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P72525

- PARC_STRPN

UniProt

P72525 - PARC_STRPN

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Protein

DNA topoisomerase 4 subunit A

Gene

parC

Organism
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Status
Reviewed - Annotation score: 5 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.2 PublicationsUniRule annotation

Catalytic activityi

ATP-dependent breakage, passage and rejoining of double-stranded DNA.2 PublicationsUniRule annotation

Enzyme regulationi

Inhibited by quinolones, such as levofloxacin.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei38 – 381Interaction with DNA
Sitei74 – 741Interaction with DNA
Sitei76 – 761Interaction with DNA
Sitei87 – 871Interaction with DNA
Sitei93 – 931Interaction with DNA
Sitei117 – 1171Transition state stabilizer
Active sitei118 – 1181O-(5'-phospho-DNA)-tyrosine intermediate1 PublicationUniRule annotation

GO - Molecular functioni

  1. ATP binding Source: InterPro
  2. DNA binding Source: UniProtKB-HAMAP
  3. DNA topoisomerase type II (ATP-hydrolyzing) activity 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, Topoisomerase

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciSPNE170187:GHGN-857-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA topoisomerase 4 subunit AUniRule annotation (EC:5.99.1.3UniRule annotation)
Alternative name(s):
Topoisomerase IV subunit AUniRule annotation
Gene namesi
Name:parCUniRule annotation
Ordered Locus Names:SP_0855
OrganismiStreptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Taxonomic identifieri170187 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
ProteomesiUP000000585: Chromosome

Subcellular locationi

Cell membrane UniRule annotation; Peripheral membrane protein UniRule annotation

GO - Cellular componenti

  1. chromosome Source: InterPro
  2. extrinsic component of plasma membrane Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 823823DNA topoisomerase 4 subunit APRO_0000145418Add
BLAST

Interactioni

Subunit structurei

Heterotetramer composed of ParC and ParE.2 PublicationsUniRule annotation

Protein-protein interaction databases

DIPiDIP-48521N.
STRINGi170187.SP_0855.

Structurei

Secondary structure

1
823
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 85Combined sources
Helixi9 – 2618Combined sources
Turni27 – 293Combined sources
Turni33 – 353Combined sources
Helixi39 – 5012Combined sources
Helixi62 – 7211Combined sources
Helixi78 – 8811Combined sources
Turni91 – 933Combined sources
Beta strandi98 – 1036Combined sources
Turni116 – 1183Combined sources
Beta strandi120 – 1234Combined sources
Helixi125 – 1306Combined sources
Turni131 – 1333Combined sources
Helixi134 – 1363Combined sources
Beta strandi141 – 1433Combined sources
Beta strandi147 – 1548Combined sources
Helixi161 – 1655Combined sources
Beta strandi167 – 1704Combined sources
Beta strandi175 – 1784Combined sources
Helixi183 – 19513Combined sources
Beta strandi196 – 1983Combined sources
Helixi201 – 2077Combined sources
Beta strandi218 – 2203Combined sources
Helixi222 – 23110Combined sources
Beta strandi232 – 2398Combined sources
Beta strandi241 – 2477Combined sources
Turni248 – 2503Combined sources
Beta strandi251 – 2588Combined sources
Helixi265 – 27713Combined sources
Beta strandi280 – 2834Combined sources
Beta strandi286 – 2894Combined sources
Beta strandi298 – 3014Combined sources
Helixi308 – 31811Combined sources
Beta strandi322 – 3287Combined sources
Beta strandi330 – 3334Combined sources
Beta strandi336 – 3394Combined sources
Helixi342 – 38342Combined sources
Helixi385 – 39410Combined sources
Beta strandi395 – 3973Combined sources
Helixi398 – 40912Combined sources
Helixi413 – 4208Combined sources
Helixi424 – 4285Combined sources
Helixi432 – 45423Combined sources
Helixi456 – 47419Combined sources
Beta strandi480 – 4823Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP72525.
SMRiP72525. Positions 29-482.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP72525.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0188.
HOGENOMiHOG000076279.
KOiK02621.
OMAiHIVEGLM.
OrthoDBiEOG661H5V.

Family and domain databases

Gene3Di3.30.1360.40. 1 hit.
3.90.199.10. 2 hits.
HAMAPiMF_00937. ParC_type2.
InterProiIPR024946. 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]
PfamiPF03989. DNA_gyraseA_C. 5 hits.
PF00521. DNA_topoisoIV. 1 hit.
[Graphical view]
SMARTiSM00434. TOP4c. 1 hit.
[Graphical view]
SUPFAMiSSF56719. SSF56719. 1 hit.
TIGRFAMsiTIGR01061. parC_Gpos. 1 hit.

Sequencei

Sequence statusi: Complete.

