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P0AES4

- GYRA_ECOLI

UniProt

P0AES4 - GYRA_ECOLI

Protein

DNA gyrase subunit A

Gene

gyrA

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 90 (01 Oct 2014)
      Sequence version 1 (20 Dec 2005)
      Previous versions | rss
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    Functioni

    DNA gyrase negatively supercoils closed circular double-stranded DNA in an ATP-dependent manner and also catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes and knotted rings.3 PublicationsUniRule annotation

    Catalytic activityi

    ATP-dependent breakage, passage and rejoining of double-stranded DNA.4 PublicationsUniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei122 – 1221O-(5'-phospho-DNA)-tyrosine intermediate1 PublicationUniRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-HAMAP
    2. DNA binding Source: EcoliWiki
    3. DNA-dependent ATPase activity Source: EcoliWiki
    4. DNA topoisomerase type II (ATP-hydrolyzing) activity Source: CACAO
    5. identical protein binding Source: IntAct
    6. protein binding Source: IntAct

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. chromosome segregation Source: RefGenome
    3. DNA topological change Source: EcoliWiki
    4. DNA unwinding involved in DNA replication Source: RefGenome
    5. response to antibiotic Source: UniProtKB-KW
    6. response to drug Source: EcoliWiki
    7. transcription, DNA-templated Source: EcoliWiki

    Keywords - Molecular functioni

    Isomerase, Topoisomerase

    Keywords - Biological processi

    Antibiotic resistance

    Keywords - Ligandi

    ATP-binding, DNA-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10423-MONOMER.
    ECOL316407:JW2225-MONOMER.
    MetaCyc:EG10423-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA gyrase subunit AUniRule annotation (EC:5.99.1.3UniRule annotation)
    Gene namesi
    Name:gyrAUniRule annotation
    Synonyms:hisW, nalA, parD
    Ordered Locus Names:b2231, JW2225
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10423. gyrA.

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. chromosome Source: InterPro
    2. cytoplasm Source: UniProtKB
    3. DNA topoisomerase complex (ATP-hydrolyzing) Source: RefGenome
    4. membrane Source: UniProtKB
    5. nucleoid Source: RefGenome

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi32 – 321R → A or Q: Nearly abolishes DNA supercoiling. Reduces DNA cleavage and relaxation. 1 Publication
    Mutagenesisi47 – 471R → Q: Nearly abolishes DNA supercoiling. Reduces DNA cleavage. Slightly reduces DNA relaxation. 1 Publication
    Mutagenesisi78 – 781H → A: Nearly abolishes DNA supercoiling. Reduces DNA cleavage and DNA relaxation. 1 Publication
    Mutagenesisi80 – 801H → A: Reduces DNA supercoiling. Slightly reduces DNA cleavage. No effect on DNA relaxation. 1 Publication
    Mutagenesisi83 – 831S → A: Resistant to fluoroquinolones. 1 Publication
    Mutagenesisi106 – 1061Q → R: Resistant to fluoroquinolones. 1 Publication
    Mutagenesisi462 – 4621R → C in gyrA462; resistant to cytotoxic protein CcdB, but not to the quinoline antibiotic enoxacin, has no effect on DNA supercoiling. Does not interact with CcdB. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 875874DNA gyrase subunit APRO_0000145232Add
    BLAST

    Proteomic databases

    PaxDbiP0AES4.
    PRIDEiP0AES4.

    2D gel databases

    SWISS-2DPAGEP0AES4.

    Expressioni

    Gene expression databases

    GenevestigatoriP0AES4.

    Interactioni

    Subunit structurei

    Heterotetramer, composed of two GyrA and two GyrB chains. Within the heterotetramer, GyrA contains the active site tyrosine that forms a covalent intermediate with the DNA, while GyrB contributes the cofactor binding sites and catalyzes ATP hydrolysis. Can form a 2:2 complex with toxin CcdB in which GyrA is inactive; rejuvenation of GyrA2CcdB2 is effected by CcdA.5 PublicationsUniRule annotation

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-547129,EBI-547129
    gyrBP0AES65EBI-547129,EBI-541911
    marRP272452EBI-547129,EBI-6409744

    Protein-protein interaction databases

    DIPiDIP-36179N.
    IntActiP0AES4. 51 interactions.
    MINTiMINT-201682.
    STRINGi511145.b2231.

