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P0AES6

- GYRB_ECOLI

UniProt

P0AES6 - GYRB_ECOLI

Protein

DNA gyrase subunit B

Gene

gyrB

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 93 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      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

    Cofactori

    Magnesium. Binds two Mg2+ per subunit. The magnesium ions form salt bridges with both the protein and the DNA. Can also accept other divalent metal cations, such as Mn2+ and Ca2+.2 PublicationsUniRule annotation

    Enzyme regulationi

    Target of two classes of inhibitors, coumarins and quinolones. Coumarins bind to GyrB and are competitive inhibitors with respect to ATP. Quinolones bind DNA gyrase when the enzyme is complexed with DNA and trap the enzyme in a covalent reaction intermediate with DNA.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi424 – 4241Magnesium 1; catalyticUniRule annotation
    Sitei449 – 4491Interaction with DNAUniRule annotation
    Sitei452 – 4521Interaction with DNAUniRule annotation
    Metal bindingi498 – 4981Magnesium 1; catalyticUniRule annotation
    Metal bindingi498 – 4981Magnesium 2UniRule annotation
    Metal bindingi500 – 5001Magnesium 2UniRule annotation

    GO - Molecular functioni

    1. ATP binding Source: EcoliWiki
    2. DNA binding Source: EcoliWiki
    3. DNA-dependent ATPase activity Source: EcoliWiki
    4. DNA topoisomerase type II (ATP-hydrolyzing) activity Source: EcoliWiki
    5. magnesium ion binding Source: UniProtKB-HAMAP
    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, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10424-MONOMER.
    ECOL316407:JW5625-MONOMER.
    MetaCyc:EG10424-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA gyrase subunit BUniRule annotation (EC:5.99.1.3UniRule annotation)
    Gene namesi
    Name:gyrBUniRule annotation
    Synonyms:acrB, himB, hisU, nalC, parA, pcbA
    Ordered Locus Names:b3699, JW5625
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10424. gyrB.

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi424 – 4241E → A or Q: Strongly reduced activity regarding both DNA supercoiling and relaxation. Reduces ATP hydrolysis in response to DNA binding, but has only minor effect on the basal rate of ATP hydrolysis. 1 Publication
    Mutagenesisi498 – 4981D → A or N: Strongly reduced activity regarding both DNA supercoiling and relaxation. Reduces ATP hydrolysis in response to DNA binding, but has only minor effect on the basal rate of ATP hydrolysis. 1 Publication
    Mutagenesisi500 – 5001D → A: Strongly reduced activity regarding both DNA supercoiling and relaxation. Reduces ATP hydrolysis in response to DNA binding, but has only minor effect on the basal rate of ATP hydrolysis. 1 Publication
    Mutagenesisi502 – 5021D → A: Strongly reduced activity regarding both DNA supercoiling and relaxation. Reduces ATP hydrolysis in response to DNA binding, but has only minor effect on the basal rate of ATP hydrolysis. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 804803DNA gyrase subunit BPRO_0000145309Add
    BLAST

    Proteomic databases

    PaxDbiP0AES6.
    PRIDEiP0AES6.

    Expressioni

    Gene expression databases

    GenevestigatoriP0AES6.

    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.3 PublicationsUniRule annotation

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    gyrAP0AES45EBI-541911,EBI-547129

    Protein-protein interaction databases

    DIPiDIP-48005N.
    IntActiP0AES6. 18 interactions.
    STRINGi511145.b3699.

