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P72525 (PARC_STRPN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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:SP_0855
OrganismStreptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) [Complete proteome] [HAMAP]
Taxonomic identifier170187 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length823 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. Ref.6 Ref.8

Catalytic activity

ATP-dependent breakage, passage and rejoining of double-stranded DNA. Ref.6 Ref.8

Enzyme regulation

Inhibited by quinolones, such as levofloxacin. Ref.8

Subunit structure

Heterotetramer composed of ParC and ParE. Ref.6 Ref.8

Subcellular location

Cell membrane; Peripheral membrane protein By similarity HAMAP-Rule MF_00937.

Sequence similarities

Belongs to the topoisomerase GyrA/ParC subunit family. ParC type 2 subfamily.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 823823DNA topoisomerase 4 subunit A HAMAP-Rule MF_00937
PRO_0000145418

Sites

Active site1181O-(5'-phospho-DNA)-tyrosine intermediate Ref.8
Site381Interaction with DNA
Site741Interaction with DNA
Site761Interaction with DNA
Site871Interaction with DNA
Site931Interaction with DNA
Site1171Transition state stabilizer

Experimental info

Sequence conflict951R → C in AAB08038. Ref.5
Sequence conflict2571I → T Ref.1
Sequence conflict2571I → T Ref.4
Sequence conflict3621R → P in CAA65021. Ref.4
Sequence conflict3731H → R in CAA65021. Ref.4
Sequence conflict4011A → P in CAA65021. Ref.4
Sequence conflict4731K → N in CAA65021. Ref.4
Sequence conflict5891E → A in CAA65021. Ref.4
Sequence conflict6081V → A in CAA65021. Ref.4

Secondary structure

................................................................................. 823
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P72525 [UniParc].

Last modified September 26, 2001. Version 3.
Checksum: D4D17BD5DED63C05

FASTA82393,133
        10         20         30         40         50         60 
MSNIQNMSLE DIMGERFGRY SKYIIQDRAL PDIRDGLKPV QRRILYSMNK DSNTFDKSYR 

        70         80         90        100        110        120 
KSAKSVGNIM GNFHPHGDSS IYDAMVRMSQ NWKNREILVE MHGNNGSMDG DPPAAMRYTE 

       130        140        150        160        170        180 
ARLSEIAGYL LQDIEKKTVP FAWNFDDTEK EPTVLPAAFP NLLVNGSTGI SAGYATDIPP 

       190        200        210        220        230        240 
HNLAEVIDAA VYMIDHPTAK IDKLMEFLPG PDFPTGAIIQ GRDEIKKAYE TGKGRVVVRS 

       250        260        270        280        290        300 
KTEIEKLKGG KEQIVIIEIP YEINKANLVK KIDDVRVNNK VAGIAEVRDE SDRDGLRIAI 

       310        320        330        340        350        360 
ELKKDANTEL VLNYLFKYTD LQINYNFNMV AIDNFTPRQV GIVPILSSYI AHRREVILAR 

       370        380        390        400        410        420 
SRFDKEKAEK RLHIVEGLIR VISILDEVIA LIRASENKAD AKENLKVSYD FTEEQAEAIV 

       430        440        450        460        470        480 
TLQLYRLTNT DVVVLQEEEA ELREKIAMLA AIIGDERTMY NLMKKELREV KKKFATPRLS 

       490        500        510        520        530        540 
SLEDTAKAIE IDTASLIAEE DTYVSVTKAG YIKRTSPRSF AASTLEEIGK RDDDRLIFVQ 

       550        560        570        580        590        600 
SAKTTQHLLM FTSLGNVIYR PIHELADIRW KDIGEHLSQT ITNFETNEEI LYVEVLDQFD 

       610        620        630        640        650        660 
DATTYFAVTR LGQIKRVERK EFTPWRTYRS KSVKYAKLKD DTDQIVAVAP IKLDDVVLVS 

       670        680        690        700        710        720 
QNGYALRFNI EEVPVVGAKA AGVKAMNLKE DDVLQSGFIC NTSSFYLLTQ RGSLKRVSIE 

       730        740        750        760        770        780 
EILATSRAKR GLQVLRELKN KPHRVFLAGA VAEQGFVGDF FSTEVDVNDQ TLLVQSNKGT 

