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)DescriptionActionsGraphical viewLength
Binding sitei5ATP1 Publication2 Publications1
Active sitei42Proton acceptor (ATPase activity)2 Publications1
Binding sitei46ADP3 Publications1
Binding sitei73ATP3 Publications1
Metal bindingi94Potassium; via carbonyl oxygen1 Publication1
Metal bindingi97Potassium; via carbonyl oxygen1 Publication1
Metal bindingi100Potassium; via carbonyl oxygen1 Publication1
Metal bindingi103Sodium1 Publication1
Metal bindingi105Sodium1 Publication1
Binding sitei109ATP3 Publications1
Metal bindingi117Potassium; via carbonyl oxygen1 Publication1
Metal bindingi121Potassium1 Publication1
Sitei337Transition state stabilizer1 Publication1
Metal bindingi424Magnesium 1; catalyticUniRule annotation2 Publications1
Metal bindingi498Magnesium 1; catalyticUniRule annotation2 Publications1
Metal bindingi498Magnesium 2UniRule annotation2 Publications1
Metal bindingi500Magnesium 2UniRule annotation2 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi102 – 103ATP3 Publications2
Nucleotide bindingi115 – 120ATP3 Publications6
Nucleotide bindingi335 – 337ATP2 Publications3

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 topological change Source: EcoliWiki
  • DNA unwinding involved in DNA replication Source: GO_Central
  • 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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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)DescriptionActionsGraphical viewLength
Mutagenesisi1 – 14Missing : No dimerization of residues 15-393, fragment has no ATPase activity. 1 PublicationAdd BLAST14
Mutagenesisi5Y → 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 Publication1
Mutagenesisi10I → G: No dimerization of residues 2-393, fragment has significantly decreased ATPase activity. 1 Publication1
Mutagenesisi38H → A: 0.2% supercoiling activity, 7% DNA-dependent ATPase activity, binds ATP normally, complements the N4177 ts mutant. 1 Publication1
Mutagenesisi42E → 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 Publication1
Mutagenesisi42E → 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 Publication1
Mutagenesisi42E → Q: No supercoiling or DNA-dependent ATPase activity, binds ATP normally, does not complement the N4177 ts mutant. 1 Publication1
Mutagenesisi103K → 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 Publication1
Mutagenesisi110K → 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 Publication1
Mutagenesisi136R → C, H or S: Resistance to coumarin antibiotics, decreased ATPase and DNA supercoiling. 1 Publication1
Mutagenesisi164G → V: Resistance to coumarin antibiotics, decreased ATPase and DNA supercoiling. 1 Publication1
Mutagenesisi335Q → 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 Publication1
Mutagenesisi337K → 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 Publication1
Mutagenesisi424E → 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 Publication1
Mutagenesisi436R → S: Cannot be made, suggesting it is lethal. This is temperature-sensitive in S.typhimurium, but not lethal. 1 Publication1
Mutagenesisi498D → 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 Publication1
Mutagenesisi500D → 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 Publication1
Mutagenesisi500D → C or H: Alters metal-dependency of ATP-independent DNA relaxation, prefers Mn(2+) and Co(2+) over wild-type Mg(2+). 1 Publication1
Mutagenesisi502D → 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 Publication1
Mutagenesisi502D → C or H: Alters metal-dependency of ATP-independent DNA relaxation, prefers Mn(2+) and Co(2+) over wild-type Mg(2+). 1 Publication1

Chemistry databases

ChEMBLiCHEMBL1826.
DrugBankiDB00817. Rosoxacin.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001453092 – 804DNA gyrase subunit BAdd BLAST803

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)DescriptionActionsGraphical viewLength
Sitei449Interaction with DNAUniRule annotation1
Sitei452Interaction with DNAUniRule annotation1

Binary interactionsi

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

Protein-protein interaction databases

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

Chemistry databases

BindingDBiP0AES6.

