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Q2A1P5

- Q2A1P5_FRATH

UniProt

Q2A1P5 - Q2A1P5_FRATH

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Protein
DNA topoisomerase 4 subunit B
Gene
parE, FTL_1726
Organism
Francisella tularensis subsp. holarctica (strain LVS)
Status
Unreviewed - Annotation score: 4 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 By similarity.UniRule annotation

Catalytic activityi

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

Cofactori

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.UniRule annotation

Sites

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi109 – 1157ATP By similarityUniRule 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
Complete GO annotation...

GO - Biological processi

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

Keywords - Molecular functioni

Isomerase, TopoisomeraseUniRule annotationSAAS annotations

Keywords - Ligandi

ATP-bindingUniRule annotationSAAS annotations, 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 B
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 By similarity.UniRule annotation

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini412 – 525114Toprim By similarityUniRule annotation
Add
BLAST

Sequence similaritiesi

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

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_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.
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

MQNYNAKSIE VLTGLDPVKK RPGMYTNIEN PNHLIQEIID NSVDEVLAGF    50
ASKINITLYE DNSIEVADDG RGMPVDIHPE HKMSGIELIM TKLHSGGKFS 100
NKNYTHSGGL HGVGVSVVNA LSTRLEAEIK RDGNVYHIVF EDGFKTKDLE 150
IIDNVGKKNT GTKIRFWPNK KYFDDIKVNF KALKNLLEAK AILCKALTIK 200
YSNEIKKEKL TWHFETGLKG YLDHKLEAET LPAEPFIIDN FSNGDSYLDA 250
VFCWCEDLSE SIKNSYVNLI PTPQDGTHVT GLKNGIYDAI KAYIEKNSLS 300
VKNIKITAND SFAQLNYVIS VKITNPQFAG QTKEKLSNKD VTNFVATAVK 350
DLLTIWLNQN PDEARQIVEN ISKVAQKRIN ADKKTTRKRI MNTTIRLPGK 400
LTDCISSDVN STELFIVEGD SAGGSAKQAR DKNFQAVLPL KGKILNSWEL 450
DADTIMNSQE IHNIATAIGV DPDSDDISAL RYNKICILAD ADSDGLHIAT 500
LLCAMFLKHF RKLIENGHIY IAQPPLFRID IGKSTFYALD ENERDTILTK 550
NSKLPGKVNI MRFKGLGEMN PAQLRESAMD VSSRRLLQLT ISDVYDDTEM 600
LDMLLAKKRA KDRRDWLENY GDRASVE 627
Length:627
Mass (Da):70,355
Last modified:April 4, 2006 - v1
Checksum:i4BA9C405648B7393
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AM233362 Genomic DNA. Translation: CAJ80165.1 .
RefSeqi YP_514357.1. NC_007880.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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...

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_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.
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: June 11, 2014
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureImported, Complete proteome

External Data

Dasty 3

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