       790        800        810        820 
IYESRLQDLN LSERTSNGSF ISDTISDEEV FDAYLQEVVT EDK 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of the parC and parE genes of Streptococcus pneumoniae encoding DNA topoisomerase IV: role in fluoroquinolone resistance."
Pan X., Fisher M.
J. Bacteriol. 178:4060-4069(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 7785.
[2]Pan X.
Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 636-643.
[3]"Complete genome sequence of a virulent isolate of Streptococcus pneumoniae."
Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D., Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J., Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D., Umayam L.A., White O., Salzberg S.L. expand/collapse author list , Lewis M.R., Radune D., Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L., McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K., Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A., Morrison D.A., Hollingshead S.K., Fraser C.M.
Science 293:498-506(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-334 / TIGR4.
[4]"ParC subunit of DNA topoisomerase IV of Streptococcus pneumoniae is a primary target of fluoroquinolones and cooperates with DNA gyrase A subunit in forming resistance phenotype."
Munoz R., de la Campa A.G.
Antimicrob. Agents Chemother. 40:2252-2257(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-620.
Strain: D39 / NCTC 7466 / Serotype 2.
[5]"Contribution of mutations in gyrA and parC genes to fluoroquinolone resistance of mutants of Streptococcus pneumoniae obtained in vivo and in vitro."
Tankovic J., Perichon B., Duval J., Courvalin P.
Antimicrob. Agents Chemother. 40:2505-2510(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-106.
Strain: BM4203.
[6]"Breakage-reunion domain of Streptococcus pneumoniae topoisomerase IV: crystal structure of a gram-positive quinolone target."
Laponogov I., Veselkov D.A., Sohi M.K., Pan X.S., Achari A., Yang C., Ferrara J.D., Fisher L.M., Sanderson M.R.
PLoS ONE 2:E301-E301(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.67 ANGSTROMS) OF 1-488, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT.
[7]"Structural insight into the quinolone-DNA cleavage complex of type IIA topoisomerases."
Laponogov I., Sohi M.K., Veselkov D.A., Pan X.S., Sawhney R., Thompson A.W., McAuley K.E., Fisher L.M., Sanderson M.R.
Nat. Struct. Mol. Biol. 16:667-669(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 1-488.
[8]"Structural basis of gate-DNA breakage and resealing by type II topoisomerases."
Laponogov I., Pan X.S., Veselkov D.A., McAuley K.E., Fisher L.M., Sanderson M.R.
PLoS ONE 5:E11338-E11338(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-488 IN COMPLEX WITH PARE; LEVOFLOXACIN AND DNA, CATALYTIC ACTIVITY, FUNCTION, ACTIVE SITE, ENZYME REGULATION, COFACTOR, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z67739 Genomic DNA. Translation: CAA91551.2.
AE005672 Genomic DNA. Translation: AAK74984.1.
X95717 Genomic DNA. Translation: CAA65021.1.
U49088 Genomic DNA. Translation: AAB08038.1.
PIRG95098.
RefSeqNP_345344.1. NC_003028.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2NOVX-ray2.67A/B/C/D1-488[»]
3FOEX-ray4.00A/B1-488[»]
3FOFX-ray4.00A/B1-488[»]
3K9FX-ray2.90A/B1-488[»]
3KSAX-ray3.30A/B1-488[»]
3KSBX-ray3.50A/B1-488[»]
3LTNX-ray3.10A/B1-488[»]
3RADX-ray3.35A/B1-488[»]
3RAEX-ray2.90A/B1-488[»]
3RAFX-ray3.24A/B1-488[»]
4JUOX-ray6.53A1-488[»]
ProteinModelPortalP72525.
SMRP72525. Positions 29-482.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-48521N.
STRING170187.SP_0855.

Chemistry

ChEMBLCHEMBL2363033.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK74984; AAK74984; SP_0855.
GeneID930805.
KEGGspn:SP_0855.
PATRIC19706095. VBIStrPne105772_0894.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0188.
HOGENOMHOG000076279.
KOK02621.
OMAFNMVAIH.
OrthoDBEOG661H5V.
ProtClustDBPRK05561.

Enzyme and pathway databases

BioCycSPNE170187:GHGN-857-MONOMER.

Family and domain databases

Gene3D3.30.1360.40. 1 hit.
3.90.199.10. 2 hits.
HAMAPMF_00937. ParC_type2.
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.
IPR005741. TopoIV_A_Gpos.
[Graphical view]
PfamPF03989. DNA_gyraseA_C. 5 hits.
PF00521. DNA_topoisoIV. 1 hit.
[Graphical view]
SMARTSM00434. TOP4c. 1 hit.
[Graphical view]
SUPFAMSSF56719. SSF56719. 1 hit.
TIGRFAMsTIGR01061. parC_Gpos. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP72525.

Entry information

Entry namePARC_STRPN
AccessionPrimary (citable) accession number: P72525
Secondary accession number(s): P72537, Q54917
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: September 26, 2001
Last modified: April 16, 2014
This is version 109 of the entry and version 3 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