Q49X35 (TOP1_STAS1) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 52.
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: DNA topoisomerase 1 EC=5.99.1.2 Alternative name(s): DNA topoisomerase I Omega-protein Relaxing enzyme Swivelase Untwisting enzyme | ||||
| Gene names |
| ||||
| Organism | Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 342451 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Staphylococcus |
Protein attributes
| Sequence length | 688 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand than undergoes passage around the unbroken strand thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone By similarity. |
| Catalytic activity | ATP-independent breakage of single-stranded DNA, followed by passage and rejoining. |
| Subunit structure | Monomer By similarity. |
| Sequence similarities | Belongs to the type IA topoisomerase family. Contains 1 Toprim domain. |
Ontologies
| Keywords | |
|---|---|
| Domain | Repeat Zinc-finger |
| Ligand | ATP-binding DNA-binding Metal-binding Nucleotide-binding Zinc |
| Molecular function | Isomerase Topoisomerase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | DNA topological change Inferred from electronic annotation. Source: InterPro |
| Cellular component | chromosome Inferred from electronic annotation. Source: InterPro |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA topoisomerase type I activityInferred from electronic annotation. Source: EC metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 688 | 688 | DNA topoisomerase 1 | PRO_0000285947 | |||||
Regions | |||||||||
| Domain | 3 – 112 | 110 | Toprim | ||||||
| Zinc finger | 576 – 602 | 27 | C4-type 1 | ||||||
| Zinc finger | 616 – 644 | 29 | C4-type 2 | ||||||
| Zinc finger | 657 – 680 | 24 | C4-type 3 | ||||||
Sites | |||||||||
| Active site | 298 | 1 | O-(5'-phospho-DNA)-tyrosine intermediate By similarity | ||||||
Sequences
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References
| [1] | "Whole genome sequence of Staphylococcus saprophyticus reveals the pathogenesis of uncomplicated urinary tract infection." Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M., Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T. Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005) [PubMed: 16135568] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 15305 / DSM 20229. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AP008934 Genomic DNA. Translation: BAE18663.1. |
| RefSeq | YP_301608.1. NC_007350.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 2GAI based on UniProtKB P46799. |
| ProteinModelPortal | Q49X35. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q49X35. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBSTAT00000048517; EBSTAP00000046886; EBSTAG00000048514. |
| GeneID | 3615164. |
| GenomeReviews | Gene locus SSP1518 in contig AP008934_GR. |
| KEGG | ssp:SSP1518. |
| NMPDR | fig|342451.4.peg.1534. |
| PATRIC | 19624626. VBIStaSap90642_1520. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0550. |
| GeneTree | EBGT00050000024420. |
| HOGENOM | HBG512935. |
| OMA | EEYWSID. |
| PhylomeDB | Q49X35. |
| ProtClustDB | PRK05582. |
Enzyme and pathway databases | |
| BioCyc | SSAP342451:SSP1518-MONOMER. |
Family and domain databases | |
| InterPro | IPR000380. Topo_IA. IPR003601. Topo_IA_2. IPR023406. Topo_IA_AS. IPR013497. Topo_IA_cen. IPR013824. Topo_IA_cen_sub1. IPR013825. Topo_IA_cen_sub2. IPR023405. Topo_IA_core_domain. IPR003602. Topo_IA_DNA-bd. IPR013498. Topo_IA_Znf. IPR005733. TopoI_bac-type. IPR006171. Toprim_domain. [Graphical view] |
| Gene3D | G3DSA:1.10.460.10. Topo_IA_cen_sub1. 3 hits. G3DSA:2.70.20.10. Topo_IA_cen_sub2. 2 hits. |
| KO | K03168. |
| PANTHER | PTHR11390. Topo_IA. 1 hit. |
| Pfam | PF01131. Topoisom_bac. 1 hit. PF01751. Toprim. 1 hit. PF01396. zf-C4_Topoisom. 2 hits. [Graphical view] |
| PRINTS | PR00417. PRTPISMRASEI. |
| SMART | SM00437. TOP1Ac. 1 hit. SM00436. TOP1Bc. 1 hit. SM00493. TOPRIM. 1 hit. [Graphical view] |
| SUPFAM | SSF56712. Topo_IA_core. 1 hit. |
| TIGRFAMs | TIGR01051. TopA_bact. 1 hit. |
| PROSITE | PS00396. TOPOISOMERASE_I_PROK. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | TOP1_STAS1 | ||||||||
| Accession | Primary (citable) accession number: Q49X35 | ||||||||
| 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 |

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