Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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 to maintain chromosomes in an underwound state (PubMed:186775, PubMed:3031051, PubMed:1323022, PubMed:8248233, PubMed:7811004, PubMed:8621650, PubMed:9657678, PubMed:12051842, PubMed:12051843, PubMed:18642932, PubMed:19060136, PubMed:19965760, PubMed:22457353, PubMed:23294697, PubMed:20356737, PubMed:20675723, PubMed:23352267, PubMed:24386374, PubMed:25202966, PubMed:25849408). This makes better substrates for topoisomerase 4 (ParC and ParE) which is the main enzyme that unlinks newly replicated chromosomes in E.coli (PubMed:9334322). Gyrase catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes (PubMed:22457352). Relaxes negatively supercoiled DNA in an ATP-independent manner (PubMed:337300). E.coli gyrase has higher supercoiling activity than other characterized bacterial gyrases; at comparable concentrations E.coli gyrase introduces more supercoils faster than M.tuberculosis gyrase, while M.tuberculosis gyrase has higher decatenation than supercoiling activity compared to E.coli (PubMed:22457352). E.coli makes 15% more negative supercoils in pBR322 plasmid DNA than S.typhimurium; the S.typhimurium GyrB subunit is toxic in E.coli, while the E.coli copy can be expressed in S.typhimurium even though the 2 subunits have 777/804 residues identical (PubMed:17400739). The enzymatic differences between E.coli gyrase and topoisomerase IV are largely due to the GyrA C-terminal domain (approximately residues 524-841) and specifically the GyrA-box (PubMed:8962066, PubMed:16332690).27 Publications

Catalytic activityi

ATP-dependent breakage, passage and rejoining of double-stranded DNA.UniRule annotation7 Publications

Cofactori

Protein has several cofactor binding sites:
  • Mg2+UniRule annotation2 Publications, Mn2+UniRule annotation2 Publications, Ca2+UniRule annotation2 PublicationsNote: 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+ or Ca2+ (PubMed:12051843, PubMed:18642932).UniRule annotation2 Publications
  • K+1 PublicationNote: Binds one K+ per subunit which interacts with the alpha-phosphate of ATP analog and stimulates ATPase activity of the N-terminal fragment; Na+ or water bind less well (PubMed:25849408).1 Publication
  • Na+1 PublicationNote: Binds one Na+ per subunit, with 4 ligands provided by water; may be able to bind K+, the functional significance of this ion is unclear (PubMed:25849408).1 Publication

Enzyme regulationi

Gyrase is the target of many classes of inhibitors, including coumarins, cyclothialidines, pyrrolopyrimidines, pyrazolthiazoles and (fluoro)quinolones. Coumarins bind to GyrB and are competitive inhibitors of its ATPase activity (PubMed:7811004). Cyclothialidines also bind GyrB and are ATPase competitive inhibitors; they seem to act differently from coumarins (PubMed:7811004, PubMed:8635474). Pyrrolopyrimidines inhibit both GyrB and its paralog in topoisomerase 4 (parE) (PubMed:23294697, PubMed:23352267, PubMed:24386374). Pyrazolthiazoles also inhibit the ATPase activity of GyrB (PubMed:20356737). Quinolones bind GyrA when the enzyme is complexed with DNA and trap the enzyme in a covalent reaction intermediate with DNA (PubMed:3031051, PubMed:12051842, PubMed:337300). Acriflavine inhibits DNA supercoiling and DNA-stimulated ATPase activity (PubMed:9148951). DNA supercoiling activity is protected from fluoroquinolone inhibition by QnrB4; QnrB4 has no effect on supercoiling activity alone (PubMed:19060136).1 Publication10 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei5 – 51ATP1 Publication2 Publications
Active sitei42 – 421Proton acceptor (ATPase activity)2 Publications
Binding sitei46 – 461ADP3 Publications
Binding sitei73 – 731ATP3 Publications
Metal bindingi94 – 941Potassium; via carbonyl oxygen1 Publication
Metal bindingi97 – 971Potassium; via carbonyl oxygen1 Publication
Metal bindingi100 – 1001Potassium; via carbonyl oxygen1 Publication
Metal bindingi103 – 1031Sodium1 Publication
Metal bindingi105 – 1051Sodium1 Publication
Binding sitei109 – 1091ATP3 Publications
Metal bindingi117 – 1171Potassium; via carbonyl oxygen1 Publication
Metal bindingi121 – 1211Potassium1 Publication
Sitei337 – 3371Transition state stabilizer1 Publication
Metal bindingi424 – 4241Magnesium 1; catalyticUniRule annotation2 Publications
Metal bindingi498 – 4981Magnesium 1; catalyticUniRule annotation2 Publications
Metal bindingi498 – 4981Magnesium 2UniRule annotation2 Publications
Metal bindingi500 – 5001Magnesium 2UniRule annotation2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi102 – 1032ATP3 Publications
Nucleotide bindingi115 – 1206ATP3 Publications
Nucleotide bindingi335 – 3373ATP2 Publications

