Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P72525

- PARC_STRPN

UniProt

P72525 - PARC_STRPN

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 3 (26 Sep 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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

    Keywords - Cellular componenti

    Cell membrane, Membrane

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    MSNIQNMSLE DIMGERFGRY SKYIIQDRAL PDIRDGLKPV QRRILYSMNK    50
    DSNTFDKSYR KSAKSVGNIM GNFHPHGDSS IYDAMVRMSQ NWKNREILVE 100
    MHGNNGSMDG DPPAAMRYTE ARLSEIAGYL LQDIEKKTVP FAWNFDDTEK 150
    EPTVLPAAFP NLLVNGSTGI SAGYATDIPP HNLAEVIDAA VYMIDHPTAK 200
    IDKLMEFLPG PDFPTGAIIQ GRDEIKKAYE TGKGRVVVRS KTEIEKLKGG 250
    KEQIVIIEIP YEINKANLVK KIDDVRVNNK VAGIAEVRDE SDRDGLRIAI 300
    ELKKDANTEL VLNYLFKYTD LQINYNFNMV AIDNFTPRQV GIVPILSSYI 350
    AHRREVILAR SRFDKEKAEK RLHIVEGLIR VISILDEVIA LIRASENKAD 400
    AKENLKVSYD FTEEQAEAIV TLQLYRLTNT DVVVLQEEEA ELREKIAMLA 450
    AIIGDERTMY NLMKKELREV KKKFATPRLS SLEDTAKAIE IDTASLIAEE 500
    DTYVSVTKAG YIKRTSPRSF AASTLEEIGK RDDDRLIFVQ SAKTTQHLLM 550
    FTSLGNVIYR PIHELADIRW KDIGEHLSQT ITNFETNEEI LYVEVLDQFD 600
    DATTYFAVTR LGQIKRVERK EFTPWRTYRS KSVKYAKLKD DTDQIVAVAP 650
    IKLDDVVLVS QNGYALRFNI EEVPVVGAKA AGVKAMNLKE DDVLQSGFIC 700
    NTSSFYLLTQ RGSLKRVSIE EILATSRAKR GLQVLRELKN KPHRVFLAGA 750
    VAEQGFVGDF FSTEVDVNDQ TLLVQSNKGT IYESRLQDLN LSERTSNGSF 800
    ISDTISDEEV FDAYLQEVVT EDK 823
    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:
    EMBL
    GenBank
    DDBJ
    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.

    Genome annotation databases

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

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.

    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

    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: October 1, 2014
    This is version 111 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