Reviewed,
UniProtKB/Swiss-Prot P46321 (LICR_BACSU)
Last modified
November 3, 2009.
Version 72.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Probable licABCH operon regulator Including the following 2 domains: 1- Recommended name: Putative phosphotransferase enzyme IIB component EC=2.7.1.69 Alternative name(s): Putative PTS system EIIB component 2- Recommended name: Putative phosphotransferase enzyme IIA component EC=2.7.1.- Alternative name(s): Putative PTS system EIIA component | ||||||
| Gene names |
| ||||||
| Organism | Bacillus subtilis [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 1423 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 641 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Positive regulator of the licABCH operon. |
| Catalytic activity | Protein EIIA N(pi)-phospho-L-histidine + protein EIIB = protein EIIA + protein EIIB N(pi)-phospho-L-histidine/cysteine. Protein EIIB N(pi)-phospho-L-histidine/cysteine + sugar = protein EIIB + sugar phosphate. |
| Domain | The PTS EIIB type-2 domain may serve a regulatory function, through its phosphorylation activity. The PTS EIIA type-2 domain may serve a regulatory function, through its phosphorylation activity. |
| Miscellaneous | Might be activated by phosphorylation of certain histidyl residues by HPr. |
| Sequence similarities | Belongs to the transcriptional antiterminator bglG family. Contains 2 PRD domains. Contains 1 PTS EIIA type-2 domain. Contains 1 PTS EIIB type-2 domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Transcription Transcription regulation |
| Domain | Repeat |
| Ligand | RNA-binding |
| Molecular function | Activator Kinase Transferase |
| PTM | Phosphoprotein |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | phosphoenolpyruvate-dependent sugar phosphotransferase system Inferred from electronic annotation. Source: InterPro regulation of transcription, DNA-dependentInferred from electronic annotation. Source: InterPro transcriptionInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | RNA binding Inferred from electronic annotation. Source: UniProtKB-KW kinase activityInferred 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 – 641 | 641 | Probable licABCH operon regulator | PRO_0000204245 | |||||
Regions | |||||||||
| Domain | 184 – 289 | 106 | PRD 1 | ||||||
| Domain | 296 – 403 | 108 | PRD 2 | ||||||
| Domain | 407 – 498 | 92 | PTS EIIB type-2 | ||||||
| Domain | 499 – 638 | 140 | PTS EIIA type-2 | ||||||
Amino acid modifications | |||||||||
| Modified residue | 219 | 1 | Phosphohistidine Potential | ||||||
| Modified residue | 278 | 1 | Phosphohistidine Potential | ||||||
| Modified residue | 333 | 1 | Phosphohistidine Potential | ||||||
| Modified residue | 392 | 1 | Phosphohistidine Potential | ||||||
| Modified residue | 413 | 1 | Phosphocysteine; by EIIA By similarity | ||||||
| Modified residue | 559 | 1 | Phosphohistidine; by HPr By similarity | ||||||
Experimental info | |||||||||
| Mutagenesis | 219 | 1 | H → A: Residual activity. Ref.4 | ||||||
| Mutagenesis | 219 | 1 | H → D: Loss of activity. Ref.4 | ||||||
| Mutagenesis | 278 | 1 | H → A: Loss of activity. Ref.4 | ||||||
| Mutagenesis | 278 | 1 | H → E: Loss of activity. Ref.4 | ||||||
| Mutagenesis | 333 | 1 | H → A: Loss of activity. Ref.4 | ||||||
| Mutagenesis | 392 | 1 | H → E: Loss of activity. Ref.4 | ||||||
| Mutagenesis | 392 | 1 | H → I: Residual activity. Ref.4 | ||||||
| Mutagenesis | 559 | 1 | H → G: Increase in activity. Ref.4 | ||||||
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "Identification and characterization of a new beta-glucoside utilization system in Bacillus subtilis." Tobisch S., Glaser P., Krueger S., Hecker M. J. Bacteriol. 179:496-506(1997) [PubMed: 8990303] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168. |
| [2] | "Sequencing of a 65 kb region of the Bacillus subtilis genome containing the lic and cel loci, and creation of a 177 kb contig covering the gnt-sacXY region." Yoshida K., Shindo K., Sano H., Seki S., Fujimura M., Yanai N., Miwa Y., Fujita Y. Microbiology 142:3113-3123(1996) [PubMed: 8969509] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168 / BGSC1A1. |
| [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] | "Regulation of the lic operon of Bacillus subtilis and characterization of potential phosphorylation sites of the LicR regulator protein by site-directed mutagenesis." Tobisch S., Stuelke J., Hecker M. J. Bacteriol. 181:4995-5003(1999) [PubMed: 10438772] [Abstract] Cited for: MUTAGENESIS OF HIS-219; HIS-278; HIS-333; HIS-392 AND HIS-559. |
Cross-references
Sequence databases | |
|---|---|
| Z49992 Genomic DNA. Translation: CAA90284.1. D83026 Genomic DNA. Translation: BAA11742.1. AL009126 Genomic DNA. Translation: CAB15886.1. | |
| PIR | H69651. |
| RefSeq | NP_391739.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 937383. |
| GenomeReviews | Gene locus BSU38600 in contig AL009126_GR. |
| KEGG | bsu:BSU38600. |
| NMPDR | fig|224308.1.peg.3865. |
Organism-specific databases | |
| SubtiList | BG11346. licR. [Micado] |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P46321. |
| OMA | IHIAIAL. |
Enzyme and pathway databases | |
| BioCyc | BSUB224308:BSU3856-MON. |
| BRENDA | 2.7.1.69. 150. |
Family and domain databases | |
| InterPro | IPR013196. HTH_11. IPR007737. Mga. IPR011608. PRD. IPR002178. PTS_EIIA_2. IPR013011. PTS_EIIB_2. IPR001550. Transcrpt_antitermin_CS. [Graphical view] |
| Gene3D | G3DSA:1.10.1790.10. PRD. 2 hits. G3DSA:3.40.930.10. PTS_EIIA_2. 1 hit. |
| Pfam | PF08279. HTH_11. 1 hit. PF05043. Mga. 1 hit. PF00874. PRD. 2 hits. PF00359. PTS_EIIA_2. 1 hit. [Graphical view] |
| ProDom | PD001689. PTS_EIIA_2. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| PROSITE | PS00654. PRD_1. False negative. PS51372. PRD_2. 2 hits. PS51094. PTS_EIIA_TYPE_2. 1 hit. PS51099. PTS_EIIB_TYPE_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | LICR_BACSU | ||||||||
| Accession | Primary (citable) accession number: P46321 | ||||||||
| Entry history |
| ||||||||
| 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 |
| SIMILARITY comments Index of protein domains and families |

Clusters with