GO - Molecular functioni

  • ATP binding Source: EcoliWiki
  • DNA binding Source: EcoliWiki
  • DNA-dependent ATPase activity Source: EcoliWiki
  • DNA supercoiling activity Source: UniProtKB
  • DNA topoisomerase type II (ATP-hydrolyzing) activity Source: EcoliWiki
  • magnesium ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  • chromosome segregation Source: GO_Central
  • DNA-dependent DNA replication Source: UniProtKB-HAMAP
  • DNA topological change Source: EcoliWiki
  • response to antibiotic Source: UniProtKB-KW
  • response to drug Source: EcoliWiki
  • 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, Potassium, Sodium

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 annotation5 Publications)
Alternative name(s):
Type IIA topoisomerase subunit GyrB
Gene namesi
Name:gyrBUniRule annotation
Synonyms:acrB1 Publication, cou, himB, hisU, nalC, parA, pcbA
Ordered Locus Names:b3699, JW5625
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10424. gyrB.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

  • chromosome Source: InterPro
  • cytoplasm Source: EcoliWiki
  • cytosol Source: EcoCyc
  • DNA topoisomerase complex (ATP-hydrolyzing) Source: EcoliWiki
  • nucleoid Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1 – 1414Missing : No dimerization of residues 15-393, fragment has no ATPase activity. 1 PublicationAdd
BLAST
Mutagenesisi5 – 51Y → F or S: 5- to 10-fold reduced dimerization of residues 2-393, fragment has 3- to 5-fold reduced ATPase activity. Fragment dimerizes upon crystallization. 1 Publication
Mutagenesisi10 – 101I → G: No dimerization of residues 2-393, fragment has significantly decreased ATPase activity. 1 Publication
Mutagenesisi38 – 381H → A: 0.2% supercoiling activity, 7% DNA-dependent ATPase activity, binds ATP normally, complements the N4177 ts mutant. 1 Publication
Mutagenesisi42 – 421E → A: No supercoiling or DNA-dependent ATPase activity, 25% fluoroquinolone-induced DNA cleavage, 50% ATP-independent DNA relaxation, binds ATP normally, does not complement the N4177 ts mutant. 1 Publication
Mutagenesisi42 – 421E → D: 7% supercoiling activity, 16% DNA-dependent ATPase activity, fluoroquinolone-induced DNA cleavage normal, 40% ATP-independent DNA relaxation, binds ATP normally, complements the N4177 ts mutant. 1 Publication
Mutagenesisi42 – 421E → Q: No supercoiling or DNA-dependent ATPase activity, binds ATP normally, does not complement the N4177 ts mutant. 1 Publication
Mutagenesisi103 – 1031K → E, I or T: Retains ATP-independent DNA relaxation and quinolone-induced DNA cleavage; loss of supercoiling activity, loss of ATPase, does not bind ATP analogs. 1 Publication
Mutagenesisi110 – 1101K → E or V: Binds about 50% ATP analog, 2- to 3-fold decreased ATPase, retains ATP-independent DNA relaxation, quinolone-induced DNA cleavage and negative supercoiling activity. 1 Publication
Mutagenesisi136 – 1361R → C, H or S: Resistance to coumarin antibiotics, decreased ATPase and DNA supercoiling. 1 Publication
Mutagenesisi164 – 1641G → V: Resistance to coumarin antibiotics, decreased ATPase and DNA supercoiling. 1 Publication
Mutagenesisi335 – 3351Q → A: Wild-type ATP analog-binding and ATPase activity in N-terminal fragment GyrB43 (residues 2-393), in whole protein wild-type DNA supercoiling and ATP-independent DNA relaxation, 50% ATPase activity which is not stimulated by DNA, complements the N4177 ts mutant. 1 Publication
Mutagenesisi337 – 3371K → Q: Binds about 60% ATP analog but strongly decreased enzyme turnover for ATPase activity in N-terminal fragment GyrB43 (residues 2-393), in whole protein <1% DNA supercoiling and ATPase activity not stimulated by DNA, wild-type ATP-independent DNA relaxation and quinolone-induced DNA cleavage, does not complement the N4177 ts mutant. 1 Publication
Mutagenesisi424 – 4241E → A or Q: Strongly reduced DNA supercoiling and relaxation activity. Reduces ATP hydrolysis in response to DNA binding, but has only minor effect on the basal rate of ATP hydrolysis. 1 Publication
Mutagenesisi436 – 4361R → S: Cannot be made, suggesting it is lethal. This is temperature-sensitive in S.typhimurium, but not lethal. 1 Publication
Mutagenesisi498 – 4981D → A or N: Strongly reduced DNA supercoiling and relaxation activity. 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 DNA supercoiling and relaxation activity. Reduces ATP hydrolysis in response to DNA binding, but has only minor effect on the basal rate of ATP hydrolysis. 1 Publication
Mutagenesisi500 – 5001D → C or H: Alters metal-dependency of ATP-independent DNA relaxation, prefers Mn(2+) and Co(2+) over wild-type Mg(2+). 1 Publication
Mutagenesisi502 – 5021D → A: Strongly reduced DNA supercoiling and relaxation activity. Reduces ATP hydrolysis in response to DNA binding, but has only minor effect on the basal rate of ATP hydrolysis. 1 Publication
Mutagenesisi502 – 5021D → C or H: Alters metal-dependency of ATP-independent DNA relaxation, prefers Mn(2+) and Co(2+) over wild-type Mg(2+). 1 Publication

