O32193 (CSSS_BACSU) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 95.
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: Sensor histidine kinase CssS EC=2.7.13.3 | ||||||
| Gene names |
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| Organism | Bacillus subtilis | ||||||
| Taxonomic identifier | 1423 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 451 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Member of the two-component regulatory system CssS/CssR required to control the cellular response to secretion stress. Required for the transcription of htrA. Could detect misfolded proteins at the membrane-cell wall interface and then activate CssR by phosphorylation. Ref.5 |
| Catalytic activity | ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. |
| Subcellular location | Cell membrane; Multi-pass membrane protein Potential. |
| Sequence similarities | Contains 1 HAMP domain. Contains 1 histidine kinase domain. |
| Sequence caution | The sequence CAB07976.1 differs from that shown. Reason: Erroneous initiation. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Two-component regulatory system |
| Cellular component | Cell membrane Membrane |
| Domain | Transmembrane Transmembrane helix |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Kinase Transferase |
| PTM | Phosphoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | peptidyl-histidine phosphorylation Inferred from electronic annotation. Source: InterPro |
| Cellular component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membraneInferred from electronic annotation. Source: UniProtKB-SubCell |
| 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 – 451 | 451 | Sensor histidine kinase CssS | PRO_0000074743 | |||||
Regions | |||||||||
| Topological domain | 1 – 9 | 9 | Cytoplasmic Potential | ||||||
| Transmembrane | 10 – 30 | 21 | Helical; Potential | ||||||
| Topological domain | 31 – 165 | 135 | Extracellular Potential | ||||||
| Transmembrane | 166 – 186 | 21 | Helical; Potential | ||||||
| Topological domain | 187 – 451 | 265 | Cytoplasmic Potential | ||||||
| Domain | 187 – 239 | 53 | HAMP | ||||||
| Domain | 247 – 451 | 205 | Histidine kinase | ||||||
Amino acid modifications | |||||||||
| Modified residue | 250 | 1 | Phosphohistidine; by autocatalysis By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 444 | 1 | T → S in CAA11751. Ref.2 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Sequencing of regions downstream of addA (98 degrees) and citG (289 degrees) in Bacillus subtilis." Medina N., Vannier F., Roche B., Autret S., Levine A., Seror S.J. Microbiology 143:3305-3308(1997) [PubMed: 9353931] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "The yvsA-yvqA (293 degrees - 289 degrees) region of the Bacillus subtilis chromosome containing genes involved in metal ion uptake and a putative sigma factor." Wipat A., Brignell C.S., Guy J.B., Rose M., Emmerson P.T., Harwood C.R. Microbiology 144:1593-1600(1998) [PubMed: 9639930] [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] | "From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later." Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A. Microbiology 155:1758-1775(2009) [PubMed: 19383706] [Abstract] Cited for: SEQUENCE REVISION TO 444. |
| [5] | "Comprehensive DNA microarray analysis of Bacillus subtilis two-component regulatory systems." Kobayashi K., Ogura M., Yamaguchi H., Yoshida K., Ogasawara N., Tanaka T., Fujita Y. J. Bacteriol. 183:7365-7370(2001) [PubMed: 11717295] [Abstract] Cited for: FUNCTION. |
| [6] | "A novel two-component regulatory system in Bacillus subtilis for the survival of severe secretion stress." Hyyrylaeinen H.-L., Bolhuis A., Darmon E., Muukkonen L., Koski P., Vitikainen M., Sarvas M., Pragai Z., Bron S., van Dijl J.M., Kontinen V.P. Mol. Microbiol. 41:1159-1172(2001) [PubMed: 11555295] [Abstract] Cited for: CHARACTERIZATION. Strain: 168. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | Z93941 Genomic DNA. Translation: CAB07976.1. Different initiation. AJ223978 Genomic DNA. Translation: CAA11751.1. AL009126 Genomic DNA. Translation: CAB15292.2. |
| PIR | D70045. |
| RefSeq | NP_391182.2. NC_000964.3. |
3D structure databases | |
| ProteinModelPortal | O32193. |
| SMR | O32193. Positions 203-451. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | O32193. 16 interactions. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBBACT00000001884; EBBACP00000001884; EBBACG00000001881. |
| GeneID | 935936. |
| GenomeReviews | Gene locus BSU33020 in contig AL009126_GR. |
| KEGG | bsu:BSU33020. |
| NMPDR | fig|224308.1.peg.3308. |
| PATRIC | 18978588. VBIBacSub10457_3457. |
Organism-specific databases | |
| GenoList | BSU33020. [Micado] |
Phylogenomic databases | |
| GeneTree | EBGT00050000000010. |
| HOGENOM | HBG338303. |
| PhylomeDB | O32193. |
| ProtClustDB | CLSK872951. |
Enzyme and pathway databases | |
| BioCyc | BSUB:BSU33020-MONOMER. |
| BRENDA | 2.7.13.3. 700. |
Family and domain databases | |
| InterPro | IPR003594. ATPase-like_ATP-bd. 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. IPR009082. Sig_transdc_His_kinase_dimeric. [Graphical view] |
| Gene3D | G3DSA:3.30.565.10. ATP_bd_ATPase. 1 hit. |
| KO | K07650. |
| 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] |
| SUPFAM | SSF55874. ATP_bd_ATPase. 1 hit. SSF47384. His_kin_homodim. 1 hit. |
| PROSITE | PS50885. HAMP. 1 hit. PS50109. HIS_KIN. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | CSSS_BACSU | ||||||||
| Accession | Primary (citable) accession number: O32193 Secondary accession number(s): O32303 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Bacillus subtilis Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList |
| SIMILARITY comments Index of protein domains and families |

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