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UniProtKB/Swiss-Prot entry P23355


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

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Entry information
Entry name PTFBC_XANCP
Primary accession number P23355
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1991
Sequence was last modified on July 11, 2002 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 74)
Name and origin of the protein
Protein name PTS system fructose-specific EIIBC component
Synonyms EIIBC-Fru
EII-Fru
Includes Fructose-specific phosphotransferase enzyme IIB component
     (EC 2.7.1.69)
     (PTS system fructose-specific EIIB component)
Fructose permease IIC component
     (PTS system fructose-specific EIIC component)
Gene name
Name: fruA
OrderedLocusNames: XCC2372
From
Xanthomonas campestris pv. campestris [TaxID: 340] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; Xanthomonadaceae; Xanthomonas.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 13951 / NCIB 11803 / NRRL B-1459;
PubMed=1655739 [NCBI, ExPASy, EBI, Israel, Japan]
de Crecy-Lagard V., Bouvet O.M., Lejeune P., Danchin A.;
"Fructose catabolism in Xanthomonas campestris pv. campestris. Sequence of the PTS operon, characterization of the fructose-specific enzymes.";
J. Biol. Chem. 266:18154-18161(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 33913 / NCPPB 528 / LMG 568;
DOI=10.1038/417459a; PubMed=12024217 [NCBI, ExPASy, EBI, Israel, Japan]
da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
"Comparison of the genomes of two Xanthomonas pathogens with differing host specificities.";
Nature 417:459-463(2002).
[3]
PROTEIN SEQUENCE OF 404-547.
DOI=10.1007/BF00273939; PubMed=1650911 [NCBI, ExPASy, EBI, Israel, Japan]
de Crecy-Lagard V., Lejeune P., Bouvet O.M., Danchin A.;
"Identification of two fructose transport and phosphorylation pathways in Xanthomonas campestris pv. campestris.";
Mol. Gen. Genet. 227:465-472(1991).
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 fructose transport.
  • CATALYTIC ACTIVITY: Protein EIIB N(pi)-phospho-L-histidine/cysteine + sugar = protein EIIB + sugar phosphate.
  • SUBCELLULAR LOCATION: Cell 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
M69242; AAA27602.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE012346; AAM41650.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR B40944; B40944.
RefSeq NP_637726.1; -.
3D structure databases
ModBase P23355.
Enzyme and pathway databases
BioCyc XCAM190485:XCC2372-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: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).
ProtoNet P23355.
Genome annotation databases
GeneID 998895; -.
GenomeReviews AE008922_GR; XCC2372.
KEGG xcc:XCC2372; -.
Phylogenomic databases
HOGENOM P23355; -.
Genome annotation databases
CMR P23355; XCC2372.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cell membrane; Complete proteome; Direct protein sequencing; Kinase; Membrane; Phosphotransferase system; Repeat; Sugar transport; Transferase; Transmembrane; Transport.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   580  580     PTS system fructose-specific EIIBC component. PRO_0000186515
TRANSMEM   254   274  21     Potential. 
TRANSMEM   289   309  21     Potential. 
TRANSMEM   332   352  21     Potential. 
TRANSMEM   369   389  21     Potential. 
TRANSMEM   410   430  21     Potential. 
TRANSMEM   451   471  21     Potential. 
TRANSMEM   483   503  21     Potential. 
TRANSMEM   509   529  21     Potential. 
TRANSMEM   549   571  23     Potential. 
DOMAIN   120   215  96     PTS EIIB type-2. 
DOMAIN   243   580  338     PTS EIIC type-2. 
ACT_SITE   126   126        Phosphocysteine intermediate; for EIIB activity (By similarity). 
CONFLICT   150   150        Q -> H (in Ref. 1; AAA27602). 
CONFLICT   260   264        AGGLL -> LAACW (in Ref. 1; AAA27602). 
CONFLICT   350   350        V -> L (in Ref. 1; AAA27602). 
CONFLICT   408   409        GS -> AG (in Ref. 1; AAA27602). 
CONFLICT   494   495        VT -> DS (in Ref. 1; AAA27602). 
CONFLICT   568   568        L -> V (in Ref. 1; AAA27602). 
Sequence information
Length: 580 AA [This is the length of the unprocessed precursor] Molecular weight: 58647 Da [This is the MW of the unprocessed precursor] CRC64: E6A3B52A7F45662B [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSSSIVVIAA GERSTEAVLA AEALRRAATA AGRSVTIEIR SDQGVLGALP TELTNGAAHV 

        70         80         90        100        110        120 
LIVGDADADT ARFGDAQLLH LSLGAVLDDP AAAVSQLAAT TAPASTSATT DASGAGGKRI 

       130        140        150        160        170        180 
VAITSCPTGI AHTFMAAEGL QQAAKKLGYQ MRVETQGSVG AQDALTDEEI RAADVVIIAA 

       190        200        210        220        230        240 
DREVDLARFG GKRLFKSGTK PAINDGPALI QKALAEAGVH GGAAPVAGAN ATSDAKGNAR 

       250        260        270        280        290        300 
TGAYKHLMTG VSFMLPFVTA GGLLIALAFA LGGIYAGDDA HQGTLAWSLF QIGAKAGFTL 

       310        320        330        340        350        360 
MVPALAGYIA YSIADRPGIA PGMIGGLVAA NLNAGFLGGI IAGFIAGYGV AALNRYIKLP 

       370        380        390        400        410        420 
RNLEGLKPVL ILPVLGTLLV GLAMMYVFGQ PVADLLAWLT AWLRGMQGSS ALLLGLLLGG 

       430        440        450        460        470        480 
MMAFDMGGPV NKAAYAFSTG LIASQVYTPM AAAMVAGMTP PLGIALATWV FRNRFTVEER 

       490        500        510        520        530        540 
GSATAAGVLG LAFVTEGAIP YAARDPLRTI PALVIGSAVA GAISMTAGAE LKAPHGGIFV 

       550        560        570        580 
LLIPNAVTHL LNYVLALVVG VVVTAVALRL LKKPVADVIA 

P23355 in FASTA format

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View entry in raw text format (no links)
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