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P0AFI2

- PARC_ECOLI

UniProt

P0AFI2 - PARC_ECOLI

Protein

DNA topoisomerase 4 subunit A

Gene

parC

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 1 (20 Dec 2005)
      Previous versions | rss
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    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. MukB stimulates the relaxation activity of topoisomerase IV and also has a modest effect on decatenation.4 PublicationsUniRule annotation

    Catalytic activityi

    ATP-dependent breakage, passage and rejoining of double-stranded DNA.3 PublicationsUniRule annotation

    Enzyme regulationi

    Inhibited by quinolones.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei39 – 391Interaction with DNAUniRule annotation
    Sitei75 – 751Interaction with DNAUniRule annotation
    Sitei77 – 771Interaction with DNAUniRule annotation
    Sitei119 – 1191Transition state stabilizerUniRule annotation
    Active sitei120 – 1201O-(5'-phospho-DNA)-tyrosine intermediateUniRule annotation

    GO - Molecular functioni

    1. ATP binding Source: InterPro
    2. DNA binding Source: EcoliWiki
    3. DNA topoisomerase type II (ATP-hydrolyzing) activity Source: UniProtKB-HAMAP
    4. protein binding Source: IntAct

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. chromosome segregation Source: EcoliWiki
    3. DNA topological change Source: EcoliWiki
    4. DNA unwinding involved in DNA replication Source: RefGenome
    5. plasmid partitioning Source: EcoliWiki
    6. sister chromatid cohesion Source: EcoliWiki

    Keywords - Molecular functioni

    Isomerase, Topoisomerase

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10686-MONOMER.
    ECOL316407:JW2987-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:b3019, JW2987
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10686. parC.

    Subcellular locationi

    GO - Cellular componenti

    1. chromosome Source: InterPro
    2. cytoplasm Source: EcoliWiki
    3. DNA topoisomerase complex (ATP-hydrolyzing) Source: EcoliWiki
    4. extrinsic component of plasma membrane Source: EcoliWiki
    5. nucleoid Source: RefGenome

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi80 – 801S → L: Confers resistance to quinolones. No effect on catalytic activity. 1 Publication
    Mutagenesisi84 – 841E → K: Strongly reduced enzyme activity. Increases stability of covalent reaction intermediate with DNA. Confers resistance to quinolones. 1 Publication
    Mutagenesisi84 – 841E → P: Confers resistance to quinolones. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 752752DNA topoisomerase 4 subunit APRO_0000145397Add
    BLAST

    Proteomic databases

    PaxDbiP0AFI2.
    PRIDEiP0AFI2.

    Expressioni

    Gene expression databases

    GenevestigatoriP0AFI2.

    Interactioni

    Subunit structurei

    Heterotetramer composed of ParC and ParE. Interacts with MukB.4 PublicationsUniRule annotation

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    mukBP225237EBI-878544,EBI-542943

    Protein-protein interaction databases

    DIPiDIP-36030N.
    IntActiP0AFI2. 23 interactions.
    MINTiMINT-1227290.
    STRINGi511145.b3019.

    Structurei

    Secondary structure

    1
    752
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni34 – 363
    Helixi40 – 4910
    Helixi67 – 715
    Turni72 – 743
    Helixi80 – 8910
    Beta strandi99 – 1024
    Beta strandi107 – 1115
    Helixi120 – 1223
    Beta strandi123 – 1253
    Helixi127 – 1293
    Helixi130 – 1334
    Turni134 – 1374
    Beta strandi143 – 1453
    Beta strandi149 – 1568
    Helixi163 – 1675
    Helixi185 – 19713
    Helixi203 – 2064
    Turni207 – 2093
    Beta strandi216 – 2216
    Helixi227 – 2348
    Beta strandi236 – 2427
    Beta strandi244 – 2485
    Beta strandi251 – 2566
    Helixi263 – 27513
    Beta strandi282 – 2876
    Beta strandi291 – 2933
    Beta strandi297 – 3059
    Helixi308 – 31811
    Beta strandi322 – 3287
    Beta strandi330 – 3323
    Beta strandi338 – 3403
    Helixi343 – 38442
    Helixi386 – 39510
    Beta strandi396 – 3983
    Helixi399 – 4057
    Helixi413 – 4186
    Helixi422 – 4254
    Helixi427 – 45226
    Helixi454 – 47219
    Beta strandi499 – 5057
    Beta strandi508 – 5169
    Beta strandi520 – 5234
    Beta strandi531 – 5388
    Beta strandi539 – 5413
    Beta strandi543 – 5475
    Beta strandi550 – 5556
    Helixi557 – 5593
    Beta strandi563 – 5653
    Helixi570 – 5723
    Beta strandi582 – 5865
    Beta strandi593 – 5986
    Beta strandi601 – 6077
    Helixi608 – 6114
    Beta strandi642 – 6476
    Beta strandi650 – 6567
    Helixi657 – 6593
    Beta strandi664 – 6674
    Beta strandi669 – 6724
    Helixi676 – 6805
    Beta strandi686 – 6927
    Beta strandi697 – 7026
    Beta strandi705 – 7095
    Helixi711 – 7155
    Beta strandi736 – 7405

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ZVTX-ray1.70A/B497-752[»]
    1ZVUX-ray3.00A27-742[»]
    4MN4X-ray2.30A/B497-752[»]
    ProteinModelPortaliP0AFI2.
    SMRiP0AFI2. Positions 28-742.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0AFI2.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni497 – 752256Sufficient for MukB bindingAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0188.
    HOGENOMiHOG000076277.
    KOiK02621.
    OMAiILSEMGW.
    OrthoDBiEOG661H5V.
    PhylomeDBiP0AFI2.