    Structurei

    Secondary structure

    1
    804
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi7 – 93
    Helixi16 – 216
    Helixi24 – 274
    Beta strandi30 – 334
    Helixi34 – 5320
    Beta strandi58 – 636
    Turni65 – 673
    Beta strandi69 – 735
    Beta strandi81 – 833
    Turni84 – 874
    Helixi90 – 967
    Turni98 – 1014
    Beta strandi104 – 1085
    Beta strandi113 – 1153
    Helixi120 – 1256
    Beta strandi127 – 13610
    Beta strandi139 – 1468
    Beta strandi149 – 1535
    Beta strandi155 – 1595
    Beta strandi164 – 1718
    Turni173 – 1753
    Helixi184 – 19714
    Turni198 – 2003
    Beta strandi201 – 2077
    Turni208 – 2103
    Beta strandi213 – 2164
    Helixi221 – 23111
    Beta strandi235 – 2384
    Beta strandi241 – 2477
    Beta strandi250 – 26112
    Beta strandi264 – 2707
    Helixi280 – 29920
    Helixi302 – 3065
    Helixi312 – 3154
    Turni316 – 3183
    Beta strandi319 – 3268
    Beta strandi332 – 3343
    Helixi343 – 36321
    Helixi365 – 38925
    Beta strandi419 – 4246
    Helixi425 – 43511
    Turni438 – 4403
    Beta strandi441 – 4466
    Helixi465 – 47410
    Beta strandi491 – 4955
    Turni501 – 5044
    Helixi505 – 51713
    Helixi519 – 5235
    Beta strandi527 – 5304
    Beta strandi534 – 5396
    Beta strandi542 – 5465
    Helixi549 – 56113
    Beta strandi564 – 5718
    Beta strandi573 – 5764
    Helixi577 – 59620
    Turni597 – 6004
    Helixi603 – 6119
    Helixi617 – 6215
    Helixi623 – 64018
    Beta strandi646 – 6538
    Beta strandi660 – 6678
    Beta strandi669 – 6768
    Helixi679 – 6835
    Helixi685 – 69915
    Turni700 – 7034
    Beta strandi704 – 7118
    Beta strandi713 – 7186
    Helixi719 – 73012
    Turni731 – 7333
    Beta strandi735 – 7384
    Helixi742 – 7443
    Helixi747 – 7548
    Turni757 – 7593
    Beta strandi762 – 7643
    Helixi767 – 78014

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AJ6X-ray2.30A2-220[»]
    1EI1X-ray2.30A/B6-392[»]
    1KZNX-ray2.30A15-219[»]
    3G7EX-ray2.20A15-217[»]
    3NUHX-ray3.10B389-804[»]
    4DUHX-ray1.50A/B1-220[»]
    4HYPX-ray2.60A/B/C/D15-220[»]
    4KFGX-ray1.60A/B15-220[»]
    ProteinModelPortaliP0AES6.
    SMRiP0AES6. Positions 10-392, 402-784.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0AES6.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini418 – 533116ToprimUniRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the type II topoisomerase family.UniRule annotation
    Contains 1 Toprim domain.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0187.
    HOGENOMiHOG000075155.
    KOiK02470.
    OMAiHIIIMTD.
    OrthoDBiEOG6P334W.
    PhylomeDBiP0AES6.

