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P0C0Q9 (GYRA_STAEP) Reviewed, UniProtKB/Swiss-Prot

Last modified July 27, 2011. Version 24. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
DNA gyrase subunit A

EC=5.99.1.3
Gene names
Name:gyrA
OrganismStaphylococcus epidermidis
Taxonomic identifier1282 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesStaphylococcus

Protein attributes

Sequence length94 AA.
Sequence statusFragment.
Protein existenceEvidence 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 processAntibiotic resistance
   Cellular componentCytoplasm
   LigandATP-binding
DNA-binding
Nucleotide-binding
   Molecular functionIsomerase
Topoisomerase
Gene Ontology (GO)
   Biological processDNA topological change

Inferred from electronic annotation. Source: InterPro

response to antibiotic

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentchromosome

Inferred from electronic annotation. Source: InterPro

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA topoisomerase (ATP-hydrolyzing) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›94›94DNA gyrase subunit A HAMAP MF_01897
PRO_0000145258

Experimental info

Mutagenesis841S → F: Resistant to ciprofloxacin. Ref.1
Non-terminal residue941

Sequences

Sequence LengthMass (Da)Tools
P0C0Q9 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: 72862CF17C045728

FASTA9410,723
        10         20         30         40         50         60 
MAELPQSRIN ERNITSEMRE SFLDYAMSVI VSRALPDVRD GLKPVHRRIL YGLNEQGMTP 

        70         80         90 
DKPYKKSARI VGDVMGKYHP HGDSSIYEAM VRMA 

« Hide

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.
PIRA49832.

3D structure databases

ProteinModelPortalP0C0Q9.
SMRP0C0Q9. Positions 31-94.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

HAMAPMF_01897. GyrA.
[Tree]
InterProIPR002205. Topo_IIA_A/C.
IPR013758. Topo_IIA_A/C_ab.
IPR013760. Topo_IIA_cen.
[Graphical view]
Gene3DG3DSA:3.90.199.10. Topo_IIA_A/C_ab. 1 hit.
PfamPF00521. DNA_topoisoIV. 1 hit.
[Graphical view]
SUPFAMSSF56719. Topo_IIA_cen. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGYRA_STAEP
AccessionPrimary (citable) accession number: P0C0Q9
Secondary accession number(s): P54112
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: November 22, 2005
Last modified: July 27, 2011
This is version 24 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families