Structurei

Secondary structure

1804
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi7 – 9Combined sources3
Helixi16 – 21Combined sources6
Helixi24 – 27Combined sources4
Beta strandi30 – 33Combined sources4
Helixi34 – 53Combined sources20
Beta strandi58 – 63Combined sources6
Turni65 – 67Combined sources3
Beta strandi69 – 73Combined sources5
Beta strandi81 – 83Combined sources3
Turni84 – 87Combined sources4
Helixi90 – 96Combined sources7
Turni98 – 101Combined sources4
Beta strandi104 – 108Combined sources5
Beta strandi113 – 115Combined sources3
Helixi120 – 125Combined sources6
Beta strandi127 – 136Combined sources10
Beta strandi139 – 146Combined sources8
Beta strandi149 – 153Combined sources5
Beta strandi155 – 159Combined sources5
Beta strandi164 – 171Combined sources8
Turni173 – 175Combined sources3
Helixi184 – 197Combined sources14
Turni198 – 200Combined sources3
Beta strandi201 – 207Combined sources7
Turni208 – 210Combined sources3
Beta strandi213 – 216Combined sources4
Helixi221 – 230Combined sources10
Beta strandi231 – 233Combined sources3
Beta strandi235 – 238Combined sources4
Beta strandi241 – 247Combined sources7
Beta strandi250 – 262Combined sources13
Beta strandi265 – 270Combined sources6
Beta strandi273 – 279Combined sources7
Helixi280 – 299Combined sources20
Helixi302 – 306Combined sources5
Helixi312 – 316Combined sources5
Beta strandi319 – 326Combined sources8
Beta strandi332 – 334Combined sources3
Helixi343 – 363Combined sources21
Helixi365 – 391Combined sources27
Beta strandi419 – 424Combined sources6
Helixi425 – 435Combined sources11
Turni438 – 440Combined sources3
Beta strandi441 – 446Combined sources6
Helixi465 – 474Combined sources10
Beta strandi491 – 495Combined sources5
Turni501 – 504Combined sources4
Helixi505 – 517Combined sources13
Helixi519 – 523Combined sources5
Beta strandi527 – 530Combined sources4
Beta strandi534 – 539Combined sources6
Beta strandi542 – 546Combined sources5
Helixi549 – 561Combined sources13
Beta strandi564 – 571Combined sources8
Beta strandi573 – 576Combined sources4
Helixi577 – 596Combined sources20
Turni597 – 600Combined sources4
Helixi603 – 611Combined sources9
Helixi617 – 621Combined sources5
Helixi623 – 640Combined sources18
Beta strandi646 – 653Combined sources8
Beta strandi660 – 667Combined sources8
Beta strandi669 – 676Combined sources8
Helixi679 – 683Combined sources5
Helixi685 – 699Combined sources15
Turni700 – 703Combined sources4
Beta strandi704 – 711Combined sources8
Beta strandi713 – 718Combined sources6
Helixi719 – 730Combined sources12
Turni731 – 733Combined sources3
Beta strandi735 – 738Combined sources4
Helixi742 – 744Combined sources3
Helixi747 – 754Combined sources8
Turni757 – 759Combined sources3
Beta strandi762 – 764Combined sources3
Helixi767 – 780Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5L3JX-ray2.83A15-392[»]
ProteinModelPortaliP0AES6.
SMRiP0AES6.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AES6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini418 – 533ToprimUniRule annotationAdd BLAST116

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 220ATPase domain2 PublicationsAdd BLAST219
Regioni221 – 392Transducer domain2 PublicationsAdd BLAST172

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.
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. 1 hit.
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)DescriptionActionsGraphical viewLength
Sequence conflicti385A → P in AAA62050 (PubMed:7686882).Curated1
Sequence conflicti436R → G in BAA20341 (PubMed:9148951).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti426D → 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 Publication1
Natural varianti447K → E in nal-31, nal-109, nal-115 and nal-120 mutants; resistant to nalidixic acid. 1 Publication1
Natural varianti751W → R in microcin B17 resistant mutant. 1 Publication1
Natural varianti759 – 760SR → RC in acriflavine susceptible mutant acrB, decreased supercoiling activity, ATPase activity no longer stimulated by DNA, decreased DNA-binding, bind GyrA normally. 1 Publication2

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
PDB 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[»]
5L3JX-ray2.83A15-392[»]
ProteinModelPortaliP0AES6.
SMRiP0AES6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry databases

BindingDBiP0AES6.
ChEMBLiCHEMBL1826.
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.
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. 1 hit.
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...

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: November 30, 2016
This is version 114 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.