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Q3HZ71 (Q3HZ71_STREE) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 67. Feed History...

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

Names and origin

Protein namesRecommended name:
DNA topoisomerase 4 subunit B HAMAP-Rule MF_00939

EC=5.99.1.3 HAMAP-Rule MF_00939
Alternative name(s):
Topoisomerase IV subunit B HAMAP-Rule MF_00939
Gene names
Name:parE HAMAP-Rule MF_00939 EMBL AAZ93056.1
OrganismStreptococcus pneumoniae EMBL AAZ93056.1
Taxonomic identifier1313 [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 By similarity. HAMAP-Rule MF_00939

Catalytic activity

ATP-dependent breakage, passage and rejoining of double-stranded DNA. HAMAP-Rule MF_00939

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. HAMAP-Rule MF_00939

Subunit structure

Heterotetramer composed of ParC and ParE By similarity. HAMAP-Rule MF_00939

Sequence similarities

Belongs to the type II topoisomerase family. RuleBase RU000380

Belongs to the type II topoisomerase family. ParE type 2 subfamily. HAMAP-Rule MF_00939

Contains 1 Toprim domain. HAMAP-Rule MF_00939

Contains Toprim domain. SAAS SAAS002288

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Domain427 – 541115Toprim By similarity HAMAP-Rule MF_00939
Nucleotide binding118 – 1247ATP By similarity HAMAP-Rule MF_00939

Sites

Metal binding4331Magnesium 1; catalytic By similarity HAMAP-Rule MF_00939
Metal binding5061Magnesium 1; catalytic By similarity HAMAP-Rule MF_00939
Metal binding5061Magnesium 2 By similarity HAMAP-Rule MF_00939
Metal binding5081Magnesium 2 By similarity HAMAP-Rule MF_00939
Binding site111ATP By similarity HAMAP-Rule MF_00939
Binding site511ATP By similarity HAMAP-Rule MF_00939
Binding site781ATP By similarity HAMAP-Rule MF_00939
Binding site3441ATP By similarity HAMAP-Rule MF_00939
Site4581Interaction with DNA By similarity HAMAP-Rule MF_00939
Site4611Interaction with DNA By similarity HAMAP-Rule MF_00939
Site5131Interaction with DNA By similarity HAMAP-Rule MF_00939
Site6291Interaction with DNA By similarity HAMAP-Rule MF_00939

Sequences

Sequence LengthMass (Da)Tools
Q3HZ71 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: DB5CF701D5F80AB4

FASTA64771,649
        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 LTDKRTDEAI 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 AILPLRGKVI 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 LEEATVF 

« Hide

References

[1]"Molecular evolution perspectives on intraspecific lateral DNA transfer of topoisomerase and gyrase loci in Streptococcus pneumoniae, with implications for fluoroquinolone resistance development and spread."
Stanhope M.J., Walsh S.L., Becker J.A., Italia M.J., Ingraham K.A., Gwynn M.N., Mathie T., Poupard J.A., Miller L.A., Brown J.R., Amrine-Madsen H.
Antimicrob. Agents Chemother. 49:4315-4326(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: 0.15GR00S EMBL AAZ93046.1, 0.68Oh92S EMBL AAZ93056.1, 128.2Ca00S EMBL AAZ93059.1, 292.1AT96S EMBL AAZ93064.1, 543.1Ca99S EMBL AAZ93074.1, 588.1JA99S EMBL AAZ93080.1, 672.1US00S EMBL AAZ93086.1 and 68.1SW99S EMBL AAZ93089.1.
[2]"Structure of an 'open' clamp type II topoisomerase-DNA complex provides a mechanism for DNA capture and transport."
Laponogov I., Veselkov D.A., Crevel I.M., Pan X.S., Fisher L.M., Sanderson M.R.
Nucleic Acids Res. 41:9911-9923(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.70 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ175245 Genomic DNA. Translation: AAZ93046.1.
DQ175255 Genomic DNA. Translation: AAZ93056.1.
DQ175258 Genomic DNA. Translation: AAZ93059.1.
DQ175263 Genomic DNA. Translation: AAZ93064.1.
DQ175273 Genomic DNA. Translation: AAZ93074.1.
DQ175279 Genomic DNA. Translation: AAZ93080.1.
DQ175285 Genomic DNA. Translation: AAZ93086.1.
DQ175288 Genomic DNA. Translation: AAZ93089.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4I3HX-ray3.70A/B1-647[»]
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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...

Entry information

Entry nameQ3HZ71_STREE
AccessionPrimary (citable) accession number: Q3HZ71
Entry history
Integrated into UniProtKB/TrEMBL: November 8, 2005
Last sequence update: November 8, 2005
Last modified: June 11, 2014
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)