Reviewed,
UniProtKB/Swiss-Prot P36557 (BASS_SALTY)
Last modified
November 3, 2009.
Version 81.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Sensor protein basS EC=2.7.13.3 | ||||||
| Gene names |
| ||||||
| Organism | Salmonella typhimurium [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 90371 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella |
Protein attributes
| Sequence length | 356 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Member of the two-component regulatory system basS/basR. Autophosphorylates and activates basR by phosphorylation. Plays a role in the adaptation of the organism to the host environment, in particular to neutrophils, and therefore it plays a role in virulence as well. Ref.3 |
| Catalytic activity | ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. |
| Subcellular location | Cell inner membrane; Multi-pass membrane protein By similarity. |
| Induction | The eptA-basRS operon is positively autoregulated by basR under high iron or aluminum concentration conditions. Ref.3 |
| Post-translational modification | Autophosphorylated. Ref.3 |
| Sequence similarities | Contains 1 HAMP domain. Contains 1 histidine kinase domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Two-component regulatory system Virulence |
| Cellular component | Cell inner membrane Cell membrane Membrane |
| Domain | Transmembrane |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Kinase Transferase |
| PTM | Phosphoprotein |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | pathogenesis Inferred from electronic annotation. Source: UniProtKB-KW peptidyl-histidine phosphorylationInferred from electronic annotation. Source: InterPro two-component signal transduction system (phosphorelay)Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membraneInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW two-component sensor 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 – 356 | 356 | Sensor protein basS | PRO_0000074702 | |||||
Regions | |||||||||
| Topological domain | 1 – 13 | 13 | Cytoplasmic Potential | ||||||
| Transmembrane | 14 – 34 | 21 | Potential | ||||||
| Topological domain | 35 – 64 | 30 | Periplasmic Potential | ||||||
| Transmembrane | 65 – 88 | 24 | Potential | ||||||
| Topological domain | 89 – 356 | 268 | Cytoplasmic Potential | ||||||
| Domain | 89 – 141 | 53 | HAMP | ||||||
| Domain | 149 – 356 | 208 | Histidine kinase | ||||||
Amino acid modifications | |||||||||
| Modified residue | 152 | 1 | Phosphohistidine; by autocatalysis By similarity | ||||||
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "Spontaneous pmrA mutants of Salmonella typhimurium LT2 define a new two-component regulatory system with a possible role in virulence." Roland K.L., Martin L.E., Esther C.R., Spitznagel J.K. J. Bacteriol. 175:4154-4164(1993) [PubMed: 8391535] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: LT2. |
| [2] | "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2." McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. Wilson R.K.Nature 413:852-856(2001) [PubMed: 11677609] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: LT2 / SGSC1412 / ATCC 700720. |
| [3] | "Molecular characterization of the PmrA regulon." Woesten M.M.S.M., Groisman E.A. J. Biol. Chem. 274:27185-27190(1999) [PubMed: 10480935] [Abstract] Cited for: FUNCTION, INDUCTION, AUTOPHOSPHORYLATION. Strain: ATCC 14028s / SGSG 2262. |
Cross-references
Sequence databases | |
|---|---|
| L13395 Genomic DNA. Translation: AAA72366.1. AE006468 Genomic DNA. Translation: AAL23115.1. | |
| PIR | C40656. |
| RefSeq | NP_463156.1. |
3D structure databases | |
| ModBase | Search... |
Proteomic databases | |
| PRIDE | P36557. |
Genome annotation databases | |
| GeneID | 1255817. |
| GenomeReviews | Gene locus STM4291 in contig AE006468_GR. |
| KEGG | stm:STM4291. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P36557. |
| OMA | SANIITE. |
Enzyme and pathway databases | |
| BioCyc | STYP99287:STM4291-MON. |
| BRENDA | 2.7.13.3. 2. |
Family and domain databases | |
| InterPro | IPR003594. ATP_bd_ATPase. IPR003660. HAMP_linker_domain. IPR004358. Sig_transdc_His_kin-like_C. IPR003661. Sig_transdc_His_kin_sub1_dim/P. IPR005467. Sig_transdc_His_kinase_core. [Graphical view] |
| Gene3D | G3DSA:3.30.565.10. ATP_bd_ATPase. 1 hit. |
| Pfam | PF00672. HAMP. 1 hit. PF02518. HATPase_c. 1 hit. PF00512. HisKA. 1 hit. [Graphical view] |
| PRINTS | PR00344. BCTRLSENSOR. |
| SMART | SM00304. HAMP. 1 hit. SM00387. HATPase_c. 1 hit. SM00388. HisKA. 1 hit. [Graphical view] |
| PROSITE | PS50885. HAMP. 1 hit. PS50109. HIS_KIN. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | BASS_SALTY | ||||||||
| Accession | Primary (citable) accession number: P36557 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

Clusters with


