P0C0Q9 (GYRA_STAEP) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA gyrase subunit A
EC=5.99.1.3

Gene names

Name:

gyrA

Organism

Staphylococcus epidermidis

Taxonomic identifier

1282 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcaceae › 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 By similarity. HAMAP-Rule MF_01897
Catalytic activity	ATP-dependent breakage, passage and rejoining of double-stranded DNA. HAMAP-Rule MF_01897
Subunit structure	Heterotetramer, composed of two GyrA and two GyrB chains. Within the heterotetramer, GyrA contains the active site tyrosine that forms a covalent intermediate with the DNA, while GyrB contributes the cofactor binding sites and catalyzes ATP hydrolysis By similarity.
Subcellular location	Cytoplasm Potential HAMAP-Rule 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 antibiotic Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	chromosome Inferred from electronic annotation. Source: InterPro cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA topoisomerase type II (ATP-hydrolyzing) activity Inferred 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-Rule MF_01897		PRO_0000145258
Experimental info
	Mutagenesis	84	1	S → F: Resistant to ciprofloxacin. Ref.1
	Non-terminal residue	94	1

Sequences

	Sequence		Length	Mass (Da)
	P0C0Q9 [UniParc]. Last modified November 22, 2005. Version 1. Checksum: 72862CF17C045728	FASTA	94	10,723
	10 20 30 40 50 60 MAELPQSRIN ERNITSEMRE SFLDYAMSVI VSRALPDVRD GLKPVHRRIL YGLNEQGMTP 70 80 90 DKPYKKSARI VGDVMGKYHP HGDSSIYEAM VRMA

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] [Europe PMC] [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
Gene3D	3.90.199.10. 1 hit.
HAMAP	MF_01897. GyrA.
InterPro	IPR002205. Topo_IIA_A/C. IPR013758. Topo_IIA_A/C_ab. IPR013760. Topo_IIA_like_dom. [Graphical view]
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

Integrated into UniProtKB/Swiss-Prot:	November 22, 2005
Last sequence update:	November 22, 2005
Last modified:	April 3, 2013
This is version 30 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program