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P0AFI2 (PARC_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA topoisomerase 4 subunit A

EC=5.99.1.3
Alternative name(s):
Topoisomerase IV subunit A
Gene names
Name:parC
Ordered Locus Names:b3019, JW2987
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length752 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. MukB stimulates the relaxation activity of topoisomerase IV and also has a modest effect on decatenation. Ref.5 Ref.8 Ref.9 Ref.10

Catalytic activity

ATP-dependent breakage, passage and rejoining of double-stranded DNA. Ref.8 Ref.9 Ref.10

Enzyme regulation

Inhibited by quinolones. Ref.8

Subunit structure

Heterotetramer composed of ParC and ParE. Interacts with MukB. Ref.5 Ref.7 Ref.9 Ref.10

Subcellular location

Cell membrane; Peripheral membrane protein HAMAP-Rule MF_00936.

Sequence similarities

Belongs to the topoisomerase GyrA/ParC subunit family. ParC type 1 subfamily.

Sequence caution

The sequence AAA24297.1 differs from that shown. Reason: Frameshift at position 10.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   LigandDNA-binding
   Molecular functionIsomerase
Topoisomerase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from direct assay Ref.7. Source: GOC

DNA topological change

Inferred from direct assay Ref.10Ref.7. Source: EcoliWiki

DNA-dependent DNA replication

Inferred from Biological aspect of Ancestor. Source: RefGenome

chromosome segregation

Inferred from direct assay Ref.10. Source: EcoliWiki

plasmid partitioning

Inferred from direct assay PubMed 8104339. Source: EcoliWiki

sister chromatid cohesion

Inferred from mutant phenotype PubMed 18765793. Source: EcoliWiki

   Cellular_componentDNA topoisomerase complex (ATP-hydrolyzing)

Inferred from direct assay Ref.7. Source: EcoliWiki

chromosome

Inferred from electronic annotation. Source: InterPro

cytoplasm

Inferred from direct assay PubMed 1334483. Source: EcoliWiki

extrinsic component of plasma membrane

Inferred from direct assay PubMed 1334483. Source: EcoliWiki

nucleoid

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_functionATP binding

Inferred from electronic annotation. Source: InterPro

DNA binding

Inferred from direct assay Ref.10. Source: EcoliWiki

DNA topoisomerase type II (ATP-hydrolyzing) activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

protein binding

Inferred from physical interaction PubMed 15690043Ref.5PubMed 24097060. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

mukBP225237EBI-878544,EBI-542943

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 752752DNA topoisomerase 4 subunit A HAMAP-Rule MF_00936
PRO_0000145397

Regions

Region497 – 752256Sufficient for MukB binding HAMAP-Rule MF_00936

Sites

Active site1201O-(5'-phospho-DNA)-tyrosine intermediate By similarity
Site391Interaction with DNA By similarity
Site751Interaction with DNA By similarity
Site771Interaction with DNA By similarity
Site1191Transition state stabilizer By similarity

Experimental info

Mutagenesis801S → L: Confers resistance to quinolones. No effect on catalytic activity. Ref.8
Mutagenesis841E → K: Strongly reduced enzyme activity. Increases stability of covalent reaction intermediate with DNA. Confers resistance to quinolones. Ref.8
Mutagenesis841E → P: Confers resistance to quinolones. Ref.8

Secondary structure

....................................................................................................................... 752
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0AFI2 [UniParc].

Last modified December 20, 2005. Version 1.
Checksum: 0D4907E96CEE7086

FASTA75283,831
        10         20         30         40         50         60 
MSDMAERLAL HEFTENAYLN YSMYVIMDRA LPFIGDGLKP VQRRIVYAMS ELGLNASAKF 

        70         80         90        100        110        120 
KKSARTVGDV LGKYHPHGDS ACYEAMVLMA QPFSYRYPLV DGQGNWGAPD DPKSFAAMRY 

       130        140        150        160        170        180 
TESRLSKYSE LLLSELGQGT ADWVPNFDGT LQEPKMLPAR LPNILLNGTT GIAVGMATDI 

       190        200        210        220        230        240 
PPHNLREVAQ AAIALIDQPK TTLDQLLDIV QGPDYPTEAE IITSRAEIRK IYENGRGSVR 

       250        260        270        280        290        300 
MRAVWKKEDG AVVISALPHQ VSGARVLEQI AAQMRNKKLP MVDDLRDESD HENPTRLVIV 

       310        320        330        340        350        360 
PRSNRVDMDQ VMNHLFATTD LEKSYRINLN MIGLDGRPAV KNLLEILSEW LVFRRDTVRR 

       370        380        390        400        410        420 
RLNYRLEKVL KRLHILEGLL VAFLNIDEVI EIIRNEDEPK PALMSRFGLT ETQAEAILEL 

       430        440        450        460        470        480 
KLRHLAKLEE MKIRGEQSEL EKERDQLQGI LASERKMNNL LKKELQADAQ AYGDDRRSPL 

       490        500        510        520        530        540 
QEREEAKAMS EHDMLPSEPV TIVLSQMGWV RSAKGHDIDA PGLNYKAGDS FKAAVKGKSN 

       550        560        570        580        590        600 
QPVVFVDSTG RSYAIDPITL PSARGQGEPL TGKLTLPPGA TVDHMLMESD DQKLLMASDA 

       610        620        630        640        650        660 
GYGFVCTFND LVARNRAGKA LITLPENAHV MPPVVIEDAS DMLLAITQAG RMLMFPVSDL 

