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P0A0K7 (GYRB_STAAW) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 56. 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 B

EC=5.99.1.3
Gene names
Name:gyrB
Ordered Locus Names:MW0005
OrganismStaphylococcus aureus (strain MW2) [Complete proteome] [HAMAP]
Taxonomic identifier196620 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length644 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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 By similarity. HAMAP-Rule MF_01898

Catalytic activity

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

Cofactor

Magnesium. Binds two Mg2+ per subunit. The magnesium ions form salt bridges with both the protein and the DNA. Can also accept other divalent metal cations, such as Mn2+ and Ca2+ By similarity.

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_01898.

Sequence similarities

Belongs to the type II topoisomerase family.

Contains 1 Toprim domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 644643DNA gyrase subunit B HAMAP-Rule MF_01898
PRO_0000145343

Regions

Domain429 – 543115Toprim

Sites

Metal binding4351Magnesium 1; catalytic By similarity
Metal binding5081Magnesium 1; catalytic By similarity
Metal binding5081Magnesium 2 By similarity
Metal binding5101Magnesium 2 By similarity
Site4601Interaction with DNA By similarity
Site4631Interaction with DNA By similarity

Sequences

Sequence LengthMass (Da)Tools
P0A0K7 [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]"Genome and virulence determinants of high virulence community-acquired MRSA."
Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y., Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.
Lancet 359:1819-1827(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MW2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000033 Genomic DNA. Translation: BAB93870.1.
RefSeqNP_644820.1. NC_003923.1.

3D structure databases

ProteinModelPortalP0A0K7.
SMRP0A0K7. Positions 14-387, 416-644.
ModBaseSearch...

Protein-protein interaction databases

STRING196620.MW0005.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB93870; BAB93870; BAB93870.
GeneID1004400.
KEGGsam:MW0005.
PATRIC19566442. VBIStaAur44266_0005.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0187.
HOGENOMHOG000075154.
KOK02470.
OMAIFETTEF.
ProtClustDBPRK05644.

Enzyme and pathway databases

BioCycSAUR196620:GJ9Z-5-MONOMER.

Family and domain databases

Gene3D3.30.230.10. 1 hit.
3.30.565.10. 1 hit.
3.40.50.670. 1 hit.
HAMAPMF_01898. GyrB.
InterProIPR002288. DNA_gyrase_B_C.
IPR011557. GyrB.
IPR003594. HATPase_ATP-bd.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR001241. Topo_IIA.
IPR013506. Topo_IIA_bsu_dom2.
IPR013759. Topo_IIA_cen_dom.
IPR013760. Topo_IIA_like_dom.
IPR018522. TopoIIA_CS.
IPR006171. Toprim_domain.
[Graphical view]
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.
PS50880. TOPRIM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBP0A0K7.

Entry information

Entry nameGYRB_STAAW
AccessionPrimary (citable) accession number: P0A0K7
Secondary accession number(s): P20832
Entry history
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: January 23, 2007
Last modified: May 1, 2013
This is version 56 of the entry and version 2 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