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Q59961 (PARE_STRPN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 101. 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 topoisomerase 4 subunit B

EC=5.99.1.3
Alternative name(s):
Topoisomerase IV subunit B
Gene names
Name:parE
Ordered Locus Names:SP_0852
OrganismStreptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) [Complete proteome] [HAMAP]
Taxonomic identifier170187 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length647 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Topoisomerase IV is essential for chromosome segregation. It relaxes supercoiled DNA. Performs the decatenation events required during the replication of a circular DNA molecule. Ref.5 Ref.7

Catalytic activity

ATP-dependent breakage, passage and rejoining of double-stranded DNA. Ref.5 Ref.7

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+. Ref.7

Enzyme regulation

Inhibited by quinolones, such as levofloxacin. Ref.7

Subunit structure

Heterotetramer composed of ParC and ParE. Ref.5 Ref.6 Ref.7

Sequence similarities

Belongs to the type II topoisomerase family. ParE type 2 subfamily.

Contains 1 Toprim domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 647647DNA topoisomerase 4 subunit B HAMAP-Rule MF_00939
PRO_0000145443

Regions

Domain427 – 541115Toprim
Nucleotide binding118 – 1247ATP By similarity

Sites

Metal binding4331Magnesium 1; catalytic
Metal binding5061Magnesium 1; catalytic
Metal binding5061Magnesium 2
Metal binding5081Magnesium 2
Binding site111ATP By similarity
Binding site511ATP By similarity
Binding site781ATP By similarity
Binding site3441ATP By similarity
Site4581Interaction with DNA By similarity
Site4611Interaction with DNA By similarity
Site5131Interaction with DNA By similarity
Site6291Interaction with DNA By similarity

Experimental info

Sequence conflict1661P → L in CAA65022. Ref.4
Sequence conflict2171N → D Ref.1
Sequence conflict2171N → D Ref.4
Sequence conflict4601V → I Ref.1
Sequence conflict4601V → I Ref.4
Sequence conflict5681R → L in CAA65022. Ref.4
Sequence conflict6441T → A Ref.1
Sequence conflict6441T → A Ref.4

Secondary structure

.................................................. 647
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q59961 [UniParc].

Last modified September 26, 2001. Version 3.
Checksum: B688A526C9A4E7BA

FASTA64771,664
        10         20         30         40         50         60 
MSKKEININN YNDDAIQVLE GLDAVRKRPG MYIGSTDGAG LHHLVWEIVD NAVDEALSGF 

        70         80         90        100        110        120 
GDRIDVTINK DGSLTVQDHG RGMPTGMHAM GIPTVEVIFT ILHAGGKFGQ GGYKTSGGLH 

       130        140        150        160        170        180 
GVGSSVVNAL SSWLEVEITR DGAVYKQRFE NGGKPVTTLK KIGTAPKSKT GTKVTFMPDA 

       190        200        210        220        230        240 
TIFSTTDFKY NTISERLNES AFLLKNVTLS LTDKRTNEAI EFHYENGVQD FVSYLNEDKE 

       250        260        270        280        290        300 
ILTPVLYFEG EDNGFQVEVA LQYNDGFSDN ILSFVNNVRT KDGGTHETGL KSAITKVMND 

       310        320        330        340        350        360 
YARKTGLLKE KDKNLEGSDY REGLAAVLSI LVPEEHLQFE GQTKDKLGSP LARPVVDGIV 

       370        380        390        400        410        420 
ADKLTFFLME NGELASNLIR KAIKARDARE AARKARDESR NGKKNKKDKG LLSGKLTPAQ 

       430        440        450        460        470        480 
SKNPAKNELY LVEGDSAGGS AKQGRDRKFQ AILPLRGKVV NTAKAKMADI LKNEEINTMI 

       490        500        510        520        530        540 
YTIGAGVGAD FSIEDANYDK IIIMTDADTD GAHIQTLLLT FFYRYMRPLV EAGHVYIALP 

       550        560        570        580        590        600 
PLYKMSKGKG KKEEVAYAWT DGELEELRKQ FGKGATLQRY KGLGEMNADQ LWETTMNPET 

