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UniProtKB/Swiss-Prot entry P26380


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

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Entry information
Entry name PTFB_BACSU
Primary accession number P26380
Secondary accession numbers None
Integrated into Swiss-Prot on August 1, 1992
Sequence was last modified on August 1, 1992 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 73)
Name and origin of the protein
Protein name Fructose-specific phosphotransferase enzyme IIB component
Synonyms EC 2.7.1.69
PTS system fructose-specific EIIB component
EIIB-Fru
p18
Gene name
Name: levE
Synonyms: sacL
OrderedLocusNames: BSU27060
From
Bacillus subtilis [TaxID: 1423] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
DOI=10.1016/0022-2836(90)90284-S; PubMed=2117666 [NCBI, ExPASy, EBI, Israel, Japan]
Martin-Verstraete I., Debarbouille M., Klier A., Rapoport G.;
"Levanase operon of Bacillus subtilis includes a fructose-specific phosphotransferase system regulating the expression of the operon.";
J. Mol. Biol. 214:657-671(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
PubMed=9141695 [NCBI, ExPASy, EBI, Israel, Japan]
Parro V., San Roman M., Galindo I., Purnelle B., Bolotin A., Sorokin A., Mellado R.P.;
"A 23911 bp region of the Bacillus subtilis genome comprising genes located upstream and downstream of the lev operon.";
Microbiology 143:1321-1326(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
DOI=10.1038/36786; PubMed=9384377 [NCBI, ExPASy, EBI, Israel, Japan]
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.;
"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis.";
Nature 390:249-256(1997).
[4]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
DOI=10.1006/jmbi.1997.1544; PubMed=9551099 [NCBI, ExPASy, EBI, Israel, Japan]
Schauder S., Nunn R.S., Lanz R., Erni B., Schirmer T.;
"Crystal structure of the IIB subunit of a fructose permease (IIBLev) from Bacillus subtilis.";
J. Mol. Biol. 276:591-602(1998).
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.
  • FUNCTION: LevD and levE act as negative regulators of the levanase operon. They may be involved in a PTS-mediated phosphorylation of a regulator.
  • CATALYTIC ACTIVITY: Protein EIIB N(pi)-phospho-L-histidine/cysteine + sugar = protein EIIB + sugar phosphate.
  • SUBCELLULAR LOCATION: Cytoplasm.
  • 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-4 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
X56098; CAA39578.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X92868; CAA63462.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z99117; CAB14648.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S11399; S11399.
RefSeq NP_390584.1; -.
3D structure databases
PDB
1BLE; X-ray; 2.90 A; A=1-163.[ExPASy / RCSB / EBI]
PDBsum 1BLE; -.
ModBase P26380.
Enzyme and pathway databases
BioCyc BSUB224308:BSU2702-MON; -.
Organism-specific databases
SubtiList BG10317; levE. [Micado]
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (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 UniProtKB-KW).
GO:0009401; Biological process: phosphoenolpyruvate-dependent sugar phosphotransferase system (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR004720; PTS_IIB_sorb.
Graphical view of domain structure.
Gene3D G3DSA:3.40.35.10; PTS_IIB_sorb; 1.
Pfam PF03830; PTSIIB_sorb; 1.
Pfam graphical view of domain structure.
ProDom PD008332; PTSIIB_sorb; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR00854; pts-sorbose; 1.
PROSITE PS51101; PTS_EIIB_TYPE_4; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P26380.
ProtoNet P26380.
Genome annotation databases
GeneID 937078; -.
GenomeReviews AL009126_GR; BSU27060.
KEGG bsu:BSU27060; -.
NMPDR fig|224308.1.peg.2709; -.
Phylogenomic databases
HOGENOM P26380; -.
Other
LinkHub P26380; -.
Genome annotation databases
CMR P26380; BSU27060.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Cytoplasm; Kinase; Phosphotransferase system; Sugar transport; Transferase; Transport.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   163  163     Fructose-specific phosphotransferase enzyme IIB component. PRO_0000186524
DOMAIN   1   163  163     PTS EIIB type-4. 
ACT_SITE   15    15        Pros-phosphohistidine intermediate (By similarity). 
STRAND   3    10  8      
HELIX   18    26  9      
STRAND   29    34  6      
HELIX   36    40  5      
HELIX   42    49  8      
STRAND   56    61  6      
HELIX   63    71  9      
TURN   74    77  4      
STRAND   79    87  9      
HELIX   88    94  7      
TURN   95    97  3      
STRAND   102   108  7      
STRAND   114   116  3      
STRAND   118   123  6      
HELIX   125   136  12      
STRAND   140   143  4      
HELIX   154   159  6      
Sequence information
Length: 163 AA [This is the length of the unprocessed precursor] Molecular weight: 18215 Da [This is the MW of the unprocessed precursor] CRC64: F3C10058A8333177 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MMNIVLARID DRFIHGQILT RWIKVHAADR IIVVSDDIAQ DEMRKTLILS VAPSNVKASA 

        70         80         90        100        110        120 
VSVSKMAKAF HSPRYEGVTA MLLFENPSDI VSLIEAGVPI KTVNVGGMRF ENHRRQITKS 

       130        140        150        160 
VSVTEQDIKA FETLSDKGVK LELRQLPSDA SEDFVQILRN VTK 

P26380 in FASTA format

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View entry in raw text format (no links)
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