the environment for changes in sugar concentration (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 (By similarity).
  • DOMAIN: The EIIC domain forms the PTS system translocation channel and contains the specific substrate-binding site.
  • 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.
  • SIMILARITY: Contains 1 PTS EIIB type-1 domain.
  • SIMILARITY: Contains 1 PTS EIIC type-1 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
AE005174; AAG55847.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BA000007; BAB34902.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR G90813; G90813.
RefSeq NP_287235.1; -.
NP_309506.1; -.
3D structure databases
SMR P69788; 400-476.
ModBase P69788.
Enzyme and pathway databases
BioCyc ECOL83334:ECS1479-MON; -.
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:0005355; Molecular function: glucose transmembrane transporter activity (inferred from electronic annotation from InterPro).
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:0015758; Biological process: glucose transport (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 IPR001996; PTS_EIIB.
IPR003352; PTS_EIIC.
IPR013013; PTS_EIIC_1.
IPR011535; PTS_Glc-like_IIB_component.
IPR011299; PTS_IIBC_glc.
IPR004719; PTS_IIC_glc.
Graphical view of domain structure.
Gene3D G3DSA:3.30.1360.60; PTS_EIIB; 1.
Pfam PF00367; PTS_EIIB; 1.
PF02378; PTS_EIIC; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR00826; EIIB_glc; 1.
TIGR00852; pts-Glc; 1.
TIGR02002; PTS-II-BC-glcB; 1.
PROSITE PS51098; PTS_EIIB_TYPE_1; 1.
PS01035; PTS_EIIB_TYPE_1_CYS; 1.
PS51103; PTS_EIIC_TYPE_1; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet P69788.
Genome annotation databases
GeneID 912363; -.
959449; -.
GenomeReviews BA000007_GR; ECs1479.
AE005174_GR; Z1740.
KEGG ece:Z1740; -.
ecs:ECs1479; -.
Phylogenomic databases
HOGENOM P69788; -.
Genome annotation databases
CMR P69788; Z1740.
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   477  477     PTS system glucose-specific EIICB component. PRO_0000186530
TOPO_DOM   1    14  14     Cytoplasmic (Potential). 
TRANSMEM   15    35  21     Potential. 
TOPO_DOM   36    50  15     Periplasmic (Potential). 
TRANSMEM   51    71  21     Potential. 
TOPO_DOM   72    79  8     Cytoplasmic (Potential). 
TRANSMEM   80   100  21     Potential. 
TOPO_DOM   101   111  11     Periplasmic (Potential). 
TRANSMEM   112   132  21     Potential. 
TOPO_DOM   133   151  19     Cytoplasmic (Potential). 
TRANSMEM   152   172  21     Potential. 
TOPO_DOM   173   190  18     Periplasmic (Potential). 
TRANSMEM   191   211  21     Potential. 
TOPO_DOM   212   249  38     Cytoplasmic (Potential). 
TRANSMEM   250   270  21     Potential. 
TOPO_DOM   271   279  9     Periplasmic (Potential). 
TRANSMEM   280   300  21     Potential. 
TOPO_DOM   301   309  9     Cytoplasmic (Potential). 
TRANSMEM   310   330  21     Potential. 
TOPO_DOM   331   355  25     Periplasmic (Potential). 
TRANSMEM   356   376  21     Potential. 
TOPO_DOM   377   477  101     Cytoplasmic (Potential). 
DOMAIN   1   388  388     PTS EIIC type-1. 
DOMAIN   399   477  79     PTS EIIB type-1. 
ACT_SITE   421   421        Phosphocysteine intermediate; for EIIB activity (By similarity). 
Sequence information
Length: 477 AA [This is the length of the unprocessed precursor] Molecular weight: 50677 Da [This is the MW of the unprocessed precursor] CRC64: D97A80FD64B74F73 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MFKNAFANLQ KVGKSLMLPV SVLPIAGILL GVGSANFSWL PAVVSHVMAE AGGSVFANMP 

        70         80         90        100        110        120 
LIFAIGVALG FTNNDGVSAL AAVVAYGIMV KTMAVVAPLV LHLPAEEIAS KHLADTGVLG 

       130        140        150        160        170        180 
GIISGAIAAY MFNRFYRIKL PEYLGFFAGK RFVPIISGLA AIFTGVVLSF IWPPIGSAIQ 

       190        200        210        220        230        240 
TFSQWAAYQN PVVAFGIYGF IERCLVPFGL HHIWNVPFQM QIGEYTNAAG QVFHGDIPRY 

       250        260        270        280        290        300 
MAGDPTAGKL SGGFLFKMYG LPAAAIAIWH SAKPENRAKV GGIMISAALT SFLTGITEPI 

       310        320        330        340        350        360 
EFSFMFVAPI LYIIHAILAG LAFPICILLG MRDGTSFSHG LIDFIVLSGN SSKLWLFPIV 

       370        380        390        400        410        420 
GIGYAIVYYT IFRVLIKALD LKTPGREDAT EDAKATGTSE MAPALVAAFG GKENITNLDA 

       430        440        450        460        470 
CITRLRVSVA DVSKVDQAGL KKLGAAGVVV AGSGVQAIFG TKSDNLKTEM DEYIRNH 

P69788 in FASTA format

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