    Family and domain databases

    Gene3Di3.30.230.10. 1 hit.
    3.30.565.10. 1 hit.
    3.40.50.670. 2 hits.
    HAMAPiMF_01898. GyrB.
    InterProiIPR002288. DNA_gyrase_B_C.
    IPR011557. GyrB.
    IPR003594. HATPase_ATP-bd.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
    IPR001241. Topo_IIA.
    IPR013506. Topo_IIA_bsu_dom2.
    IPR013759. Topo_IIA_cen_dom.
    IPR013760. Topo_IIA_like_dom.
    IPR018522. TopoIIA_CS.
    IPR006171. Toprim_domain.
    [Graphical view]
    PfamiPF00204. DNA_gyraseB. 1 hit.
    PF00986. DNA_gyraseB_C. 1 hit.
    PF02518. HATPase_c. 1 hit.
    PF01751. Toprim. 1 hit.
    [Graphical view]
    PRINTSiPR00418. TPI2FAMILY.
    SMARTiSM00387. HATPase_c. 1 hit.
    SM00433. TOP2c. 1 hit.
    [Graphical view]
    SUPFAMiSSF54211. SSF54211. 1 hit.
    SSF55874. SSF55874. 1 hit.
    SSF56719. SSF56719. 2 hits.
    TIGRFAMsiTIGR01059. gyrB. 1 hit.
    PROSITEiPS00177. TOPOISOMERASE_II. 1 hit.
    PS50880. TOPRIM. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P0AES6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSNSYDSSSI KVLKGLDAVR KRPGMYIGDT DDGTGLHHMV FEVVDNAIDE    50
    ALAGHCKEII VTIHADNSVS VQDDGRGIPT GIHPEEGVSA AEVIMTVLHA 100
    GGKFDDNSYK VSGGLHGVGV SVVNALSQKL ELVIQREGKI HRQIYEHGVP 150
    QAPLAVTGET EKTGTMVRFW PSLETFTNVT EFEYEILAKR LRELSFLNSG 200
    VSIRLRDKRD GKEDHFHYEG GIKAFVEYLN KNKTPIHPNI FYFSTEKDGI 250
    GVEVALQWND GFQENIYCFT NNIPQRDGGT HLAGFRAAMT RTLNAYMDKE 300
    GYSKKAKVSA TGDDAREGLI AVVSVKVPDP KFSSQTKDKL VSSEVKSAVE 350
    QQMNELLAEY LLENPTDAKI VVGKIIDAAR AREAARRARE MTRRKGALDL 400
    AGLPGKLADC QERDPALSEL YLVEGDSAGG SAKQGRNRKN QAILPLKGKI 450
    LNVEKARFDK MLSSQEVATL ITALGCGIGR DEYNPDKLRY HSIIIMTDAD 500
    VDGSHIRTLL LTFFYRQMPE IVERGHVYIA QPPLYKVKKG KQEQYIKDDE 550
    AMDQYQISIA LDGATLHTNA SAPALAGEAL EKLVSEYNAT QKMINRMERR 600
    YPKAMLKELI YQPTLTEADL SDEQTVTRWV NALVSELNDK EQHGSQWKFD 650
    VHTNAEQNLF EPIVRVRTHG VDTDYPLDHE FITGGEYRRI CTLGEKLRGL 700
    LEEDAFIERG ERRQPVASFE QALDWLVKES RRGLSIQRYK GLGEMNPEQL 750
    WETTMDPESR RMLRVTVKDA IAADQLFTTL MGDAVEPRRA FIEENALKAA 800
    NIDI 804
    Length:804
    Mass (Da):89,950
    Last modified:January 23, 2007 - v2
    Checksum:iD831B95FFB3A7EE3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti385 – 3851A → P in AAA62050. (PubMed:7686882)Curated
    Sequence conflicti436 – 4361R → G in BAA20341. (PubMed:9148951)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti426 – 4261D → N in nal-24, nal-102, nal-103, nal-107, nal-108, nal-111, nal-114, en-2 and en-5 mutants; resistant to nalidixic acid and to enoxacin.
    Natural varianti447 – 4471K → E in nal-31, nal-109, nal-115 and nal-120 mutants; resistant to nalidixic acid.
    Natural varianti751 – 7511W → R in B17 resistant mutant.
    Natural varianti759 – 7602SR → RC in acriflavine susceptible mutant.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04341 Genomic DNA. Translation: CAA27871.1.
    D87842 Genomic DNA. Translation: BAA20341.1.
    L10328 Genomic DNA. Translation: AAA62050.1.
    U00096 Genomic DNA. Translation: AAT48201.1.
    AP009048 Genomic DNA. Translation: BAE77595.1.
    M15548 Genomic DNA. Translation: AAA23949.1.
    PIRiD65172. ISECTB.
    RefSeqiYP_026241.1. NC_000913.3.
    YP_491736.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAT48201; AAT48201; b3699.
    BAE77595; BAE77595; BAE77595.
    GeneIDi12930543.
    948211.
    KEGGiecj:Y75_p3474.
    eco:b3699.
    PATRICi32122895. VBIEscCol129921_3823.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04341 Genomic DNA. Translation: CAA27871.1 .
    D87842 Genomic DNA. Translation: BAA20341.1 .
    L10328 Genomic DNA. Translation: AAA62050.1 .
    U00096 Genomic DNA. Translation: AAT48201.1 .
    AP009048 Genomic DNA. Translation: BAE77595.1 .
    M15548 Genomic DNA. Translation: AAA23949.1 .
    PIRi D65172. ISECTB.
    RefSeqi YP_026241.1. NC_000913.3.
    YP_491736.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AJ6 X-ray 2.30 A 2-220 [» ]
    1EI1 X-ray 2.30 A/B 6-392 [» ]
    1KZN X-ray 2.30 A 15-219 [» ]
    3G7E X-ray 2.20 A 15-217 [» ]
    3NUH X-ray 3.10 B 389-804 [» ]
    4DUH X-ray 1.50 A/B 1-220 [» ]
    4HYP X-ray 2.60 A/B/C/D 15-220 [» ]
    4KFG X-ray 1.60 A/B 15-220 [» ]
    ProteinModelPortali P0AES6.
    SMRi P0AES6. Positions 10-392, 402-784.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-48005N.
    IntActi P0AES6. 18 interactions.
    STRINGi 511145.b3699.