P72525-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSNIQNMSLE DIMGERFGRY SKYIIQDRAL PDIRDGLKPV QRRILYSMNK
60 70 80 90 100
DSNTFDKSYR KSAKSVGNIM GNFHPHGDSS IYDAMVRMSQ NWKNREILVE
110 120 130 140 150
MHGNNGSMDG DPPAAMRYTE ARLSEIAGYL LQDIEKKTVP FAWNFDDTEK
160 170 180 190 200
EPTVLPAAFP NLLVNGSTGI SAGYATDIPP HNLAEVIDAA VYMIDHPTAK
210 220 230 240 250
IDKLMEFLPG PDFPTGAIIQ GRDEIKKAYE TGKGRVVVRS KTEIEKLKGG
260 270 280 290 300
KEQIVIIEIP YEINKANLVK KIDDVRVNNK VAGIAEVRDE SDRDGLRIAI
310 320 330 340 350
ELKKDANTEL VLNYLFKYTD LQINYNFNMV AIDNFTPRQV GIVPILSSYI
360 370 380 390 400
AHRREVILAR SRFDKEKAEK RLHIVEGLIR VISILDEVIA LIRASENKAD
410 420 430 440 450
AKENLKVSYD FTEEQAEAIV TLQLYRLTNT DVVVLQEEEA ELREKIAMLA
460 470 480 490 500
AIIGDERTMY NLMKKELREV KKKFATPRLS SLEDTAKAIE IDTASLIAEE
510 520 530 540 550
DTYVSVTKAG YIKRTSPRSF AASTLEEIGK RDDDRLIFVQ SAKTTQHLLM
560 570 580 590 600
FTSLGNVIYR PIHELADIRW KDIGEHLSQT ITNFETNEEI LYVEVLDQFD
610 620 630 640 650
DATTYFAVTR LGQIKRVERK EFTPWRTYRS KSVKYAKLKD DTDQIVAVAP
660 670 680 690 700
IKLDDVVLVS QNGYALRFNI EEVPVVGAKA AGVKAMNLKE DDVLQSGFIC
710 720 730 740 750
NTSSFYLLTQ RGSLKRVSIE EILATSRAKR GLQVLRELKN KPHRVFLAGA
760 770 780 790 800
VAEQGFVGDF FSTEVDVNDQ TLLVQSNKGT IYESRLQDLN LSERTSNGSF
810 820
ISDTISDEEV FDAYLQEVVT EDK
Length:823
Mass (Da):93,133
Last modified:September 26, 2001 - v3
Checksum:iD4D17BD5DED63C05
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti95 – 951R → C in AAB08038. (PubMed:8913454)Curated
Sequence conflicti257 – 2571I → T(PubMed:8763932)Curated
Sequence conflicti257 – 2571I → T(PubMed:8891124)Curated
Sequence conflicti362 – 3621R → P in CAA65021. (PubMed:8891124)Curated
Sequence conflicti373 – 3731H → R in CAA65021. (PubMed:8891124)Curated
Sequence conflicti401 – 4011A → P in CAA65021. (PubMed:8891124)Curated
Sequence conflicti473 – 4731K → N in CAA65021. (PubMed:8891124)Curated
Sequence conflicti589 – 5891E → A in CAA65021. (PubMed:8891124)Curated
Sequence conflicti608 – 6081V → A in CAA65021. (PubMed:8891124)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z67739 Genomic DNA. Translation: CAA91551.2.
AE005672 Genomic DNA. Translation: AAK74984.1.
X95717 Genomic DNA. Translation: CAA65021.1.
U49088 Genomic DNA. Translation: AAB08038.1.
PIRiG95098.
RefSeqiNP_345344.1. NC_003028.3.
WP_010963255.1. NC_003028.3.

Genome annotation databases

EnsemblBacteriaiAAK74984; AAK74984; SP_0855.
GeneIDi930805.
KEGGispn:SP_0855.
PATRICi19706095. VBIStrPne105772_0894.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z67739 Genomic DNA. Translation: CAA91551.2 .
AE005672 Genomic DNA. Translation: AAK74984.1 .
X95717 Genomic DNA. Translation: CAA65021.1 .
U49088 Genomic DNA. Translation: AAB08038.1 .
PIRi G95098.
RefSeqi NP_345344.1. NC_003028.3.
WP_010963255.1. NC_003028.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2NOV X-ray 2.67 A/B/C/D 1-488 [» ]
3FOE X-ray 4.00 A/B 1-488 [» ]
3FOF X-ray 4.00 A/B 1-488 [» ]
3K9F X-ray 2.90 A/B 1-488 [» ]
3KSA X-ray 3.30 A/B 1-488 [» ]
3KSB X-ray 3.50 A/B 1-488 [» ]
3LTN X-ray 3.10 A/B 1-488 [» ]
3RAD X-ray 3.35 A/B 1-488 [» ]
3RAE X-ray 2.90 A/B 1-488 [» ]
3RAF X-ray 3.24 A/B 1-488 [» ]
4JUO X-ray 6.53 A 1-488 [» ]
ProteinModelPortali P72525.
SMRi P72525. Positions 29-482.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-48521N.
STRINGi 170187.SP_0855.

Chemistry

ChEMBLi CHEMBL2363033.
DrugBanki DB06771. Besifloxacin.
DB01044. Gatifloxacin.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAK74984 ; AAK74984 ; SP_0855 .
GeneIDi 930805.
KEGGi spn:SP_0855.
PATRICi 19706095. VBIStrPne105772_0894.

Phylogenomic databases

eggNOGi COG0188.
HOGENOMi HOG000076279.
KOi K02621.
OMAi HIVEGLM.
OrthoDBi EOG661H5V.

Enzyme and pathway databases

BioCyci SPNE170187:GHGN-857-MONOMER.

Miscellaneous databases

EvolutionaryTracei P72525.

Family and domain databases

Gene3Di 3.30.1360.40. 1 hit.
3.90.199.10. 2 hits.
HAMAPi MF_00937. ParC_type2.
InterProi IPR024946. 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 ]
Pfami PF03989. DNA_gyraseA_C. 5 hits.
PF00521. DNA_topoisoIV. 1 hit.
[Graphical view ]
SMARTi SM00434. TOP4c. 1 hit.
[Graphical view ]
SUPFAMi SSF56719. SSF56719. 1 hit.
TIGRFAMsi TIGR01061. parC_Gpos. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiPARC_STRPN
AccessioniPrimary (citable) accession number: P72525
Secondary accession number(s): P72537, Q54917
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: September 26, 2001
Last modified: November 26, 2014
This is version 113 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3