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Q2A1P5

- Q2A1P5_FRATH

UniProt

Q2A1P5 - Q2A1P5_FRATH

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Protein

DNA topoisomerase 4 subunit B

Gene

parE

Organism
Francisella tularensis subsp. holarctica (strain LVS)
Status
Unreviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

ATP-dependent breakage, passage and rejoining of double-stranded DNA.UniRule annotation

Cofactori

Note: Magnesium. Binds two Mg(2+) per subunit. The magnesium ions form salt bridges with both the protein and the DNA. Can also accept other divalent metal cations, such as Mn(2+) and Ca(2+).UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei4 – 41ATPUniRule annotation
Binding sitei41 – 411ATPUniRule annotation
Binding sitei68 – 681ATPUniRule annotation
Binding sitei333 – 3331ATPUniRule annotation
Metal bindingi418 – 4181Magnesium 1; catalyticUniRule annotation
Sitei443 – 4431Interaction with DNAUniRule annotation
Sitei446 – 4461Interaction with DNAUniRule annotation
Metal bindingi490 – 4901Magnesium 1; catalyticUniRule annotation
Metal bindingi490 – 4901Magnesium 2UniRule annotation
Metal bindingi492 – 4921Magnesium 2UniRule annotation
Sitei497 – 4971Interaction with DNAUniRule annotation
Sitei613 – 6131Interaction with DNAUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi109 – 1157ATPUniRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. DNA binding Source: UniProtKB-HAMAP
  3. DNA topoisomerase type II (ATP-hydrolyzing) activity Source: UniProtKB-HAMAP
  4. magnesium ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. chromosome segregation Source: UniProtKB-HAMAP
  2. DNA topological change Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, TopoisomeraseUniRule annotation

Keywords - Ligandi

ATP-bindingUniRule annotation, DNA-bindingUniRule annotation, MagnesiumUniRule annotation, Metal-bindingUniRule annotation, Nucleotide-binding

Enzyme and pathway databases

BioCyciFTUL376619:GI22-1770-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA topoisomerase 4 subunit BUniRule annotation (EC:5.99.1.3UniRule annotation)
Alternative name(s):
Topoisomerase IV subunit BUniRule annotation
Gene namesi
Name:parEUniRule annotation
Ordered Locus Names:FTL_1726Imported
OrganismiFrancisella tularensis subsp. holarctica (strain LVS)Imported
Taxonomic identifieri376619 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaThiotrichalesFrancisellaceaeFrancisella
ProteomesiUP000001944: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. chromosome Source: InterPro
Complete GO annotation...

Interactioni

Subunit structurei

Heterotetramer composed of ParC and ParE.UniRule annotation

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4HXZX-ray2.70A/B1-382[»]
4HY1X-ray1.90A/B1-382[»]
4HYMX-ray1.90A/B1-382[»]
4KQVX-ray2.38A/B1-382[»]
ProteinModelPortaliQ2A1P5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini412 – 525114ToprimUniRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the type II topoisomerase family.UniRule annotation
Belongs to the type II topoisomerase family. ParE type 1 subfamily.UniRule annotation
Contains 1 Toprim domain.UniRule annotation
Contains Toprim domain.SAAS annotation

Phylogenomic databases

HOGENOMiHOG000075154.
KOiK02622.
OMAiQSYNADA.
OrthoDBiEOG6P334W.

Family and domain databases

Gene3Di3.30.230.10. 1 hit.
3.30.565.10. 1 hit.
3.40.50.670. 1 hit.
HAMAPiMF_00938. ParE_type1.
InterProiIPR002288. DNA_gyrase_B_C.
IPR003594. HATPase_C.
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.
IPR005737. TopoIV_B_Gneg.
IPR006171. Toprim_domain.
[Graphical view]
PfamiPF00204. DNA_gyraseB. 1 hit.
PF00986. DNA_gyraseB_C. 1 hit.
PF02518. HATPase_c. 1 hit.
PF01751. Toprim. 1 hit.
[Graphical view]
PRINTSiPR00418. TPI2FAMILY.
SMARTiSM00387. HATPase_c. 1 hit.
SM00433. TOP2c. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 1 hit.
SSF56719. SSF56719. 1 hit.
TIGRFAMsiTIGR01055. parE_Gneg. 1 hit.
PROSITEiPS00177. TOPOISOMERASE_II. 1 hit.
PS50880. TOPRIM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q2A1P5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQNYNAKSIE VLTGLDPVKK RPGMYTNIEN PNHLIQEIID NSVDEVLAGF
60 70 80 90 100
ASKINITLYE DNSIEVADDG RGMPVDIHPE HKMSGIELIM TKLHSGGKFS
110 120 130 140 150
NKNYTHSGGL HGVGVSVVNA LSTRLEAEIK RDGNVYHIVF EDGFKTKDLE
160 170 180 190 200
IIDNVGKKNT GTKIRFWPNK KYFDDIKVNF KALKNLLEAK AILCKALTIK
210 220 230 240 250
YSNEIKKEKL TWHFETGLKG YLDHKLEAET LPAEPFIIDN FSNGDSYLDA
260 270 280 290 300
VFCWCEDLSE SIKNSYVNLI PTPQDGTHVT GLKNGIYDAI KAYIEKNSLS
310 320 330 340 350
VKNIKITAND SFAQLNYVIS VKITNPQFAG QTKEKLSNKD VTNFVATAVK
360 370 380 390 400
DLLTIWLNQN PDEARQIVEN ISKVAQKRIN ADKKTTRKRI MNTTIRLPGK
410 420 430 440 450
LTDCISSDVN STELFIVEGD SAGGSAKQAR DKNFQAVLPL KGKILNSWEL
460 470 480 490 500
DADTIMNSQE IHNIATAIGV DPDSDDISAL RYNKICILAD ADSDGLHIAT
510 520 530 540 550
LLCAMFLKHF RKLIENGHIY IAQPPLFRID IGKSTFYALD ENERDTILTK
560 570 580 590 600
NSKLPGKVNI MRFKGLGEMN PAQLRESAMD VSSRRLLQLT ISDVYDDTEM
610 620
LDMLLAKKRA KDRRDWLENY GDRASVE
Length:627
Mass (Da):70,355
Last modified:April 4, 2006 - v1
Checksum:i4BA9C405648B7393
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM233362 Genomic DNA. Translation: CAJ80165.1.
RefSeqiYP_514357.1. NC_007880.1.

