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Q8DQB5 (Q8DQB5_STRR6) Unreviewed, UniProtKB/TrEMBL

Last modified April 16, 2014. Version 87. 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 AAK99560.1
Ordered Locus Names:spr0756 EMBL AAK99560.1
OrganismStreptococcus pneumoniae (strain ATCC BAA-255 / R6) [Reference proteome] [HAMAP] EMBL AAK99560.1
Taxonomic identifier171101 [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. 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
Q8DQB5 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 0AF7382C72772713

FASTA64771,665
        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 KIGTALKSKT 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

« Hide 'large scale' references
[1]"Genome of the bacterium Streptococcus pneumoniae strain R6."
Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S., DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C., Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J., Lee L.N. expand/collapse author list , Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M., McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B., Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y., Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R., Rosteck P.R. Jr., Skatrud P.L., Glass J.I.
J. Bacteriol. 183:5709-5717(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-255 / R6.
[2]"Fragment-to-hit-to-lead discovery of a novel pyridylurea scaffold of ATP competitive dual targeting type II topoisomerase inhibiting antibacterial agents."
Basarab G.S., Manchester J.I., Bist S., Boriack-Sjodin P.A., Dangel B., Illingworth R., Sherer B.A., Sriram S., Uria-Nickelsen M., Eakin A.E.
J. Med. Chem. 56:8712-8735(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 1-226.
[3]"Thiazolopyridone ureas as DNA gyrase B inhibitors: Optimization of antitubercular activity and efficacy."
Kale R.R., Kale M.G., Waterson D., Raichurkar A., Hameed S.P., Manjunatha M.R., Kishore Reddy B.K., Malolanarasimhan K., Shinde V., Koushik K., Jena L.K., Menasinakai S., Humnabadkar V., Madhavapeddi P., Basavarajappa H., Sharma S., Nandishaiah R., Mahesh Kumar K.N. expand/collapse author list , Ganguly S., Ahuja V., Gaonkar S., Naveen Kumar C.N., Ogg D., Boriack-Sjodin P.A., Sambandamurthy V.K., de Sousa S.M., Ghorpade S.R.
Bioorg. Med. Chem. Lett. 24:870-879(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 1-226.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE007317 Genomic DNA. Translation: AAK99560.1.
PIRD97966.
RefSeqNP_358350.1. NC_003098.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4LP0X-ray1.95A1-226[»]
4LPBX-ray1.75A1-226[»]
4MOTX-ray1.75A1-226[»]
ProteinModelPortalQ8DQB5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING171101.spr0756.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK99560; AAK99560; spr0756.
GeneID934298.
KEGGspr:spr0756.
PATRIC19701428. VBIStrPne107296_0836.

Phylogenomic databases

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

Enzyme and pathway databases

BioCycSPNE171101:GJC8-763-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...

Entry information

Entry nameQ8DQB5_STRR6
AccessionPrimary (citable) accession number: Q8DQB5
Entry history
Integrated into UniProtKB/TrEMBL: March 1, 2003
Last sequence update: March 1, 2003
Last modified: April 16, 2014
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)