    Family and domain databases

    Gene3Di3.30.1360.40. 1 hit.
    3.90.199.10. 2 hits.
    HAMAPiMF_00936. ParC_type1.
    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.
    IPR005742. TopoIV_A_Gneg.
    [Graphical view]
    PfamiPF03989. DNA_gyraseA_C. 2 hits.
    PF00521. DNA_topoisoIV. 1 hit.
    [Graphical view]
    SMARTiSM00434. TOP4c. 1 hit.
    [Graphical view]
    SUPFAMiSSF56719. SSF56719. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P0AFI2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSDMAERLAL HEFTENAYLN YSMYVIMDRA LPFIGDGLKP VQRRIVYAMS    50
    ELGLNASAKF KKSARTVGDV LGKYHPHGDS ACYEAMVLMA QPFSYRYPLV 100
    DGQGNWGAPD DPKSFAAMRY TESRLSKYSE LLLSELGQGT ADWVPNFDGT 150
    LQEPKMLPAR LPNILLNGTT GIAVGMATDI PPHNLREVAQ AAIALIDQPK 200
    TTLDQLLDIV QGPDYPTEAE IITSRAEIRK IYENGRGSVR MRAVWKKEDG 250
    AVVISALPHQ VSGARVLEQI AAQMRNKKLP MVDDLRDESD HENPTRLVIV 300
    PRSNRVDMDQ VMNHLFATTD LEKSYRINLN MIGLDGRPAV KNLLEILSEW 350
    LVFRRDTVRR RLNYRLEKVL KRLHILEGLL VAFLNIDEVI EIIRNEDEPK 400
    PALMSRFGLT ETQAEAILEL KLRHLAKLEE MKIRGEQSEL EKERDQLQGI 450
    LASERKMNNL LKKELQADAQ AYGDDRRSPL QEREEAKAMS EHDMLPSEPV 500
    TIVLSQMGWV RSAKGHDIDA PGLNYKAGDS FKAAVKGKSN QPVVFVDSTG 550
    RSYAIDPITL PSARGQGEPL TGKLTLPPGA TVDHMLMESD DQKLLMASDA 600
    GYGFVCTFND LVARNRAGKA LITLPENAHV MPPVVIEDAS DMLLAITQAG 650
    RMLMFPVSDL PQLSKGKGNK IINIPSAEAA RGEDGLAQLY VLPPQSTLTI 700
    HVGKRKIKLR PEELQKVTGE RGRRGTLMRG LQRIDRVEID SPRRASSGDS 750
    EE 752
    Length:752
    Mass (Da):83,831
    Last modified:December 20, 2005 - v1
    Checksum:i0D4907E96CEE7086
    GO

    Sequence cautioni

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

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    PIRiA65089.
    RefSeqiNP_417491.1. NC_000913.3.
    YP_491211.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76055; AAC76055; b3019.
    BAE77075; BAE77075; BAE77075.
    GeneIDi12933371.
    947499.
    KEGGiecj:Y75_p2945.
    eco:b3019.
    PATRICi32121452. VBIEscCol129921_3113.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    PIRi A65089.
    RefSeqi NP_417491.1. NC_000913.3.
    YP_491211.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ZVT X-ray 1.70 A/B 497-752 [» ]
    1ZVU X-ray 3.00 A 27-742 [» ]
    4MN4 X-ray 2.30 A/B 497-752 [» ]
    ProteinModelPortali P0AFI2.
    SMRi P0AFI2. Positions 28-742.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-36030N.
    IntActi P0AFI2. 23 interactions.
    MINTi MINT-1227290.
    STRINGi 511145.b3019.

    Chemistry

    BindingDBi P0AFI2.
    ChEMBLi CHEMBL2363076.
    DrugBanki DB00817. Rosoxacin.

    Proteomic databases

    PaxDbi P0AFI2.
    PRIDEi P0AFI2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76055 ; AAC76055 ; b3019 .
    BAE77075 ; BAE77075 ; BAE77075 .
    GeneIDi 12933371.
    947499.
    KEGGi ecj:Y75_p2945.
    eco:b3019.
    PATRICi 32121452. VBIEscCol129921_3113.

    Organism-specific databases

    EchoBASEi EB0680.
    EcoGenei EG10686. parC.

    Phylogenomic databases

    eggNOGi COG0188.
    HOGENOMi HOG000076277.
    KOi K02621.
    OMAi ILSEMGW.
    OrthoDBi EOG661H5V.
    PhylomeDBi P0AFI2.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10686-MONOMER.
    ECOL316407:JW2987-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0AFI2.
    PROi P0AFI2.

    Gene expression databases

    Genevestigatori P0AFI2.

    Family and domain databases

    Gene3Di 3.30.1360.40. 1 hit.
    3.90.199.10. 2 hits.
    HAMAPi MF_00936. ParC_type1.
    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.
    IPR005742. TopoIV_A_Gneg.
    [Graphical view ]
    Pfami PF03989. DNA_gyraseA_C. 2 hits.
    PF00521. DNA_topoisoIV. 1 hit.
    [Graphical view ]
    SMARTi SM00434. TOP4c. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56719. SSF56719. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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. 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.

    Entry informationi

    Entry nameiPARC_ECOLI
    AccessioniPrimary (citable) accession number: P0AFI2
    Secondary accession number(s): O69154, P20082, Q2M9I1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 20, 2005
    Last sequence update: December 20, 2005
    Last modified: October 1, 2014
    This is version 87 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3