Genome annotation databases

EnsemblBacteriaiCAJ80165; CAJ80165; FTL_1726.
GeneIDi3951577.
KEGGiftl:FTL_1726.
PATRICi17944687. VBIFraTul90181_1881.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM233362 Genomic DNA. Translation: CAJ80165.1 .
RefSeqi YP_514357.1. NC_007880.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4HXZ X-ray 2.70 A/B 1-382 [» ]
4HY1 X-ray 1.90 A/B 1-382 [» ]
4HYM X-ray 1.90 A/B 1-382 [» ]
4KQV X-ray 2.38 A/B 1-382 [» ]
ProteinModelPortali Q2A1P5.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAJ80165 ; CAJ80165 ; FTL_1726 .
GeneIDi 3951577.
KEGGi ftl:FTL_1726.
PATRICi 17944687. VBIFraTul90181_1881.

Phylogenomic databases

HOGENOMi HOG000075154.
KOi K02622.
OMAi QSYNADA.
OrthoDBi EOG6P334W.

Enzyme and pathway databases

BioCyci FTUL376619:GI22-1770-MONOMER.

Family and domain databases

Gene3Di 3.30.230.10. 1 hit.
3.30.565.10. 1 hit.
3.40.50.670. 1 hit.
HAMAPi MF_00938. ParE_type1.
InterProi IPR002288. DNA_gyrase_B_C.
IPR003594. HATPase_C.
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.
IPR005737. TopoIV_B_Gneg.
IPR006171. Toprim_domain.
[Graphical view ]
Pfami PF00204. DNA_gyraseB. 1 hit.
PF00986. DNA_gyraseB_C. 1 hit.
PF02518. HATPase_c. 1 hit.
PF01751. Toprim. 1 hit.
[Graphical view ]
PRINTSi PR00418. TPI2FAMILY.
SMARTi SM00387. HATPase_c. 1 hit.
SM00433. TOP2c. 1 hit.
[Graphical view ]
SUPFAMi SSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 1 hit.
SSF56719. SSF56719. 1 hit.
TIGRFAMsi TIGR01055. parE_Gneg. 1 hit.
PROSITEi PS00177. TOPOISOMERASE_II. 1 hit.
PS50880. TOPRIM. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Complete genome sequence of Francisella tularensis LVS (Live Vaccine Strain)."
    Chain P., Larimer F., Land M., Stilwagen S., Larsson P., Bearden S., Chu M., Oyston P., Forsman M., Andersson S., Lindler L., Titball R., Garcia E.
    Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: LVSImported.
  2. "Pyrrolopyrimidine inhibitors of DNA gyrase B (GyrB) and topoisomerase IV (ParE). Part I: Structure guided discovery and optimization of dual targeting agents with potent, broad-spectrum enzymatic activity."
    Tari L.W., Trzoss M., Bensen D.C., Li X., Chen Z., Lam T., Zhang J., Creighton C.J., Cunningham M.L., Kwan B., Stidham M., Shaw K.J., Lightstone F.C., Wong S.E., Nguyen T.B., Nix J., Finn J.
    Bioorg. Med. Chem. Lett. 23:1529-1536(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-382.
  3. "A new class of type iia topoisomerase inhibitors withbroad-spectrum antibacterial activity."
    Tari L.W., Bensen D.C., Finn J.
    Submitted (MAY-2013) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 1-382.

Entry informationi

Entry nameiQ2A1P5_FRATH
AccessioniPrimary (citable) accession number: Q2A1P5
Entry historyi
Integrated into UniProtKB/TrEMBL: April 4, 2006
Last sequence update: April 4, 2006
Last modified: November 26, 2014
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureImported, Complete proteomeImported

External Data

Dasty 3