    Structurei

    Secondary structure

    1
    875
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni31 – 333
    Turni37 – 393
    Helixi43 – 5412
    Beta strandi59 – 613
    Helixi66 – 7611
    Helixi82 – 9110
    Turni95 – 973
    Beta strandi102 – 1076
    Turni120 – 1223
    Beta strandi124 – 1274
    Helixi131 – 1344
    Turni136 – 1416
    Beta strandi145 – 1473
    Beta strandi151 – 1588
    Helixi165 – 1695
    Beta strandi171 – 1733
    Beta strandi180 – 1823
    Helixi187 – 19913
    Helixi205 – 2084
    Turni209 – 2113
    Helixi227 – 2359
    Beta strandi236 – 2438
    Beta strandi245 – 2495
    Beta strandi258 – 2636
    Helixi270 – 28112
    Turni282 – 2843
    Beta strandi292 – 2943
    Beta strandi298 – 3003
    Beta strandi303 – 3053
    Helixi314 – 32310
    Beta strandi327 – 3337
    Beta strandi335 – 3384
    Beta strandi341 – 3444
    Helixi347 – 38842
    Helixi390 – 39910
    Beta strandi400 – 4023
    Helixi403 – 41210
    Helixi419 – 4213
    Beta strandi441 – 4499
    Helixi452 – 4598
    Helixi463 – 4664
    Helixi468 – 49326
    Helixi495 – 51319
    Beta strandi519 – 5213
    Beta strandi538 – 5447
    Beta strandi547 – 5537
    Beta strandi578 – 5858
    Beta strandi589 – 5946
    Beta strandi597 – 6037
    Helixi604 – 6063
    Beta strandi612 – 6143
    Helixi619 – 6213
    Beta strandi631 – 6388
    Beta strandi645 – 6506
    Beta strandi653 – 6597
    Helixi660 – 6634
    Beta strandi671 – 6744
    Beta strandi682 – 6887
    Beta strandi693 – 6986
    Beta strandi701 – 7077
    Helixi708 – 7103
    Beta strandi732 – 7365
    Beta strandi743 – 7486
    Beta strandi751 – 7566
    Helixi758 – 7603
    Beta strandi771 – 7744
    Turni778 – 7803
    Beta strandi782 – 7898
    Beta strandi794 – 8018
    Beta strandi804 – 8085
    Helixi809 – 8113
    Beta strandi833 – 8386

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AB4X-ray2.80A30-522[»]
    1X75X-ray2.80A/B363-494[»]
    1ZI0X-ray2.60A/B535-841[»]
    2Y3PX-ray2.62A/B2-523[»]
    3NUHX-ray3.10A1-525[»]
    4ELYX-ray1.93A/B363-497[»]
    ProteinModelPortaliP0AES4.
    SMRiP0AES4. Positions 13-522, 535-841.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0AES4.

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0188.
    HOGENOMiHOG000076278.
    KOiK02469.
    OMAiQTVFGIN.
    OrthoDBiEOG661H5V.
    PhylomeDBiP0AES4.

    Family and domain databases

    Gene3Di1.10.268.10. 1 hit.
    3.30.1360.40. 1 hit.
    3.90.199.10. 1 hit.
    HAMAPiMF_01897. GyrA.
    InterProiIPR024946. Arg_repress_C-like.
    IPR005743. GyrA.
    IPR006691. GyrA/parC_pinwhl.
    IPR002205. Topo_IIA_A/C.
    IPR013758. Topo_IIA_A/C_ab.
    IPR013757. Topo_IIA_A_a.
    IPR013760. Topo_IIA_like_dom.
    [Graphical view]
    PfamiPF03989. DNA_gyraseA_C. 6 hits.
    PF00521. DNA_topoisoIV. 1 hit.
    [Graphical view]
    SMARTiSM00434. TOP4c. 1 hit.
    [Graphical view]
    SUPFAMiSSF56719. SSF56719. 1 hit.
    TIGRFAMsiTIGR01063. gyrA. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P0AES4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSDLAREITP VNIEEELKSS YLDYAMSVIV GRALPDVRDG LKPVHRRVLY    50
    AMNVLGNDWN KAYKKSARVV GDVIGKYHPH GDSAVYDTIV RMAQPFSLRY 100
    MLVDGQGNFG SIDGDSAAAM RYTEIRLAKI AHELMADLEK ETVDFVDNYD 150
    GTEKIPDVMP TKIPNLLVNG SSGIAVGMAT NIPPHNLTEV INGCLAYIDD 200
    EDISIEGLME HIPGPDFPTA AIINGRRGIE EAYRTGRGKV YIRARAEVEV 250
    DAKTGRETII VHEIPYQVNK ARLIEKIAEL VKEKRVEGIS ALRDESDKDG 300
    MRIVIEVKRD AVGEVVLNNL YSQTQLQVSF GINMVALHHG QPKIMNLKDI 350
    IAAFVRHRRE VVTRRTIFEL RKARDRAHIL EALAVALANI DPIIELIRHA 400
    PTPAEAKTAL VANPWQLGNV AAMLERAGDD AARPEWLEPE FGVRDGLYYL 450
    TEQQAQAILD LRLQKLTGLE HEKLLDEYKE LLDQIAELLR ILGSADRLME 500
    VIREELELVR EQFGDKRRTE ITANSADINL EDLITQEDVV VTLSHQGYVK 550
    YQPLSEYEAQ RRGGKGKSAA RIKEEDFIDR LLVANTHDHI LCFSSRGRVY 600
    SMKVYQLPEA TRGARGRPIV NLLPLEQDER ITAILPVTEF EEGVKVFMAT 650
    ANGTVKKTVL TEFNRLRTAG KVAIKLVDGD ELIGVDLTSG EDEVMLFSAE 700
    GKVVRFKESS VRAMGCNTTG VRGIRLGEGD KVVSLIVPRG DGAILTATQN 750
    GYGKRTAVAE YPTKSRATKG VISIKVTERN GLVVGAVQVD DCDQIMMITD 800
    AGTLVRTRVS EISIVGRNTQ GVILIRTAED ENVVGLQRVA EPVDEEDLDT 850
    IDGSAAEGDD EIAPEVDVDD EPEEE 875
    Length:875
    Mass (Da):96,964
    Last modified:December 20, 2005 - v1
    Checksum:i3FD5BD52A5969069
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti67 – 671A → S in PPA-10; quinolone-resistant.
    Natural varianti81 – 811G → C in NAL-97; quinolone-resistant.
    Natural varianti83 – 831S → L in NAL-51, NAL-112, NAL-118 and NAL-119; quinolone-resistant.
    Natural varianti83 – 831S → W in PPA-18 and strain 227; quinolone-resistant.
    Natural varianti84 – 841A → P in PPA-05; quinolone-resistant.
    Natural varianti87 – 871D → N in NAL-113 and KL-16; quinolone-resistant.
    Natural varianti87 – 871D → V in strain: 202; quinolone-resistant.
    Natural varianti106 – 1061Q → H in NAL-89; quinolone-resistant.
    Natural varianti678 – 6781D → E in strain: 227.
    Natural varianti798 – 7981I → IMMI in KL-16; quinolone-resistant.
    Natural varianti828 – 8281A → S in strain: 227.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X06373 Genomic DNA. Translation: CAA29676.1.
    X06744 Genomic DNA. Translation: CAA29919.1.
    M15631 Genomic DNA. Translation: AAA23948.1.
    U00096 Genomic DNA. Translation: AAC75291.1.
    AP009048 Genomic DNA. Translation: BAA16048.1.
    Y00544 Genomic DNA. Translation: CAA68611.1.
    PIRiS02340. ITECAP.
    RefSeqiNP_416734.1. NC_000913.3.
    YP_490470.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75291; AAC75291; b2231.
    BAA16048; BAA16048; BAA16048.
    GeneIDi12933138.
    946614.
    KEGGiecj:Y75_p2193.
    eco:b2231.
    PATRICi32119821. VBIEscCol129921_2320.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X06373 Genomic DNA. Translation: CAA29676.1 .
    X06744 Genomic DNA. Translation: CAA29919.1 .
    M15631 Genomic DNA. Translation: AAA23948.1 .
    U00096 Genomic DNA. Translation: AAC75291.1 .
    AP009048 Genomic DNA. Translation: BAA16048.1 .
    Y00544 Genomic DNA. Translation: CAA68611.1 .
    PIRi S02340. ITECAP.
    RefSeqi NP_416734.1. NC_000913.3.
    YP_490470.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AB4 X-ray 2.80 A 30-522 [» ]
    1X75 X-ray 2.80 A/B 363-494 [» ]
    1ZI0 X-ray 2.60 A/B 535-841 [» ]
    2Y3P X-ray 2.62 A/B 2-523 [» ]
    3NUH X-ray 3.10 A 1-525 [» ]
    4ELY X-ray 1.93 A/B 363-497 [» ]
    ProteinModelPortali P0AES4.
    SMRi P0AES4. Positions 13-522, 535-841.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-36179N.
    IntActi P0AES4. 51 interactions.
    MINTi MINT-201682.
    STRINGi 511145.b2231.