Chemistry

ChEMBLiCHEMBL2311224.
DrugBankiDB00817. Rosoxacin.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 804803DNA gyrase subunit BPRO_0000145309Add
BLAST

Proteomic databases

EPDiP0AES6.
PaxDbiP0AES6.
PRIDEiP0AES6.

Interactioni

Subunit structurei

Heterotetramer, composed of two GyrA and two GyrB chains (PubMed:9148951, PubMed:12051842). In the heterotetramer, GyrA contains the active site tyrosine that forms a transient covalent intermediate with the DNA, while GyrB binds cofactors and catalyzes ATP hydrolysis (PubMed:12051843, PubMed:18642932, PubMed:20675723, PubMed:19965760).UniRule annotation6 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei449 – 4491Interaction with DNAUniRule annotation
Sitei452 – 4521Interaction with DNAUniRule annotation

Binary interactionsi

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

Protein-protein interaction databases

BioGridi4259537. 154 interactions.
DIPiDIP-48005N.
IntActiP0AES6. 18 interactions.
STRINGi511145.b3699.

Chemistry

BindingDBiP0AES6.

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 strandi265 – 2706Combined sources
Helixi280 – 29920Combined sources
Helixi302 – 3065Combined sources
Helixi312 – 3165Combined sources
Beta strandi319 – 3268Combined sources
Beta strandi332 – 3343Combined sources
Helixi343 – 36321Combined sources
Helixi365 – 39127Combined 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/B2-392[»]
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[»]
4WUBX-ray1.75A2-393[»]
4WUCX-ray1.90A2-393[»]
4WUDX-ray1.95A2-393[»]
4XTJX-ray1.92A2-392[»]
4ZVIX-ray2.20A16-392[»]
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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 220219ATPase domain2 PublicationsAdd
BLAST
Regioni221 – 392172Transducer domain2 PublicationsAdd
BLAST

Domaini

Consists of 3 domains; the ATPase domain (residues 1-220), the transducer domain (221-392) and the toprim domain (393-804) (PubMed:1646964, PubMed:10734094). ATP-binding is cooperative, and both subunits must be wild-type at residue 103 for supercoiling to occur (PubMed:8621650). Non-hydrolyzable ATP analogs (and ATP-binding) induce dimerization and enhance ATPase activity (PubMed:10734094, PubMed:9657678). ATP hydrolysis induces domain shifts that are probably part of the mechanism of DNA cleavage and rejoining (PubMed:25202966).2 Publications3 Publications

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105C7D. Bacteria.
COG0187. LUCA.
HOGENOMiHOG000075155.
InParanoidiP0AES6.
KOiK02470.
OMAiIKNMITA.
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.
IPR013760. Topo_IIA-like_dom.
IPR013506. Topo_IIA_bsu_dom2.
IPR013759. Topo_IIA_cen_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. 1 Publication
Natural varianti447 – 4471K → E in nal-31, nal-109, nal-115 and nal-120 mutants; resistant to nalidixic acid. 1 Publication
Natural varianti751 – 7511W → R in microcin B17 resistant mutant. 1 Publication
Natural varianti759 – 7602SR → RC in acriflavine susceptible mutant acrB, decreased supercoiling activity, ATPase activity no longer stimulated by DNA, decreased DNA-binding, bind GyrA normally. 1 Publication

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.
RefSeqiWP_000072067.1. NZ_LN832404.1.
YP_026241.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAT48201; AAT48201; b3699.
BAE77595; BAE77595; BAE77595.
GeneIDi948211.
KEGGiecj:JW5625.
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.
RefSeqiWP_000072067.1. NZ_LN832404.1.
YP_026241.1. NC_000913.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AJ6X-ray2.30A2-220[»]
1EI1X-ray2.30A/B2-392[»]
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[»]
4WUBX-ray1.75A2-393[»]
4WUCX-ray1.90A2-393[»]
4WUDX-ray1.95A2-393[»]
4XTJX-ray1.92A2-392[»]
4ZVIX-ray2.20A16-392[»]
ProteinModelPortaliP0AES6.
SMRiP0AES6. Positions 10-392, 406-783.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259537. 154 interactions.
DIPiDIP-48005N.
IntActiP0AES6. 18 interactions.
STRINGi511145.b3699.

Chemistry

BindingDBiP0AES6.
ChEMBLiCHEMBL2311224.
DrugBankiDB00817. Rosoxacin.

Proteomic databases

EPDiP0AES6.
PaxDbiP0AES6.
PRIDEiP0AES6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAT48201; AAT48201; b3699.
BAE77595; BAE77595; BAE77595.
GeneIDi948211.
KEGGiecj:JW5625.
eco:b3699.
PATRICi32122895. VBIEscCol129921_3823.

Organism-specific databases

EchoBASEiEB0419.
EcoGeneiEG10424. gyrB.

Phylogenomic databases

eggNOGiENOG4105C7D. Bacteria.
COG0187. LUCA.
HOGENOMiHOG000075155.
InParanoidiP0AES6.
KOiK02470.
OMAiIKNMITA.
OrthoDBiEOG6P334W.
PhylomeDBiP0AES6.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP0AES6.
PROiP0AES6.

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.
IPR013760. Topo_IIA-like_dom.
IPR013506. Topo_IIA_bsu_dom2.
IPR013759. Topo_IIA_cen_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(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] OF VARIANT ACRB, FUNCTION, ENZYME REGULATION, SUBUNIT, DNA-BINDING, ACRIDINE SENSITIVITY.
    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, ATP-BINDING.
  11. "DNA gyrase: an enzyme that introduces superhelical turns into DNA."
    Gellert M., Mizuuchi K., O'Dea M.H., Nash H.A.
    Proc. Natl. Acad. Sci. U.S.A. 73:3872-3876(1976) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN GENERATING NEGATIVELY SUPERCOILED DNA, CATALYTIC ACTIVITY, ATP-DEPENDENCE.
  12. "Nalidixic acid resistance: a second genetic character involved in DNA gyrase activity."
    Gellert M., Mizuuchi K., O'Dea M.H., Itoh T., Tomizawa J.I.
    Proc. Natl. Acad. Sci. U.S.A. 74:4772-4776(1977) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN RELAXING SUPERCOILED DNA, ENZYME REGULATION.
  13. "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: REACTION MECHANISM, DNA-BINDING.
  14. "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 MICROCIN B17 RESISTANT.
  15. "gyrB mutations which confer coumarin resistance also affect DNA supercoiling and ATP hydrolysis by Escherichia coli DNA gyrase."
    Contreras A., Maxwell A.
    Mol. Microbiol. 6:1617-1624(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ARG-136 AND GLY-164, ANTIBIOTIC RESISTANCE.
  16. "Identifying the catalytic residue of the ATPase reaction of DNA gyrase."
    Jackson A.P., Maxwell A.
    Proc. Natl. Acad. Sci. U.S.A. 90:11232-11236(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ATPASE ACTIVE SITE, MUTAGENESIS OF HIS-38 AND GLU-42.
  17. "Mechanism of inhibition of DNA gyrase by cyclothialidine, a novel DNA gyrase inhibitor."
    Nakada N., Gmuender H., Hirata T., Arisawa M.
    Antimicrob. Agents Chemother. 38:1966-1973(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION.
  18. "Mutations in the B subunit of Escherichia coli DNA gyrase that affect ATP-dependent reactions."
    O'Dea M.H., Tamura J.K., Gellert M.
    J. Biol. Chem. 271:9723-9729(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DOMAIN, MUTAGENESIS OF LYS-103 AND LYS-110.
  19. "Conversion of DNA gyrase into a conventional type II topoisomerase."
    Kampranis S.C., Maxwell A.
    Proc. Natl. Acad. Sci. U.S.A. 93:14416-14421(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  20. "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.
  21. "Topoisomerase IV, not gyrase, decatenates products of site-specific recombination in Escherichia coli."
    Zechiedrich E.L., Khodursky A.B., Cozzarelli N.R.
    Genes Dev. 11:2580-2592(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  22. "Identification of a residue involved in transition-state stabilization in the ATPase reaction of DNA gyrase."
    Smith C.V., Maxwell A.
    Biochemistry 37:9658-9667(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DOMAIN, MUTAGENESIS OF GLN-335 AND LYS-337.
  23. "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.
  24. "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.
  25. "The 'GyrA-box' is required for the ability of DNA gyrase to wrap DNA and catalyze the supercoiling reaction."
    Kramlinger V.M., Hiasa H.
    J. Biol. Chem. 281:3738-3742(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  26. "Growth rate toxicity phenotypes and homeostatic supercoil control differentiate Escherichia coli from Salmonella enterica serovar Typhimurium."
    Champion K., Higgins N.P.
    J. Bacteriol. 189:5839-5849(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ARG-436.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  27. "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.
  28. "The pentapeptide repeat proteins MfpAMt and QnrB4 exhibit opposite effects on DNA gyrase catalytic reactions and on the ternary gyrase-DNA-quinolone complex."
    Merens A., Matrat S., Aubry A., Lascols C., Jarlier V., Soussy C.J., Cavallo J.D., Cambau E.
    J. Bacteriol. 191:1587-1594(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION.
  29. "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: FUNCTION, CATALYTIC ACTIVITY, SUBUNIT.
  30. "Mechanisms for defining supercoiling set point of DNA gyrase orthologs: I. A nonconserved acidic C-terminal tail modulates Escherichia coli gyrase activity."
    Tretter E.M., Berger J.M.
    J. Biol. Chem. 287:18636-18644(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DNA-BINDING.
  31. "Mechanisms for defining supercoiling set point of DNA gyrase orthologs: II. The shape of the GyrA subunit C-terminal domain (CTD) is not a sole determinant for controlling supercoiling efficiency."
    Tretter E.M., Berger J.M.
    J. Biol. Chem. 287:18645-18654(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DNA-BINDING.
  32. "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 ASN-426 AND GLU-447.
    Strain: K16.
  33. "Pyrrolopyrimidine inhibitors of DNA gyrase B (GyrB) and topoisomerase IV (ParE), Part II: development of inhibitors with broad spectrum, Gram-negative antibacterial activity."
    Trzoss M., Bensen D.C., Li X., Chen Z., Lam T., Zhang J., Creighton C.J., Cunningham M.L., Kwan B., Stidham M., Nelson K., Brown-Driver V., Castellano A., Shaw K.J., Lightstone F.C., Wong S.E., Nguyen T.B., Finn J., Tari L.W.
    Bioorg. Med. Chem. Lett. 23:1537-1543(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION.
  34. "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 IN COMPLEX WITH ATP ANALOG, DOMAIN.
  35. "The nature of inhibition of DNA gyrase by the coumarins and the cyclothialidines revealed by X-ray crystallography."
    Lewis R.J., Singh O.M., Smith C.V., Skarzynski T., Maxwell A., Wonacott A.J., Wigley D.B.
    EMBO J. 15:1412-1420(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-220 IN COMPLEX WITH COUMARIN AND CYCLOTHIALIDINE ANTIBIOTICS, ENZYME REGULATION.
  36. "The high-resolution crystal structure of a 24-kDa gyrase B fragment from E. coli complexed with one of the most potent coumarin inhibitors, clorobiocin."
    Tsai F.T., Singh O.M., Skarzynski T., Wonacott A.J., Weston S., Tucker A., Pauptit R.A., Breeze A.L., Poyser J.P., O'Brien R., Ladbury J.E., Wigley D.B.
    Proteins 28:41-52(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-220 IN COMPLEX WITH CHLOROBIOCIN.
  37. "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 2-220 OF MUTANT HIS-136 IN COMPLEX WITH NOVOBIOCIN.
  38. "Dimerization of Escherichia coli DNA-gyrase B provides a structural mechanism for activating the ATPase catalytic center."
    Brino L., Urzhumtsev A., Mousli M., Bronner C., Mitschler A., Oudet P., Moras D.
    J. Biol. Chem. 275:9468-9475(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 2-392 OF MUTANT SER-5 IN COMPLEX WITH ATP ANALOG, ACTIVE SITE, DOMAIN, MUTAGENESIS OF 1-MET--LYS-14; TYR-5 AND ILE-10, ATP-BINDING.
  39. "DNA gyrase interaction with coumarin-based inhibitors: the role of the hydroxybenzoate isopentenyl moiety and the 5'-methyl group of the noviose."
    Lafitte D., Lamour V., Tsvetkov P.O., Makarov A.A., Klich M., Deprez P., Moras D., Briand C., Gilli R.
    Biochemistry 41:7217-7223(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 15-219 IN COMPLEX WITH CLOROBIOCIN.
  40. Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 15-217 IN COMPLEX WITH PYRAZOLTHIAZOLE INHIBITOR, FUNCTION, ENZYME REGULATION.
  41. "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, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT.
  42. "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.
  43. "Pyrrolopyrimidine inhibitors of DNA gyrase B (GyrB) and topoisomerase IV (ParE). Part I: Structure guided discovery and optimization of dual targeting agents with potent, broad-spectrum enzymatic activity."
    Tari L.W., Trzoss M., Bensen D.C., Li X., Chen Z., Lam T., Zhang J., Creighton C.J., Cunningham M.L., Kwan B., Stidham M., Shaw K.J., Lightstone F.C., Wong S.E., Nguyen T.B., Nix J., Finn J.
    Bioorg. Med. Chem. Lett. 23:1529-1536(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 15-220 IN COMPLEX WITH INHIBITOR, FUNCTION, ENZYME REGULATION.
  44. Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 15-220 IN COMPLEX WITH INHIBITOR, FUNCTION, ENZYME REGULATION.
  45. "Structure of the N-terminal Gyrase B fragment in complex with ADPPi reveals rigid-body motion induced by ATP hydrolysis."
    Stanger F.V., Dehio C., Schirmer T.
    PLoS ONE 9:E107289-E107289(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 2-392 IN OPEN; SEMI-OPEN AND CLOSED STATES IN COMPLEX WITH ADP AND ATP ANALOGS, ATPASE ACTIVITY, PROBABLE MECHANISM, DOMAIN, ATP-BINDING.
  46. "The role of monovalent cations in the ATPase reaction of DNA gyrase."
    Hearnshaw S.J., Chung T.T., Stevenson C.E., Maxwell A., Lawson D.M.
    Acta Crystallogr. D 71:996-1005(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 2-393 IN COMPLEX WITH ATP ANALOG AND MONOVALENT CATIONS, ATPASE ACTIVITY.

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 13, 2016
This is version 109 of the entry and version 2 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 in an ATP-independent manner (PubMed:3031051). In the presence of quinolones this intermediate can be trapped and is used as an indicator of drug toxicity (PubMed:12051842).1 Publication1 Publication

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

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 one 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.