P48371 (GYRA_NEIGO) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 54.
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 gyrase subunit A EC=5.99.1.3 | ||
| Gene names |
| ||
| Organism | Neisseria gonorrhoeae | ||
| Taxonomic identifier | 485 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria |
Protein attributes
| Sequence length | 916 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | DNA gyrase negatively supercoils closed circular double-stranded DNA in an ATP-dependent manner and also catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes and knotted rings. HAMAP MF_01897 |
| Catalytic activity | ATP-dependent breakage, passage and rejoining of double-stranded DNA. HAMAP MF_01897 |
| Subunit structure | Made up of two chains. The A chain is responsible for DNA breakage and rejoining; the B chain catalyzes ATP hydrolysis. The enzyme forms an A2B2 tetramer. |
| Subcellular location | Cytoplasm Potential HAMAP MF_01897. |
| Sequence similarities | Belongs to the topoisomerase GyrA/ParC subunit family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | ATP-binding DNA-binding Nucleotide-binding |
| Molecular function | Isomerase Topoisomerase |
| Gene Ontology (GO) | |
| Biological process | DNA topological change Inferred from electronic annotation. Source: InterPro regulation of transcription, DNA-dependentInferred from electronic annotation. Source: InterPro |
| Cellular component | chromosome Inferred from electronic annotation. Source: InterPro cytoplasmInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA topoisomerase (ATP-hydrolyzing) activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 916 | 916 | DNA gyrase subunit A HAMAP MF_01897 | PRO_0000145244 | |||||
Sites | |||||||||
| Active site | 130 | 1 | O-(5'-phospho-DNA)-tyrosine intermediate By similarity | ||||||
Sequences
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References
| [1] | "Neisseria gonorrhoeae acquires mutations in analogous regions of gyrA and parC in fluoroquinolone-resistant isolates." Belland R.J., Morrison S.G., Ison C., Huang W.M. Mol. Microbiol. 14:371-380(1994) [PubMed: 7830580] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: MS11. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U08817 Genomic DNA. Translation: AAA82128.1. |
| PIR | S60779. |
3D structure databases | |
| ProteinModelPortal | P48371. |
| SMR | P48371. Positions 38-533. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| HAMAP | MF_01897. GyrA. [Tree] |
| InterPro | IPR005743. GyrA. IPR006691. GyrA/parC_pinwhl. IPR002205. Topo_IIA_A/C. IPR013758. Topo_IIA_A/C_ab. IPR013757. Topo_IIA_A_a. IPR013760. Topo_IIA_cen. [Graphical view] |
| Gene3D | G3DSA:3.90.199.10. Topo_IIA_A/C_ab. 1 hit. G3DSA:1.10.268.10. Topo_IIA_A_a. 1 hit. |
| Pfam | PF03989. DNA_gyraseA_C. 6 hits. PF00521. DNA_topoisoIV. 1 hit. [Graphical view] |
| SMART | SM00434. TOP4c. 1 hit. [Graphical view] |
| SUPFAM | SSF56719. Topo_IIA_cen. 1 hit. |
| TIGRFAMs | TIGR01063. GyrA. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | GYRA_NEIGO | ||||||||
| Accession | Primary (citable) accession number: P48371 | ||||||||
| 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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