       670        680        690        700        710        720 
PQLSKGKGNK IINIPSAEAA RGEDGLAQLY VLPPQSTLTI HVGKRKIKLR PEELQKVTGE 

       730        740        750 
RGRRGTLMRG LQRIDRVEID SPRRASSGDS EE 

« Hide

References

« Hide 'large scale' references
[1]"New topoisomerase essential for chromosome segregation in E. coli."
Kato J., Nishimura Y., Imamura R., Niki H., Hiraga S., Suzuki H.
Cell 63:393-404(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]Erratum
Kato J., Nishimura Y., Imamura R., Niki H., Hiraga S., Suzuki H.
Cell 65:1289-1290(1991)
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Escherichia coli condensin MukB stimulates topoisomerase IV activity by a direct physical interaction."
Li Y., Stewart N.K., Berger A.J., Vos S., Schoeffler A.J., Berger J.M., Chait B.T., Oakley M.G.
Proc. Natl. Acad. Sci. U.S.A. 107:18832-18837(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 30-43; 97-113; 201-225 AND 552-564, FUNCTION MODIFIED BY MUKB, INTERACTION WITH MUKB.
[6]"Characterization of the Escherichia coli gene for 1-acyl-sn-glycerol-3-phosphate acyltransferase (plsC)."
Coleman J.
Mol. Gen. Genet. 232:295-303(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 724-752.
[7]"Escherichia coli topoisomerase IV. Purification, characterization, subunit structure, and subunit interactions."
Peng H., Marians K.J.
J. Biol. Chem. 268:24481-24490(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION, SUBUNIT, CHARACTERIZATION.
Strain: K12.
[8]"The Glu-84 of the ParC subunit plays critical roles in both topoisomerase IV-quinolone and topoisomerase IV-DNA interactions."
Hiasa H.
Biochemistry 41:11779-11785(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF SER-80 AND GLU-84, FUNCTION, ENZYME REGULATION, CATALYTIC ACTIVITY.
[9]"Use of divalent metal ions in the DNA cleavage reaction of topoisomerase IV."
Pitts S.L., Liou G.F., Mitchenall L.A., Burgin A.B., Maxwell A., Neuman K.C., Osheroff N.
Nucleic Acids Res. 39:4808-4817(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, CATALYTIC ACTIVITY.
[10]"The structural basis for substrate specificity in DNA topoisomerase IV."
Corbett K.D., Schoeffler A.J., Thomsen N.D., Berger J.M.
J. Mol. Biol. 351:545-561(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 27-752, FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH PARE, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M58408 Genomic DNA. Translation: AAA24297.1. Frameshift.
M63491 Genomic DNA. Translation: AAA24396.1.
U28377 Genomic DNA. Translation: AAA69187.1.
U00096 Genomic DNA. Translation: AAC76055.1.
AP009048 Genomic DNA. Translation: BAE77075.1.
L22025 Unassigned DNA. Translation: AAC36840.1.
PIRA65089.
RefSeqNP_417491.1. NC_000913.3.
YP_491211.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZVTX-ray1.70A/B497-752[»]
1ZVUX-ray3.00A27-742[»]
4MN4X-ray2.30A/B497-752[»]
ProteinModelPortalP0AFI2.
SMRP0AFI2. Positions 28-742.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-36030N.
IntActP0AFI2. 23 interactions.
MINTMINT-1227290.
STRING511145.b3019.

Chemistry

BindingDBP0AFI2.
ChEMBLCHEMBL2363076.
DrugBankDB00817. Rosoxacin.

Proteomic databases

PaxDbP0AFI2.
PRIDEP0AFI2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76055; AAC76055; b3019.
BAE77075; BAE77075; BAE77075.
GeneID12933371.
947499.
KEGGecj:Y75_p2945.
eco:b3019.
PATRIC32121452. VBIEscCol129921_3113.

Organism-specific databases

EchoBASEEB0680.
EcoGeneEG10686. parC.

Phylogenomic databases

eggNOGCOG0188.
HOGENOMHOG000076277.
KOK02621.
OMAILSEMGW.
OrthoDBEOG661H5V.
PhylomeDBP0AFI2.

Enzyme and pathway databases

BioCycEcoCyc:EG10686-MONOMER.
ECOL316407:JW2987-MONOMER.

Gene expression databases

GenevestigatorP0AFI2.

Family and domain databases

Gene3D3.30.1360.40. 1 hit.
3.90.199.10. 2 hits.
HAMAPMF_00936. ParC_type1.
InterProIPR024946. Arg_repress_C-like.
IPR006691. GyrA/parC_pinwhl.
IPR002205. Topo_IIA_A/C.
IPR013758. Topo_IIA_A/C_ab.
IPR013760. Topo_IIA_like_dom.
IPR005742. TopoIV_A_Gneg.
[Graphical view]
PfamPF03989. DNA_gyraseA_C. 2 hits.
PF00521. DNA_topoisoIV. 1 hit.
[Graphical view]
SMARTSM00434. TOP4c. 1 hit.
[Graphical view]
SUPFAMSSF56719. SSF56719. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP0AFI2.
PROP0AFI2.

Entry information

Entry namePARC_ECOLI
AccessionPrimary (citable) accession number: P0AFI2
Secondary accession number(s): O69154, P20082, Q2M9I1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: July 9, 2014
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene