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Protein

DNA gyrase subunit B

Gene

gyrB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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.UniRule annotation3 Publications

Catalytic activityi

ATP-dependent breakage, passage and rejoining of double-stranded DNA.UniRule annotation4 Publications

Cofactori

Mg2+UniRule annotation2 Publications, Mn2+UniRule annotation2 Publications, Ca2+UniRule annotation2 PublicationsNote: Binds two Mg(2+) per subunit. The magnesium ions form salt bridges with both the protein and the DNA. Can also accept other divalent metal cations, such as Mn(2+) or Ca2+.UniRule annotation2 Publications

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

GO - Biological processi

  1. chromosome segregation Source: GO_Central
  2. DNA topological change Source: EcoliWiki
  3. DNA unwinding involved in DNA replication Source: GO_Central
  4. response to antibiotic Source: UniProtKB-KW
  5. response to drug Source: EcoliWiki
  6. transcription, DNA-templated Source: EcoliWiki
Complete GO annotation...

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.
BRENDAi5.99.1.3. 2026.

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 Componenti: Chromosome UP000000625 Componenti: 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: GO_Central
Complete GO annotation...

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.UniRule annotation3 Publications

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 – 93Combined sources
Helixi16 – 216Combined sources
Helixi24 – 274Combined sources
Beta strandi30 – 334Combined sources
Helixi34 – 5320Combined sources
Beta strandi58 – 636Combined sources
Turni65 – 673Combined sources
Beta strandi69 – 735Combined sources
Beta strandi81 – 833Combined sources
Turni84 – 874Combined sources
Helixi90 – 967Combined sources
Turni98 – 1014Combined sources
Beta strandi104 – 1085Combined sources
Beta strandi113 – 1153Combined sources
Helixi120 – 1256Combined sources
Beta strandi127 – 13610Combined sources
Beta strandi139 – 1468Combined sources
Beta strandi149 – 1535Combined sources
Beta strandi155 – 1595Combined sources
Beta strandi164 – 1718Combined sources
Turni173 – 1753Combined sources
Helixi184 – 19714Combined sources
Turni198 – 2003Combined sources
Beta strandi201 – 2077Combined sources
Turni208 – 2103Combined sources
Beta strandi213 – 2164Combined sources
Helixi221 – 23010Combined sources
Beta strandi231 – 2333Combined sources
Beta strandi235 – 2384Combined sources
Beta strandi241 – 2477Combined sources
Beta strandi250 – 26213Combined sources
Beta strandi264 – 2707Combined sources
Helixi280 – 29920Combined sources
Helixi302 – 3065Combined sources
Helixi312 – 3154Combined sources
Turni316 – 3183Combined sources
Beta strandi319 – 3268Combined sources
Beta strandi332 – 3343Combined sources
Helixi343 – 36321Combined sources
Helixi365 – 37612Combined sources
Beta strandi419 – 4246Combined sources
Helixi425 – 43511Combined sources
Turni438 – 4403Combined sources
Beta strandi441 – 4466Combined sources
Helixi465 – 47410Combined sources
Beta strandi491 – 4955Combined sources
Turni501 – 5044Combined sources
Helixi505 – 51713Combined sources
Helixi519 – 5235Combined sources
Beta strandi527 – 5304Combined sources
Beta strandi534 – 5396Combined sources
Beta strandi542 – 5465Combined sources
Helixi549 – 56113Combined sources
Beta strandi564 – 5718Combined sources
Beta strandi573 – 5764Combined sources
Helixi577 – 59620Combined sources
Turni597 – 6004Combined sources
Helixi603 – 6119Combined sources
Helixi617 – 6215Combined sources
Helixi623 – 64018Combined sources
Beta strandi646 – 6538Combined sources
Beta strandi660 – 6678Combined sources
Beta strandi669 – 6768Combined sources
Helixi679 – 6835Combined sources
Helixi685 – 69915Combined sources
Turni700 – 7034Combined sources
Beta strandi704 – 7118Combined sources
Beta strandi713 – 7186Combined sources
Helixi719 – 73012Combined sources
Turni731 – 7333Combined sources
Beta strandi735 – 7384Combined sources
Helixi742 – 7443Combined sources
Helixi747 – 7548Combined sources
Turni757 – 7593Combined sources
Beta strandi762 – 7643Combined sources
Helixi767 – 78014Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4PRVX-ray2.00A2-392[»]
4PRXX-ray1.80A2-392[»]
4PU9X-ray2.40A2-392[»]
ProteinModelPortaliP0AES6.
SMRiP0AES6. Positions 10-392, 406-783.
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.
InParanoidiP0AES6.
KOiK02470.
OMAiIFETTEF.
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_C.
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

        10         20         30         40         50
MSNSYDSSSI KVLKGLDAVR KRPGMYIGDT DDGTGLHHMV FEVVDNAIDE
60 70 80 90 100
ALAGHCKEII VTIHADNSVS VQDDGRGIPT GIHPEEGVSA AEVIMTVLHA
110 120 130 140 150
GGKFDDNSYK VSGGLHGVGV SVVNALSQKL ELVIQREGKI HRQIYEHGVP
160 170 180 190 200
QAPLAVTGET EKTGTMVRFW PSLETFTNVT EFEYEILAKR LRELSFLNSG
210 220 230 240 250
VSIRLRDKRD GKEDHFHYEG GIKAFVEYLN KNKTPIHPNI FYFSTEKDGI
260 270 280 290 300
GVEVALQWND GFQENIYCFT NNIPQRDGGT HLAGFRAAMT RTLNAYMDKE
310 320 330 340 350
GYSKKAKVSA TGDDAREGLI AVVSVKVPDP KFSSQTKDKL VSSEVKSAVE
360 370 380 390 400
QQMNELLAEY LLENPTDAKI VVGKIIDAAR AREAARRARE MTRRKGALDL
410 420 430 440 450
AGLPGKLADC QERDPALSEL YLVEGDSAGG SAKQGRNRKN QAILPLKGKI
460 470 480 490 500
LNVEKARFDK MLSSQEVATL ITALGCGIGR DEYNPDKLRY HSIIIMTDAD
510 520 530 540 550
VDGSHIRTLL LTFFYRQMPE IVERGHVYIA QPPLYKVKKG KQEQYIKDDE
560 570 580 590 600
AMDQYQISIA LDGATLHTNA SAPALAGEAL EKLVSEYNAT QKMINRMERR
610 620 630 640 650
YPKAMLKELI YQPTLTEADL SDEQTVTRWV NALVSELNDK EQHGSQWKFD
660 670 680 690 700
VHTNAEQNLF EPIVRVRTHG VDTDYPLDHE FITGGEYRRI CTLGEKLRGL
710 720 730 740 750
LEEDAFIERG ERRQPVASFE QALDWLVKES RRGLSIQRYK GLGEMNPEQL
760 770 780 790 800
WETTMDPESR RMLRVTVKDA IAADQLFTTL MGDAVEPRRA FIEENALKAA

NIDI
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4PRVX-ray2.00A2-392[»]
4PRXX-ray1.80A2-392[»]
4PU9X-ray2.40A2-392[»]
ProteinModelPortaliP0AES6.
SMRiP0AES6. Positions 10-392, 406-783.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry

BindingDBiP0AES6.
ChEMBLiCHEMBL2311224.
DrugBankiDB00817. Rosoxacin.

Proteomic databases

PaxDbiP0AES6.
PRIDEiP0AES6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EchoBASEiEB0419.
EcoGeneiEG10424. gyrB.

Phylogenomic databases

eggNOGiCOG0187.
HOGENOMiHOG000075155.
InParanoidiP0AES6.
KOiK02470.
OMAiIFETTEF.
OrthoDBiEOG6P334W.
PhylomeDBiP0AES6.

Enzyme and pathway databases

BioCyciEcoCyc:EG10424-MONOMER.
ECOL316407:JW5625-MONOMER.
MetaCyc:EG10424-MONOMER.
BRENDAi5.99.1.3. 2026.

Miscellaneous databases

EvolutionaryTraceiP0AES6.
PROiP0AES6.

Gene expression databases

GenevestigatoriP0AES6.

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_C.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1985) [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(1986) [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(1996) [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(1992) [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(2005) [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(1983) [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(1986) [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(1989) [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(1990) [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(1996) [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(2001) [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(2007) [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(2009) [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(2011) [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(1990) [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(1990) [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(1996) [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: April 1, 2015
This is version 99 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.