DNA topoisomerase 4 subunit B - parE - Streptococcus pneumoniae (strain ATCC BAA-255 / R6)

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Q8DQB5 (Q8DQB5_STRR6) Unreviewed, UniProtKB/TrEMBL

Last modified April 16, 2014. Version 87. History...

Clusters with 100%, 90%, 50% identity |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info Customize order

Names and origin

Protein names

Recommended 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

Organism

Streptococcus pneumoniae (strain ATCC BAA-255 / R6) [Reference proteome] [HAMAP] EMBL AAK99560.1

Taxonomic identifier

171101 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacilli › Lactobacillales › Streptococcaceae › Streptococcus ›

Protein attributes

Sequence length	647 AA.
Sequence status	Complete.
Protein existence	Evidence 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

Ontologies

Keywords
Ligand	ATP-binding HAMAP-Rule MF_00939 RuleBase RU000380 SAAS SAAS002288 DNA-binding HAMAP-Rule MF_00939 Magnesium HAMAP-Rule MF_00939 Metal-binding HAMAP-Rule MF_00939 Nucleotide-binding
Molecular function	Isomerase Topoisomerase HAMAP-Rule MF_00939 SAAS SAAS002288 RuleBase RU000380
Technical term	3D-structure PDB 4LPB PDB 4MOT PDB 4LP0 Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA topological change Inferred from electronic annotation. Source: UniProtKB-HAMAP chromosome segregation Inferred from electronic annotation. Source: UniProtKB-HAMAP
Cellular_component	chromosome Inferred from electronic annotation. Source: InterPro
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-HAMAP DNA binding Inferred from electronic annotation. Source: UniProtKB-HAMAP DNA topoisomerase type II (ATP-hydrolyzing) activity Inferred from electronic annotation. Source: UniProtKB-HAMAP magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Regions

Domain

427 – 541

115

Toprim By similarity HAMAP-Rule MF_00939

Nucleotide binding

118 – 124

ATP By similarity HAMAP-Rule MF_00939

Sites

Metal binding

433

Magnesium 1; catalytic By similarity HAMAP-Rule MF_00939

Metal binding

506

Magnesium 1; catalytic By similarity HAMAP-Rule MF_00939

Metal binding

506

Magnesium 2 By similarity HAMAP-Rule MF_00939

Metal binding

508

Magnesium 2 By similarity HAMAP-Rule MF_00939

Binding site

ATP By similarity HAMAP-Rule MF_00939

Binding site

ATP By similarity HAMAP-Rule MF_00939

Binding site

ATP By similarity HAMAP-Rule MF_00939

Binding site

344

ATP By similarity HAMAP-Rule MF_00939

Site

458

Interaction with DNA By similarity HAMAP-Rule MF_00939

Site

461

Interaction with DNA By similarity HAMAP-Rule MF_00939

Site

513

Interaction with DNA By similarity HAMAP-Rule MF_00939

Site

629

Interaction with DNA By similarity HAMAP-Rule MF_00939

Sequences

Sequence

Length

Mass (Da)

Tools

Q8DQB5 [UniParc].

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

FASTA

647

71,665

        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' referencesShow '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. 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. 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.

PIR

D97966.

RefSeq

NP_358350.1. NC_003098.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4LP0	X-ray	1.95	A	1-226	[»]
4LPB	X-ray	1.75	A	1-226	[»]
4MOT	X-ray	1.75	A	1-226	[»]

ProteinModelPortal

Q8DQB5.

ModBase

Search...

MobiDB

Search...

Protein-protein interaction databases

STRING

171101.spr0756.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAK99560; AAK99560; spr0756.

GeneID

934298.

KEGG

spr:spr0756.

PATRIC

19701428. VBIStrPne107296_0836.

Phylogenomic databases

eggNOG

COG0187.

HOGENOM

HOG000075154.

K02622.

OMA

TDGTGLH.

OrthoDB

EOG6P334W.

ProtClustDB

PRK05559.

Enzyme and pathway databases

BioCyc

SPNE171101:GJC8-763-MONOMER.

Family and domain databases

Gene3D

3.30.230.10. 1 hit.
3.30.565.10. 1 hit.
3.40.50.670. 1 hit.

HAMAP

MF_00939. ParE_type2.

InterPro

IPR002288. 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]

Pfam

PF00204. DNA_gyraseB. 1 hit.
PF00986. DNA_gyraseB_C. 1 hit.
PF02518. HATPase_c. 1 hit.
PF01751. Toprim. 1 hit.
[Graphical view]

PRINTS

PR00418. TPI2FAMILY.

SMART

SM00387. HATPase_c. 1 hit.
SM00433. TOP2c. 1 hit.
[Graphical view]

SUPFAM

SSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 1 hit.
SSF56719. SSF56719. 1 hit.

TIGRFAMs

TIGR01058. parE_Gpos. 1 hit.

PROSITE

PS00177. TOPOISOMERASE_II. 1 hit.
PS50880. TOPRIM. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

Q8DQB5_STRR6

Accession

Primary (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 status

Unreviewed (UniProtKB/TrEMBL)

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information