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P0A0K8 (GYRB_STAAU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 B

EC=5.99.1.3
Gene names
Name:gyrB
OrganismStaphylococcus aureus
Taxonomic identifier1280 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesStaphylococcus

Protein attributes

Sequence length644 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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_01898

Catalytic activity

ATP-dependent breakage, passage and rejoining of double-stranded DNA. HAMAP MF_01898

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_01898.

Sequence similarities

Belongs to the type II topoisomerase family.

Contains 1 Toprim domain.

Ontologies

Keywords
   Biological processAntibiotic resistance
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionIsomerase
Topoisomerase
   Technical term3D-structure
Direct protein sequencing
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

Initiator methionine11Removed Ref.1
Chain2 – 644643DNA gyrase subunit B HAMAP MF_01898
PRO_0000145342

Regions

Domain459 – 54082Toprim

Experimental info

Sequence conflict40 – 4910SERGLHHLVW → QRELHISV in AAA73951. Ref.3
Sequence conflict661Q → K in AAA73951. Ref.3
Sequence conflict312 – 32110KIMKEEKDRL → RYEEEKIA in AAA73951. Ref.3
Sequence conflict4241K → Q in AAA73951. Ref.3
Sequence conflict5221T → I in AAA73951. Ref.3
Sequence conflict5791R → L in AAA73951. Ref.3

Secondary structure

............................. 644
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A0K8 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: CED22E8C446A1138

FASTA64472,540
        10         20         30         40         50         60 
MVTALSDVNN TDNYGAGQIQ VLEGLEAVRK RPGMYIGSTS ERGLHHLVWE IVDNSIDEAL 

        70         80         90        100        110        120 
AGYANQIEVV IEKDNWIKVT DNGRGIPVDI QEKMGRPAVE VILTVLHAGG KFGGGGYKVS 

       130        140        150        160        170        180 
GGLHGVGSSV VNALSQDLEV YVHRNETIYH QAYKKGVPQF DLKEVGTTDK TGTVIRFKAD 

       190        200        210        220        230        240 
GEIFTETTVY NYETLQQRIR ELAFLNKGIQ ITLRDERDEE NVREDSYHYE GGIKSYVELL 

       250        260        270        280        290        300 
NENKEPIHDE PIYIHQSKDD IEVEIAIQYN SGYATNLLTY ANNIHTYEGG THEDGFKRAL 

       310        320        330        340        350        360 
TRVLNSYGLS SKIMKEEKDR LSGEDTREGM TAIISIKHGD PQFEGQTKTK LGNSEVRQVV 

       370        380        390        400        410        420 
DKLFSEHFER FLYENPQVAR TVVEKGIMAA RARVAAKKAR EVTRRKSALD VASLPGKLAD 

       430        440        450        460        470        480 
CSSKSPEECE IFLVEGDSAG GSTKSGRDSR TQAILPLRGK ILNVEKARLD RILNNNEIRQ 

       490        500        510        520        530        540 
MITAFGTGIG GDFDLAKARY HKIVIMTDAD VDGAHIRTLL LTFFYRFMRP LIEAGYVYIA 

       550        560        570        580        590        600 
QPPLYKLTQG KQKYYVYNDR ELDKLKSELN PTPKWSIARY KGLGEMNADQ LWETTMNPEH 

       610        620        630        640 
RALLQVKLED AIEADQTFEM LMGDVVENRR QFIEDNAVYA NLDF 

« Hide

References

[1]"Cloning, sequencing, and expression of the DNA gyrase genes from Staphylococcus aureus."
Brockbank S.M.V., Barth P.T.
J. Bacteriol. 175:3269-3277(1993) [PubMed: 8388872] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-27 AND 314-335.
Strain: 601055.
[2]"Quinolone resistance mutations in the DNA gyrase gyrA and gyrB genes of Staphylococcus aureus."
Ito H., Yoshida H., Bogaki-Shonai M., Niga T., Hattori H., Nakamura S.
Antimicrob. Agents Chemother. 38:2014-2023(1994) [PubMed: 7811012] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 12600 / IAM 12544 / NCTC 8532.
[3]"Nucleotide sequence of the Staphylococcus aureus gyrB-gyrA locus encoding the DNA gyrase A and B proteins."
Margerrison E.E.C., Hopewell R., Fisher L.M.
J. Bacteriol. 174:1596-1603(1992) [PubMed: 1311298] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Nucleotide sequence of the recF gene cluster from Staphylococcus aureus and complementation analysis in Bacillus subtilis recF mutants."
Alonso J.C., Fisher L.M.
Mol. Gen. Genet. 246:680-686(1995) [PubMed: 7898435] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-30.
Strain: YB886.
[5]"DNA cloning and organization of the Staphylococcus aureus gyrA and gyrB genes: close homology among gyrase proteins and implications for 4-quinolone action and resistance."
Hopewell R., Oram M., Briesewitz R., Fisher L.M.
J. Bacteriol. 172:3481-3484(1990) [PubMed: 2160946] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 593-644.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X71437 Genomic DNA. Translation: CAA50570.1.
D10489 Genomic DNA. Translation: BAA01369.1.
M86227 Genomic DNA. Translation: AAA73951.1.
M37915 Genomic DNA. Translation: AAA26635.1.
PIRA40585.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3G75X-ray2.30A/B24-230[»]
3G7BX-ray2.30A/B24-230[»]
3TTZX-ray1.63A/B14-233[»]
ProteinModelPortalP0A0K8.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

HAMAPMF_01898. GyrB.
[Tree]
InterProIPR003594. ATPase-like_ATP-bd.
IPR011557. GyrB.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR001241. Topo_IIA.
IPR013759. Topo_IIA_B/N_ab.
IPR002288. Topo_IIA_B_C.
IPR013506. Topo_IIA_bsu_dom2.
IPR013760. Topo_IIA_cen.
IPR018522. TopoIIA_CS.
IPR006171. Toprim_domain.
[Graphical view]
Gene3DG3DSA:3.30.565.10. ATP_bd_ATPase. 1 hit.
G3DSA:3.30.230.10. Ribosomal_S5_D2-type_fold. 1 hit.
G3DSA:3.40.50.670. Topo_IIA_B/N_ab. 1 hit.
PfamPF00204. DNA_gyraseB. 1 hit.
PF00986. DNA_gyraseB_C. 1 hit.
PF02518. HATPase_c. 1 hit.
PF01751. Toprim. 1 hit.
[Graphical view]
PRINTSPR00418. TPI2FAMILY.
SMARTSM00387. HATPase_c. 1 hit.
SM00433. TOP2c. 1 hit.
[Graphical view]
SUPFAMSSF55874. ATP_bd_ATPase. 1 hit.
SSF54211. Ribosomal_S5_D2-typ_fold. 1 hit.
SSF56719. Topo_IIA_cen. 1 hit.
TIGRFAMsTIGR01059. GyrB. 1 hit.
PROSITEPS00177. TOPOISOMERASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

DrugBankDB01051. Novobiocin.

Entry information

Entry nameGYRB_STAAU
AccessionPrimary (citable) accession number: P0A0K8
Secondary accession number(s): P20832
Entry history
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: January 23, 2007
Last modified: January 25, 2012
This is version 40 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families