Q4L9Y1 (PTMCB_STAHJ) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 49.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: PTS system mannitol-specific EIICB component Alternative name(s): EIICB-Mtl Short name=EII-Mtl Including the following 2 domains:
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| Gene names |
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| Organism | Staphylococcus haemolyticus (strain JCSC1435) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 279808 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Staphylococcus |
Protein attributes
| Sequence length | 519 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
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 mannitol transport. |
| Catalytic activity | Protein EIIB N(pi)-phospho-L-histidine/cysteine + sugar = protein EIIB + sugar phosphate. |
| Subunit structure | Homodimer By similarity. |
| Subcellular location | Cell membrane; Multi-pass membrane protein Potential. |
| Domain | The EIIC domain forms the PTS system translocation channel and contains the specific substrate-binding site. 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-2 domain. Contains 1 PTS EIIC type-2 domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Phosphotransferase system Sugar transport Transport |
| Cellular component | Cell membrane Membrane |
| Domain | Transmembrane Transmembrane helix |
| Molecular function | Kinase Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | phosphoenolpyruvate-dependent sugar phosphotransferase system Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membraneInferred 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 sugar:hydrogen symporter activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 519 | 519 | PTS system mannitol-specific EIICB component | PRO_0000186627 | |||||
Regions | |||||||||
| Transmembrane | 25 – 45 | 21 | Helical; Potential | ||||||
| Transmembrane | 55 – 75 | 21 | Helical; Potential | ||||||
| Transmembrane | 95 – 115 | 21 | Helical; Potential | ||||||
| Transmembrane | 145 – 165 | 21 | Helical; Potential | ||||||
| Transmembrane | 168 – 188 | 21 | Helical; Potential | ||||||
| Transmembrane | 221 – 241 | 21 | Helical; Potential | ||||||
| Transmembrane | 250 – 272 | 23 | Helical; Potential | ||||||
| Transmembrane | 277 – 299 | 23 | Helical; Potential | ||||||
| Transmembrane | 321 – 341 | 21 | Helical; Potential | ||||||
| Domain | 19 – 351 | 333 | PTS EIIC type-2 | ||||||
| Domain | 425 – 519 | 95 | PTS EIIB type-2 | ||||||
Sites | |||||||||
| Active site | 431 | 1 | Phosphocysteine intermediate; for EIIB activity By similarity | ||||||
Sequences
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References
| [1] | "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the extreme plasticity of its genome and the evolution of human-colonizing staphylococcal species." Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y., Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C., Hiramatsu K. J. Bacteriol. 187:7292-7308(2005) [PubMed: 16237012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: JCSC1435. |
Cross-references
Sequence databases | |
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| EMBL GenBank DDBJ | AP006716 Genomic DNA. Translation: BAE03544.1. |
| RefSeq | YP_252150.1. NC_007168.1. |
3D structure databases | |
| ProteinModelPortal | Q4L9Y1. |
| SMR | Q4L9Y1. Positions 422-517. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q4L9Y1. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBSTAT00000046498; EBSTAP00000044949; EBSTAG00000046495. |
| GeneID | 3482069. |
| GenomeReviews | Gene locus SH0235 in contig AP006716_GR. |
| KEGG | sha:SH0235. |
| NMPDR | fig|279808.3.peg.248. |
| PATRIC | 19616501. VBIStaHae67511_0227. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG2213. |
| GeneTree | EBGT00050000024561. |
| HOGENOM | HBG296680. |
| OMA | ITHKDLT. |
| PhylomeDB | Q4L9Y1. |
| ProtClustDB | CLSK2460866. |
Enzyme and pathway databases | |
| BioCyc | SHAE279808:SH0235-MONOMER. |
Family and domain databases | |
| InterPro | IPR013011. PTS_EIIB_2. IPR003501. PTS_EIIB_2/3. IPR003352. PTS_EIIC. IPR013014. PTS_EIIC_2. IPR004718. PTS_IIC_mtl. [Graphical view] |
| KO | K02799. K02800. |
| Pfam | PF02378. PTS_EIIC. 1 hit. PF02302. PTS_IIB. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00851. MtlA. 1 hit. |
| PROSITE | PS51099. PTS_EIIB_TYPE_2. 1 hit. PS51104. PTS_EIIC_TYPE_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PTMCB_STAHJ | ||||||||
| Accession | Primary (citable) accession number: Q4L9Y1 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with