Reviewed,
UniProtKB/Swiss-Prot P26380 (PTFB_BACSU)
Last modified
February 9, 2010.
Version 82.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Fructose-specific phosphotransferase enzyme IIB component EC=2.7.1.69 Alternative name(s): PTS system fructose-specific EIIB component EIIB-Fru p18 | ||||||
| Gene names |
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| Organism | Bacillus subtilis [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 1423 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 163 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level. |
General annotation (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. 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 | |
| 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. |
| Sequence similarities | Contains 1 PTS EIIB type-4 domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Phosphotransferase system Sugar transport Transport |
| Cellular component | Cytoplasm |
| Molecular function | Kinase Transferase |
| Technical term | 3D-structure Complete proteome |
| Gene Ontology (GO) | |
| Biological process | phosphoenolpyruvate-dependent sugar phosphotransferase system Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | kinase activity Inferred from electronic annotation. Source: UniProtKB-KW protein-N(PI)-phosphohistidine-sugar phosphotransferase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 163 | 163 | Fructose-specific phosphotransferase enzyme IIB component | PRO_0000186524 | |||||||||||||||||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||||||||||||||||
| Domain | 1 – 163 | 163 | PTS EIIB type-4 | ||||||||||||||||||||||||||||||||||||||
Sites | |||||||||||||||||||||||||||||||||||||||||
| Active site | 15 | 1 | Pros-phosphohistidine intermediate By similarity | ||||||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 3 – 10 | 8 | |||||||||||||||||||||||||||||||||||||||
| Helix | 18 – 26 | 9 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 29 – 34 | 6 | |||||||||||||||||||||||||||||||||||||||
| Helix | 36 – 40 | 5 | |||||||||||||||||||||||||||||||||||||||
| Helix | 42 – 49 | 8 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 56 – 61 | 6 | |||||||||||||||||||||||||||||||||||||||
| Helix | 63 – 71 | 9 | |||||||||||||||||||||||||||||||||||||||
| Turn | 74 – 77 | 4 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 79 – 87 | 9 | |||||||||||||||||||||||||||||||||||||||
| Helix | 88 – 94 | 7 | |||||||||||||||||||||||||||||||||||||||
| Turn | 95 – 97 | 3 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 102 – 108 | 7 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 114 – 116 | 3 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 118 – 123 | 6 | |||||||||||||||||||||||||||||||||||||||
| Helix | 125 – 136 | 12 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 140 – 143 | 4 | |||||||||||||||||||||||||||||||||||||||
| Helix | 154 – 159 | 6 | |||||||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Levanase operon of Bacillus subtilis includes a fructose-specific phosphotransferase system regulating the expression of the operon." Martin-Verstraete I., Debarbouille M., Klier A., Rapoport G. J. Mol. Biol. 214:657-671(1990) [PubMed: 2117666] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168. |
| [2] | "A 23911 bp region of the Bacillus subtilis genome comprising genes located upstream and downstream of the lev operon." Parro V., San Roman M., Galindo I., Purnelle B., Bolotin A., Sorokin A., Mellado R.P. Microbiology 143:1321-1326(1997) [PubMed: 9141695] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168. |
| [3] | "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." 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. Danchin A.Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168. |
| [4] | "Crystal structure of the IIB subunit of a fructose permease (IIBLev) from Bacillus subtilis." Schauder S., Nunn R.S., Lanz R., Erni B., Schirmer T. J. Mol. Biol. 276:591-602(1998) [PubMed: 9551099] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS). |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | X56098 Genomic DNA. Translation: CAA39578.1. X92868 Genomic DNA. Translation: CAA63462.1. Different initiation. AL009126 Genomic DNA. Translation: CAB14648.1. Different initiation. | ||||||||||||
| PIR | S11399. | ||||||||||||
| RefSeq | NP_390584.1. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
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| ModBase | Search... | ||||||||||||
Protein family/group databases | |||||||||||||
| TCDB | 4.A.6.1.2. PTS mannose-fructose-sorbose (Man) family. | ||||||||||||
Genome annotation databases | |||||||||||||
| GeneID | 937078. | ||||||||||||
| GenomeReviews | Gene locus BSU27060 in contig AL009126_GR. | ||||||||||||
| KEGG | bsu:BSU27060. | ||||||||||||
| NMPDR | fig|224308.1.peg.2709. | ||||||||||||
Organism-specific databases | |||||||||||||
| SubtiList | BG10317. levE. [Micado] | ||||||||||||
| CMR | Search... | ||||||||||||
Phylogenomic databases | |||||||||||||
| HOGENOM | HBG702768. | ||||||||||||
| PhylomeDB | P26380. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BRENDA | 2.7.1.69. 150. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR004720. PTS_IIB_sorbose-sp. IPR018455. PTS_IIB_sorbose-sp_subgr. [Graphical view] | ||||||||||||
| Gene3D | G3DSA:3.40.35.10. PTS_IIB_sorb. 1 hit. | ||||||||||||
| Pfam | PF03830. PTSIIB_sorb. 1 hit. [Graphical view] | ||||||||||||
| TIGRFAMs | TIGR00854. pts-sorbose. 1 hit. | ||||||||||||
| PROSITE | PS51101. PTS_EIIB_TYPE_4. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | PTFB_BACSU | ||||||||
| Accession | Primary (citable) accession number: P26380 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Bacillus subtilis Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


