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UniProtKB/Swiss-Prot entry P23387


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

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Entry information
Entry name PTF3E_RHOCA
Primary accession number P23387
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1991
Sequence was last modified on November 1, 1991 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 64)
Name and origin of the protein
Protein name PTS system fructose-specific EIIBBC component
Synonym EIIBBC-Fru
Includes Fructose-specific phosphotransferase enzyme IIB component
     (EC 2.7.1.69)
     (PTS system fructose-specific EIIB component)
     (EIII-Fru)
Fructose permease IIC component
     (PTS system fructose-specific EIIC component)
Gene name
Name: fruA
From
Rhodobacter capsulatus (Rhodopseudomonas capsulata) [TaxID: 1061] 
Taxonomy Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; Rhodobacteraceae; Rhodobacter.
Protein existence 4: Predicted;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=DSM 938 / 37b4;
PubMed=2254279 [NCBI, ExPASy, EBI, Israel, Japan]
Wu L.-F., Saier M.H. Jr.;
"Nucleotide sequence of the fruA gene, encoding the fructose permease of the Rhodobacter capsulatus phosphotransferase system, and analyses of the deduced protein sequence.";
J. Bacteriol. 172:7167-7178(1990).
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 2 PTS EIIB type-2 domains.
  • SIMILARITY: Contains 1 PTS EIIC type-2 domain.
  • CAUTION: Only one of the two EIIB domains may be active since the first domain lacks the active site and is probably unable to bind and transfer a phosphate group.
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
X53150; CAA37303.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR B37852; B37852.
3D structure databases
ModBase P23387.
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; 2.
Pfam graphical view of domain structure.
TIGRFAMs TIGR00829; FRU; 1.
TIGR01427; PTS_IIC_fructo; 1.
PROSITE PS51099; PTS_EIIB_TYPE_2; 2.
PS51104; PTS_EIIC_TYPE_2; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet P23387.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cell membrane; 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   578  578     PTS system fructose-specific EIIBBC component. PRO_0000186513
TRANSMEM   251   271  21     Potential. 
TRANSMEM   284   304  21     Potential. 
TRANSMEM   319   339  21     Potential. 
TRANSMEM   364   384  21     Potential. 
TRANSMEM   405   425  21     Potential. 
TRANSMEM   428   450  23     Potential. 
TRANSMEM   477   497  21     Potential. 
TRANSMEM   518   538  21     Potential. 
TRANSMEM   545   565  21     Potential. 
DOMAIN   1    99  99     PTS EIIB type-2 1. 
DOMAIN   119   214  96     PTS EIIB type-2 2. 
DOMAIN   241   576  336     PTS EIIC type-2. 
ACT_SITE   125   125        Phosphocysteine intermediate; for EIIB activity (By similarity). 
Sequence information
Length: 578 AA [This is the length of the unprocessed precursor] Molecular weight: 58576 Da [This is the MW of the unprocessed precursor] CRC64: 87793E5AAA608E4E [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSKIVAVTAG AKGVAHTHLA AEALSATAQA LGHQIRVERH SAEGVEAPLQ GAEIAAADVV 

        70         80         90        100        110        120 
LIAADLRIED VRFVTKPVYR TSTARAVTQT AAVLAEALAL TGEETPQMTT DTGQRPLRVV 

       130        140        150        160        170        180 
AITSCPTGIA HTFMAADALK KTAAARGWEI AVETQGSVGS QNALSAAQIQ AADLVVIAAD 

       190        200        210        220        230        240 
THVDDSRFAG KKVYKTSVGA AVKGAAKVLD AALAEGVVLG TNLADTVDAL KAQRAATRSG 

       250        260        270        280        290        300 
PYMHLLTGVS YMLPLVVAGG LLIALSFVFG IKAFEVEGTL PAALMAIGGG AAFKLMVPVL 

       310        320        330        340        350        360 
AGFIAYSIAD RPGLTPGLIG GMLAVNLNAG FLGGIVAGFL AGYVARWLRD AIKLPRTLEG 

       370        380        390        400        410        420 
LKPVLILPLL STAITGLIMV YVVGTPVAAI LAAMTAFLQG LGTTNAVVLG LILGGMMAVD 

       430        440        450        460        470        480 
MGGPINKAAY TFAVGLLTSS TYAPMAAVMA AGMTPPLGLA LATLVAKNRF TAEEREAGGA 

       490        500        510        520        530        540 
AAVLGLSFIT EGAIPFAAKD PARVIPSIIV GSAITGALSM ALGCLLVAPH GGIFVLAIPH 

       550        560        570 
AVTNLGLYAL SIVVGTLVTT GLLIALKKPI PAEERARS 

P23387 in FASTA format

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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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