P0C0Q9 (GYRA_STAEP) Reviewed, UniProtKB/Swiss-Prot
Last modified
July 27, 2011.
Version 24.
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 | Staphylococcus epidermidis | ||
| Taxonomic identifier | 1282 [NCBI] | ||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Staphylococcus |
Protein attributes
| Sequence length | 94 AA. |
| Sequence status | Fragment. |
| Protein existence | Evidence at protein level |
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 | |
|---|---|
| Biological process | Antibiotic resistance |
| 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 response to antibioticInferred from electronic annotation. Source: UniProtKB-KW |
| 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 – ›94 | ›94 | DNA gyrase subunit A HAMAP MF_01897 | PRO_0000145258 | |||||
Experimental info | |||||||||
| Mutagenesis | 84 | 1 | S → F: Resistant to ciprofloxacin. Ref.1 | ||||||
| Non-terminal residue | 94 | 1 | |||||||
Sequences
References
| [1] | "Ciprofloxacin resistance in coagulase-positive and -negative staphylococci: role of mutations at serine 84 in the DNA gyrase A protein of Staphylococcus aureus and Staphylococcus epidermidis." Sreedharan S., Peterson L.R., Fisher L.M. Antimicrob. Agents Chemother. 35:2151-2154(1991) [PubMed: 1662027] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF SER-84. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | S72603 Genomic DNA. Translation: AAB20672.1. |
| PIR | A49832. |
3D structure databases | |
| ProteinModelPortal | P0C0Q9. |
| SMR | P0C0Q9. Positions 31-94. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| HAMAP | MF_01897. GyrA. [Tree] |
| InterPro | IPR002205. Topo_IIA_A/C. IPR013758. Topo_IIA_A/C_ab. IPR013760. Topo_IIA_cen. [Graphical view] |
| Gene3D | G3DSA:3.90.199.10. Topo_IIA_A/C_ab. 1 hit. |
| Pfam | PF00521. DNA_topoisoIV. 1 hit. [Graphical view] |
| SUPFAM | SSF56719. Topo_IIA_cen. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | GYRA_STAEP | ||||||||
| Accession | Primary (citable) accession number: P0C0Q9 Secondary accession number(s): P54112 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with