       610        620        630        640 
RTLIRVTIED LARAERRVNV LMGDKVEPRR KWIEDNVKFT LEETTVF 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of the parC and parE genes of Streptococcus pneumoniae encoding DNA topoisomerase IV: role in fluoroquinolone resistance."
Pan X., Fisher M.
J. Bacteriol. 178:4060-4069(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 7785.
[2]Pan X.
Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 329; 347 AND 351.
[3]"Complete genome sequence of a virulent isolate of Streptococcus pneumoniae."
Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D., Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J., Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D., Umayam L.A., White O., Salzberg S.L. expand/collapse author list , Lewis M.R., Radune D., Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L., McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K., Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A., Morrison D.A., Hollingshead S.K., Fraser C.M.
Science 293:498-506(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-334 / TIGR4.
[4]"ParC subunit of DNA topoisomerase IV of Streptococcus pneumoniae is a primary target of fluoroquinolones and cooperates with DNA gyrase A subunit in forming resistance phenotype."
Munoz R., de la Campa A.G.
Antimicrob. Agents Chemother. 40:2252-2257(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 93-647.
Strain: D39 / NCTC 7466 / Serotype 2.
[5]"Breakage-reunion domain of Streptococcus pneumoniae topoisomerase IV: crystal structure of a gram-positive quinolone target."
Laponogov I., Veselkov D.A., Sohi M.K., Pan X.S., Achari A., Yang C., Ferrara J.D., Fisher L.M., Sanderson M.R.
PLoS ONE 2:E301-E301(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBUNIT.
[6]"Structural insight into the quinolone-DNA cleavage complex of type IIA topoisomerases."
Laponogov I., Sohi M.K., Veselkov D.A., Pan X.S., Sawhney R., Thompson A.W., McAuley K.E., Fisher L.M., Sanderson M.R.
Nat. Struct. Mol. Biol. 16:667-669(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 404-647 IN COMPLEX WITH PARC AND DNA, SUBUNIT.
[7]"Structural basis of gate-DNA breakage and resealing by type II topoisomerases."
Laponogov I., Pan X.S., Veselkov D.A., McAuley K.E., Fisher L.M., Sanderson M.R.
PLoS ONE 5:E11338-E11338(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 404-647 IN COMPLEX WITH PARC; MAGNESIUM; LEVOFLOXACIN AND DNA, CATALYTIC ACTIVITY, FUNCTION, ENZYME REGULATION, COFACTOR, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z67739 Genomic DNA. Translation: CAA91550.2.
AE005672 Genomic DNA. Translation: AAK74981.1.
X95717 Genomic DNA. Translation: CAA65022.1.
PIRD95098.
RefSeqNP_345341.1. NC_003028.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3FOEX-ray4.00C/D404-647[»]
3FOFX-ray4.00C/D404-647[»]
3K9FX-ray2.90C/D404-647[»]
3KSAX-ray3.30C/D404-647[»]
3KSBX-ray3.50C/D404-647[»]
3LTNX-ray3.10C/D404-647[»]
3RADX-ray3.35C/D404-647[»]
3RAEX-ray2.90C/D404-647[»]
3RAFX-ray3.24C/D404-647[»]
4JUOX-ray6.53C1-647[»]
ProteinModelPortalQ59961.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-48520N.
STRING170187.SP_0852.

Chemistry

ChEMBLCHEMBL2363033.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK74981; AAK74981; SP_0852.
GeneID930802.
KEGGspn:SP_0852.
PATRIC19706089. VBIStrPne105772_0891.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0187.
HOGENOMHOG000075154.
KOK02622.
OMATDGTGLH.
OrthoDBEOG6P334W.
ProtClustDBPRK05559.

Enzyme and pathway databases

BioCycSPNE170187:GHGN-854-MONOMER.

Family and domain databases

Gene3D3.30.230.10. 1 hit.
3.30.565.10. 1 hit.
3.40.50.670. 1 hit.
HAMAPMF_00939. ParE_type2.
InterProIPR002288. DNA_gyrase_B_C.
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.
IPR005740. TopoIV_B_Gpos.
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]
SUPFAMSSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 1 hit.
SSF56719. SSF56719. 1 hit.
TIGRFAMsTIGR01058. parE_Gpos. 1 hit.
PROSITEPS00177. TOPOISOMERASE_II. 1 hit.
PS50880. TOPRIM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ59961.

Entry information

Entry namePARE_STRPN
AccessionPrimary (citable) accession number: Q59961
Secondary accession number(s): P77956
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: September 26, 2001
Last modified: April 16, 2014
This is version 101 of the entry and version 3 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references