    Chemistry

    BindingDBi P0AES6.
    ChEMBLi CHEMBL2311224.
    DrugBanki DB00817. Rosoxacin.

    Proteomic databases

    PaxDbi P0AES6.
    PRIDEi P0AES6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAT48201 ; AAT48201 ; b3699 .
    BAE77595 ; BAE77595 ; BAE77595 .
    GeneIDi 12930543.
    948211.
    KEGGi ecj:Y75_p3474.
    eco:b3699.
    PATRICi 32122895. VBIEscCol129921_3823.

    Organism-specific databases

    EchoBASEi EB0419.
    EcoGenei EG10424. gyrB.

    Phylogenomic databases

    eggNOGi COG0187.
    HOGENOMi HOG000075155.
    KOi K02470.
    OMAi HIIIMTD.
    OrthoDBi EOG6P334W.
    PhylomeDBi P0AES6.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10424-MONOMER.
    ECOL316407:JW5625-MONOMER.
    MetaCyc:EG10424-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0AES6.
    PROi P0AES6.

    Gene expression databases

    Genevestigatori P0AES6.

    Family and domain databases

    Gene3Di 3.30.230.10. 1 hit.
    3.30.565.10. 1 hit.
    3.40.50.670. 2 hits.
    HAMAPi MF_01898. GyrB.
    InterProi IPR002288. DNA_gyrase_B_C.
    IPR011557. GyrB.
    IPR003594. HATPase_ATP-bd.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
    IPR001241. Topo_IIA.
    IPR013506. Topo_IIA_bsu_dom2.
    IPR013759. Topo_IIA_cen_dom.
    IPR013760. Topo_IIA_like_dom.
    IPR018522. TopoIIA_CS.
    IPR006171. Toprim_domain.
    [Graphical view ]
    Pfami PF00204. DNA_gyraseB. 1 hit.
    PF00986. DNA_gyraseB_C. 1 hit.
    PF02518. HATPase_c. 1 hit.
    PF01751. Toprim. 1 hit.
    [Graphical view ]
    PRINTSi PR00418. TPI2FAMILY.
    SMARTi SM00387. HATPase_c. 1 hit.
    SM00433. TOP2c. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54211. SSF54211. 1 hit.
    SSF55874. SSF55874. 1 hit.
    SSF56719. SSF56719. 2 hits.
    TIGRFAMsi TIGR01059. gyrB. 1 hit.
    PROSITEi PS00177. TOPOISOMERASE_II. 1 hit.
    PS50880. TOPRIM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nalidixic acid-resistant mutations of the gyrB gene of Escherichia coli."
      Yamagishi J., Yoshida H., Yamayoshi M., Nakamura S.
      Mol. Gen. Genet. 204:367-373(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    2. "DNA sequence of the E. coli gyrB gene: application of a new sequencing strategy."
      Adachi T., Mizuuchi M., Robinson E.A., Appella E., O'Dea M.H., Gellert M., Mizuuchi K.
      Nucleic Acids Res. 15:771-784(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    3. "acrB mutation located at carboxyl-terminal region of gyrase B subunit reduces DNA binding of DNA gyrase."
      Funatsuki K., Tanaka R., Inagaki S., Konno H., Katoh K., Nakamura H.
      J. Biol. Chem. 272:13302-13308(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12 / N2879.
    4. "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication."
      Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.
      Genomics 16:551-561(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    6. Cited for: SEQUENCE REVISION TO 385.
    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. "DNA sequence and transcription of the region upstream of the E. coli gyrB gene."