    Chemistry

    BindingDBi P0AES4.
    ChEMBLi CHEMBL1858.

    2D gel databases

    SWISS-2DPAGE P0AES4.

    Proteomic databases

    PaxDbi P0AES4.
    PRIDEi P0AES4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC75291 ; AAC75291 ; b2231 .
    BAA16048 ; BAA16048 ; BAA16048 .
    GeneIDi 12933138.
    946614.
    KEGGi ecj:Y75_p2193.
    eco:b2231.
    PATRICi 32119821. VBIEscCol129921_2320.

    Organism-specific databases

    EchoBASEi EB0418.
    EcoGenei EG10423. gyrA.

    Phylogenomic databases

    eggNOGi COG0188.
    HOGENOMi HOG000076278.
    KOi K02469.
    OMAi QTVFGIN.
    OrthoDBi EOG661H5V.
    PhylomeDBi P0AES4.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10423-MONOMER.
    ECOL316407:JW2225-MONOMER.
    MetaCyc:EG10423-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0AES4.
    PROi P0AES4.

    Gene expression databases

    Genevestigatori P0AES4.

    Family and domain databases

    Gene3Di 1.10.268.10. 1 hit.
    3.30.1360.40. 1 hit.
    3.90.199.10. 1 hit.
    HAMAPi MF_01897. GyrA.
    InterProi IPR024946. Arg_repress_C-like.
    IPR005743. GyrA.
    IPR006691. GyrA/parC_pinwhl.
    IPR002205. Topo_IIA_A/C.
    IPR013758. Topo_IIA_A/C_ab.
    IPR013757. Topo_IIA_A_a.
    IPR013760. Topo_IIA_like_dom.
    [Graphical view ]
    Pfami PF03989. DNA_gyraseA_C. 6 hits.
    PF00521. DNA_topoisoIV. 1 hit.
    [Graphical view ]
    SMARTi SM00434. TOP4c. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56719. SSF56719. 1 hit.
    TIGRFAMsi TIGR01063. gyrA. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and sequencing of the Escherichia coli gyrA gene coding for the A subunit of DNA gyrase."
      Swanberg S.L., Wang J.C.
      J. Mol. Biol. 197:729-736(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Quinolone-resistant mutations of the gyrA gene of Escherichia coli."
      Yoshida H., Kojima T., Yamagishi J., Nakamura S.
      Mol. Gen. Genet. 211:1-7(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12 / KL16.
    3. "The parD- mutant of Escherichia coli also carries a gyrAam mutation. The complete sequence of gyrA."
      Hussain K., Elliott E.J., Salmond G.P.C.
      Mol. Microbiol. 1:259-273(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: OV6.
    4. "Cloning and characterization of a DNA gyrase A gene from Escherichia coli that confers clinical resistance to 4-quinolones."
      Cullen M.E., Wyke A.W., Kuroda R., Fisher L.M.
      Antimicrob. Agents Chemother. 33:886-894(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 227.
    5. "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
      Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T.
      , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
      DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    7. "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.
    8. "Fusions of the Escherichia coli gyrA and gyrB control regions to the galactokinase gene are inducible by coumermycin treatment."
      Menzel R., Gellert M.
      J. Bacteriol. 169:1272-1278(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-88, PARTIAL PROTEIN SEQUENCE.
    9. "Mapping the active site tyrosine of Escherichia coli DNA gyrase."
      Horowitz D.S., Wang J.C.
      J. Biol. Chem. 262:5339-5344(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACTIVE SITE TYR-122.
    10. "Escherichia coli proteome analysis using the gene-protein database."
      VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
      Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY 2D-GEL.
    11. "Identification of four GyrA residues involved in the DNA breakage-reunion reaction of DNA gyrase."
      Hockings S.C., Maxwell A.
      J. Mol. Biol. 318:351-359(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, MUTAGENESIS OF ARG-32; ARG-47; HIS-78 AND HIS-80.
    12. "DNA gyrase requires DNA for effective two-site coordination of divalent metal ions: further insight into the mechanism of enzyme action."
