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Q2A1P5 (Q2A1P5_FRATH) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 64. 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_00938

EC=5.99.1.3 HAMAP-Rule MF_00938
Alternative name(s):
Topoisomerase IV subunit B HAMAP-Rule MF_00938
Gene names
Name:parE HAMAP-Rule MF_00938
Ordered Locus Names:FTL_1726 EMBL CAJ80165.1
OrganismFrancisella tularensis subsp. holarctica (strain LVS) [Complete proteome] [HAMAP] EMBL CAJ80165.1
Taxonomic identifier376619 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaThiotrichalesFrancisellaceaeFrancisella

Protein attributes

Sequence length627 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_00938

Catalytic activity

ATP-dependent breakage, passage and rejoining of double-stranded DNA. HAMAP-Rule MF_00938

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_00938

Subunit structure

Heterotetramer composed of ParC and ParE By similarity. HAMAP-Rule MF_00938

Sequence similarities

Belongs to the type II topoisomerase family. RuleBase RU000380

Belongs to the type II topoisomerase family. ParE type 1 subfamily. HAMAP-Rule MF_00938

Contains 1 Toprim domain. HAMAP-Rule MF_00938

Contains Toprim domain. SAAS SAAS002288

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Domain412 – 525114Toprim By similarity HAMAP-Rule MF_00938
Nucleotide binding109 – 1157ATP By similarity HAMAP-Rule MF_00938

Sites

Metal binding4181Magnesium 1; catalytic By similarity HAMAP-Rule MF_00938
Metal binding4901Magnesium 1; catalytic By similarity HAMAP-Rule MF_00938
Metal binding4901Magnesium 2 By similarity HAMAP-Rule MF_00938
Metal binding4921Magnesium 2 By similarity HAMAP-Rule MF_00938
Binding site41ATP By similarity HAMAP-Rule MF_00938
Binding site411ATP By similarity HAMAP-Rule MF_00938
Binding site681ATP By similarity HAMAP-Rule MF_00938
Binding site3331ATP By similarity HAMAP-Rule MF_00938
Site4431Interaction with DNA By similarity HAMAP-Rule MF_00938
Site4461Interaction with DNA By similarity HAMAP-Rule MF_00938
Site4971Interaction with DNA By similarity HAMAP-Rule MF_00938
Site6131Interaction with DNA By similarity HAMAP-Rule MF_00938

Sequences

Sequence LengthMass (Da)Tools
Q2A1P5 [UniParc].

Last modified April 4, 2006. Version 1.
Checksum: 4BA9C405648B7393

FASTA62770,355
        10         20         30         40         50         60 
MQNYNAKSIE VLTGLDPVKK RPGMYTNIEN PNHLIQEIID NSVDEVLAGF ASKINITLYE 

        70         80         90        100        110        120 
DNSIEVADDG RGMPVDIHPE HKMSGIELIM TKLHSGGKFS NKNYTHSGGL HGVGVSVVNA 

       130        140        150        160        170        180 
LSTRLEAEIK RDGNVYHIVF EDGFKTKDLE IIDNVGKKNT GTKIRFWPNK KYFDDIKVNF 

       190        200        210        220        230        240 
KALKNLLEAK AILCKALTIK YSNEIKKEKL TWHFETGLKG YLDHKLEAET LPAEPFIIDN 

       250        260        270        280        290        300 
FSNGDSYLDA VFCWCEDLSE SIKNSYVNLI PTPQDGTHVT GLKNGIYDAI KAYIEKNSLS 

       310        320        330        340        350        360 
VKNIKITAND SFAQLNYVIS VKITNPQFAG QTKEKLSNKD VTNFVATAVK DLLTIWLNQN 

       370        380        390        400        410        420 
PDEARQIVEN ISKVAQKRIN ADKKTTRKRI MNTTIRLPGK LTDCISSDVN STELFIVEGD 

       430        440        450        460        470        480 
SAGGSAKQAR DKNFQAVLPL KGKILNSWEL DADTIMNSQE IHNIATAIGV DPDSDDISAL 

       490        500        510        520        530        540 
RYNKICILAD ADSDGLHIAT LLCAMFLKHF RKLIENGHIY IAQPPLFRID IGKSTFYALD 

       550        560        570        580        590        600 
ENERDTILTK NSKLPGKVNI MRFKGLGEMN PAQLRESAMD VSSRRLLQLT ISDVYDDTEM 

       610        620 
LDMLLAKKRA KDRRDWLENY GDRASVE 

« Hide

References

« Hide 'large scale' references
[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: LVS EMBL CAJ80165.1.
[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM233362 Genomic DNA. Translation: CAJ80165.1.
RefSeqYP_514357.1. NC_007880.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4HXZX-ray2.70A/B1-382[»]
4HY1X-ray1.90A/B1-382[»]
4HYMX-ray1.90A/B1-382[»]
4KQVX-ray2.38A/B1-382[»]
ProteinModelPortalQ2A1P5.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAJ80165; CAJ80165; FTL_1726.
GeneID3951577.
KEGGftl:FTL_1726.
PATRIC17944687. VBIFraTul90181_1881.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000075154.
KOK02622.
OMAQSYNADA.
OrthoDBEOG6P334W.

Enzyme and pathway databases

BioCycFTUL376619:GI22-1770-MONOMER.

Family and domain databases

Gene3D3.30.230.10. 1 hit.
3.30.565.10. 1 hit.
3.40.50.670. 1 hit.
HAMAPMF_00938. ParE_type1.
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.
IPR005737. TopoIV_B_Gneg.
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.
TIGRFAMsTIGR01055. parE_Gneg. 1 hit.
PROSITEPS00177. TOPOISOMERASE_II. 1 hit.
PS50880. TOPRIM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQ2A1P5_FRATH
AccessionPrimary (citable) accession number: Q2A1P5
Entry history
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 statusUnreviewed (UniProtKB/TrEMBL)