      Adachi T., Mizuuchi K., Menzel R., Gellert M.
      Nucleic Acids Res. 12:6389-6395(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-106.
      Strain: K12.
    9. "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 1-22.
    10. "Characterization of the ATP binding site on Escherichia coli DNA gyrase. Affinity labeling of Lys-103 and Lys-110 of the B subunit by pyridoxal 5'-diphospho-5'-adenosine."
      Tamura J.K., Gellert M.
      J. Biol. Chem. 265:21342-21349(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 93-129.
    11. "The peptide antibiotic microcin B17 induces double-strand cleavage of DNA mediated by E. coli DNA gyrase."
      Vizan J.L., Hernandez-Chico C., del Castillo I., Moreno F.
      EMBO J. 10:467-476(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTANTS B17 RESISTANT.
    12. "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.
    13. "The role of GyrB in the DNA cleavage-religation reaction of DNA gyrase: a proposed two metal-ion mechanism."
      Noble C.G., Maxwell A.
      J. Mol. Biol. 318:361-371(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, MUTAGENESIS OF GLU-424; ASP-498; ASP-500 AND ASP-502.
    14. "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: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT.
    15. "A domain insertion in Escherichia coli GyrB adopts a novel fold that plays a critical role in gyrase function."
      Schoeffler A.J., May A.P., Berger J.M.
      Nucleic Acids Res. 38:7830-7844(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 388-804, SUBUNIT, CATALYTIC ACTIVITY, FUNCTION.
    16. "Structure-based discovery of substituted 4,5'-bithiazoles as novel DNA gyrase inhibitors."
      Brvar M., Perdih A., Renko M., Anderluh G., Turk D., Solmajer T.
      J. Med. Chem. 55:6413-6426(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 1-220, CATALYTIC ACTIVITY.
    17. "Quinolone resistance-determining region in the DNA gyrase gyrB gene of Escherichia coli."
      Yoshida H., Bogaki M., Nakamura M., Yamanaka L.M., Nakamura S.
      Antimicrob. Agents Chemother. 35:1647-1650(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS QUINOLONE-RESISTANT.
      Strain: K16.
    18. "Crystal structure of an N-terminal fragment of the DNA gyrase B protein."
      Wigley D.B., Davies G.J., Dodson E.J., Maxwell A., Dodson G.
      Nature 351:624-629(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-393.
    19. "The entropic penalty of ordered water accounts for weaker binding of the antibiotic novobiocin to a resistant mutant of DNA gyrase: a thermodynamic and crystallographic study."
      Holdgate G.A., Tunnicliffe A., Ward W.H., Weston S.A., Rosenbrock G., Barth P.T., Taylor I.W., Pauptit R.A., Timms D.
      Biochemistry 36:9663-9673(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-221 OF MUTANT HIS-136.

    Entry informationi

    Entry nameiGYRB_ECOLI
    AccessioniPrimary (citable) accession number: P0AES6
    Secondary accession number(s): O08438, P06982, Q2M811
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 93 of the entry and version 2 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