      Sissi C., Chemello A., Vazquez E., Mitchenall L.A., Maxwell A., Palumbo M.
      Biochemistry 47:8538-8545(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, FUNCTION, COFACTOR, SUBUNIT.
    13. "A superhelical spiral in the Escherichia coli DNA gyrase A C-terminal domain imparts unidirectional supercoiling bias."
      Ruthenburg A.J., Graybosch D.M., Huetsch J.C., Verdine G.L.
      J. Biol. Chem. 280:26177-26184(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 535-841.
    14. "A crystal structure of the bifunctional antibiotic simocyclinone D8, bound to DNA gyrase."
      Edwards M.J., Flatman R.H., Mitchenall L.A., Stevenson C.E., Le T.B., Clarke T.A., McKay A.R., Fiedler H.P., Buttner M.J., Lawson D.M., Maxwell A.
      Science 326:1415-1418(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.62 ANGSTROMS) OF 2-523 IN COMPLEX WITH ANTIBIOTIC SIMOCYCLINONE D8, CATALYTIC ACTIVITY, SUBUNIT, FUNCTION.
    15. "Quinolone resistance-determining region in the DNA gyrase gyrA gene of Escherichia coli."
      Yoshida H., Bogaki M., Nakamura M., Nakamura S.
      Antimicrob. Agents Chemother. 34:1271-1272(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS QUINOLONE-RESISTANT.
    16. "4-quinolone resistance mutations in the DNA gyrase of Escherichia coli clinical isolates identified by using the polymerase chain reaction."
      Oram M., Fisher L.M.
      Antimicrob. Agents Chemother. 35:387-389(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS QUINOLONE-RESISTANT.
    17. "Novel quinolone resistance mutations of the Escherichia coli DNA gyrase A protein: enzymatic analysis of the mutant proteins."
      Hallett P., Maxwell A.
      Antimicrob. Agents Chemother. 35:335-340(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF SER-83 AND GLN-106.
      Strain: K12.
    18. "Cell killing by the F plasmid CcdB protein involves poisoning of DNA-topoisomerase II complexes."
      Bernard P., Couturier M.
      J. Mol. Biol. 226:735-745(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: INHIBITION BY TOXIN PROTEIN CCDB, MUTAGENESIS OF ARG-462.
      Strain: K12.
    19. "The F plasmid CcdB protein induces efficient ATP-dependent DNA cleavage by gyrase."
      Bernard P., Kezdy K.E., Van Melderen L., Steyaert J., Wyns L., Pato M.L., Higgins P.N., Couturier M.
      J. Mol. Biol. 234:534-541(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ARG-462.
    20. "Partner switching mechanisms in inactivation and rejuvenation of Escherichia coli DNA gyrase by F plasmid proteins LetD (CcdB) and LetA (CcdA)."
      Maki S., Takiguchi S., Horiuchi T., Sekimizu K., Miki T.
      J. Mol. Biol. 256:473-482(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INHIBITION BY TOXIN PROTEIN CCDB, REJUVENATION BY CCDA, SUBUNIT.
    21. "Crystal structure of the breakage-reunion domain of DNA gyrase."
      Cabral J.H., Jackson A.P., Smith C.V., Shikotra N., Maxwell A., Liddington R.C.
      Nature 388:903-906(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 30-522, CATALYTIC ACTIVITY.
    22. "Molecular basis of gyrase poisoning by the addiction toxin CcdB."
      Dao-Thi M.H., Van Melderen L., De Genst E., Afif H., Buts L., Wyns L., Loris R.
      J. Mol. Biol. 348:1091-1102(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 363-494 IN COMPLEX WITH CCBD.

    Entry informationi

    Entry nameiGYRA_ECOLI
    AccessioniPrimary (citable) accession number: P0AES4
    Secondary accession number(s): P09097
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 20, 2005
    Last sequence update: December 20, 2005
    Last modified: October 1, 2014
    This is version 90 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    When the enzyme transiently cleaves DNA a phosphotyrosine bond is formed between GyrA and DNA. This enzyme-DNA intermediate is the target of a number of topoisomerase poisons, including toxin CcdB.

    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