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P21557 (GYRA_HALL2) Reviewed, UniProtKB/Swiss-Prot

Last modified July 27, 2011. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA gyrase subunit A

EC=5.99.1.3
Gene names
Name:gyrA
OrganismHaloferax lucentense (strain DSM 14919 / JCM 9276 / NCIMB 13854 / Aa 2.2) (Haloferax sp. (strain Aa 2.2))
Taxonomic identifier2254 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHaloferax

Protein attributes

Sequence length82 AA.
Sequence statusFragment.
Protein existenceInferred 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 By similarity.

Subcellular location

Cytoplasm Potential HAMAP MF_01897.

Miscellaneous

Mutations in DNA gyrase result in novobiocin resistance in halophilic archaebacteria. HAMAP MF_01897

Sequence similarities

Belongs to the topoisomerase GyrA/ParC subunit family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandATP-binding
DNA-binding
Nucleotide-binding
   Molecular functionIsomerase
Topoisomerase
Gene Ontology (GO)
   Biological processDNA topological change

Inferred from electronic annotation. Source: InterPro

   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 – ›82›82DNA gyrase subunit A HAMAP MF_01897
PRO_0000145273

Experimental info

Non-terminal residue821

Sequences

Sequence LengthMass (Da)Tools
P21557 [UniParc].

Last modified May 1, 1991. Version 1.
Checksum: 8DD3543CF5111286

FASTA828,847
        10         20         30         40         50         60 
MSSDAPDSFE PGAGIAAEVK NARIEDEMEQ SYIDYAMSVI AGRALPDVRD GLKPVHRRIL 

        70         80 
YAMHQAGVTS NSSHRKSSSI VG 

« Hide

References

[1]"Mutations in DNA gyrase result in novobiocin resistance in halophilic archaebacteria."
Holmes M.L., Dyall-Smith M.L.
J. Bacteriol. 173:642-648(1991) [PubMed: 1846146] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M38373 Genomic DNA. Translation: AAB09606.1.

3D structure databases

ProteinModelPortalP21557.
SMRP21557. Positions 42-82.
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_HALL2
AccessionPrimary (citable) accession number: P21557
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: July 27, 2011
This is version 48 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