UniProtKB - P0AES6 (GYRB_ECOLI)
DNA gyrase subunit B
gyrB
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 PublicationsMiscellaneous
Catalytic activityi
- ATP-dependent breakage, passage and rejoining of double-stranded DNA.UniRule annotation7 Publications EC:5.6.2.2
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
Activity regulationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 5 | ATP1 Publication2 Publications | 1 | |
Active sitei | 42 | Proton acceptor (ATPase activity)2 Publications | 1 | |
Binding sitei | 46 | ADP3 Publications | 1 | |
Binding sitei | 73 | ATP3 Publications | 1 | |
Metal bindingi | 94 | Potassium; via carbonyl oxygen1 Publication | 1 | |
Metal bindingi | 97 | Potassium; via carbonyl oxygen1 Publication | 1 | |
Metal bindingi | 100 | Potassium; via carbonyl oxygen1 Publication | 1 | |
Metal bindingi | 103 | Sodium1 Publication | 1 | |
Metal bindingi | 105 | Sodium1 Publication | 1 | |
Binding sitei | 109 | ATP3 Publications | 1 | |
Metal bindingi | 117 | Potassium; via carbonyl oxygen1 Publication | 1 | |
Metal bindingi | 121 | Potassium1 Publication | 1 | |
Sitei | 337 | Transition state stabilizer1 Publication | 1 | |
Metal bindingi | 424 | Magnesium 1; catalyticUniRule annotation2 Publications | 1 | |
Metal bindingi | 498 | Magnesium 1; catalyticUniRule annotation2 Publications | 1 | |
Metal bindingi | 498 | Magnesium 2UniRule annotation2 Publications | 1 | |
Metal bindingi | 500 | Magnesium 2UniRule annotation2 Publications | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 102 – 103 | ATP3 Publications | 2 | |
Nucleotide bindingi | 115 – 120 | ATP3 Publications | 6 | |
Nucleotide bindingi | 335 – 337 | ATP2 Publications | 3 |
GO - Molecular functioni
- ATP binding Source: EcoliWiki
- ATP-dependent activity, acting on DNA Source: EcoliWiki
- DNA binding Source: EcoliWiki
- DNA negative supercoiling activity Source: UniProtKB
- DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity Source: EcoliWiki
- metal ion binding Source: UniProtKB-KW
GO - Biological processi
- DNA-dependent DNA replication Source: UniProtKB-UniRule
- DNA topological change Source: ComplexPortal
- response to antibiotic Source: UniProtKB-KW
- transcription, DNA-templated Source: EcoliWiki
Keywordsi
Molecular function | DNA-binding, Isomerase, Topoisomerase |
Biological process | Antibiotic resistance |
Ligand | ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Potassium, Sodium |
Enzyme and pathway databases
BioCyci | EcoCyc:EG10424-MONOMER |
BRENDAi | 5.6.2.2, 2026 |
Names & Taxonomyi
Protein namesi | Recommended name: DNA gyrase subunit BUniRule annotation (EC:5.6.2.2UniRule 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 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm UniRule annotation
Cytosol
- cytosol Source: EcoCyc
Other locations
- chromosome Source: InterPro
- cytoplasm Source: EcoliWiki
- DNA gyrase complex Source: ComplexPortal
- DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex Source: EcoliWiki
Keywords - Cellular componenti
CytoplasmPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 1 – 14 | Missing : No dimerization of residues 15-393, fragment has no ATPase activity. 1 PublicationAdd BLAST | 14 | |
Mutagenesisi | 5 | Y → 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 | 1 | |
Mutagenesisi | 10 | I → G: No dimerization of residues 2-393, fragment has significantly decreased ATPase activity. 1 Publication | 1 | |
Mutagenesisi | 38 | H → A: 0.2% supercoiling activity, 7% DNA-dependent ATPase activity, binds ATP normally, complements the N4177 ts mutant. 1 Publication | 1 | |
Mutagenesisi | 42 | E → 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 | 1 | |
Mutagenesisi | 42 | E → 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 | 1 | |
Mutagenesisi | 42 | E → Q: No supercoiling or DNA-dependent ATPase activity, binds ATP normally, does not complement the N4177 ts mutant. 1 Publication | 1 | |
Mutagenesisi | 103 | K → 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 | 1 | |
Mutagenesisi | 110 | K → 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 | 1 | |
Mutagenesisi | 136 | R → C, H or S: Resistance to coumarin antibiotics, decreased ATPase and DNA supercoiling. 1 Publication | 1 | |
Mutagenesisi | 164 | G → V: Resistance to coumarin antibiotics, decreased ATPase and DNA supercoiling. 1 Publication | 1 | |
Mutagenesisi | 335 | Q → 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 | 1 | |
Mutagenesisi | 337 | K → 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 | 1 | |
Mutagenesisi | 424 | E → 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 | 1 | |
Mutagenesisi | 436 | R → S: Cannot be made, suggesting it is lethal. This is temperature-sensitive in S.typhimurium, but not lethal. 1 Publication | 1 | |
Mutagenesisi | 498 | D → 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 | 1 | |
Mutagenesisi | 500 | D → 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 | 1 | |
Mutagenesisi | 500 | D → C or H: Alters metal-dependency of ATP-independent DNA relaxation, prefers Mn(2+) and Co(2+) over wild-type Mg(2+). 1 Publication | 1 | |
Mutagenesisi | 502 | D → 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 | 1 | |
Mutagenesisi | 502 | D → C or H: Alters metal-dependency of ATP-independent DNA relaxation, prefers Mn(2+) and Co(2+) over wild-type Mg(2+). 1 Publication | 1 |
Chemistry databases
ChEMBLi | CHEMBL1826 |
DrugBanki | DB03966, Clorobiocin DB04395, Phosphoaminophosphonic Acid-Adenylate Ester DB00817, Rosoxacin DB05488, Technetium Tc-99m ciprofloxacin |
DrugCentrali | P0AES6 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed1 Publication | |||
ChainiPRO_0000145309 | 2 – 804 | DNA gyrase subunit BAdd BLAST | 803 |
Proteomic databases
jPOSTi | P0AES6 |
PaxDbi | P0AES6 |
PRIDEi | P0AES6 |
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 PublicationsSites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 449 | Interaction with DNAUniRule annotation | 1 | |
Sitei | 452 | Interaction with DNAUniRule annotation | 1 |
Binary interactionsi
P0AES6
With | #Exp. | IntAct |
---|---|---|
gyrA [P0AES4] | 7 | EBI-541911,EBI-547129 |
Protein-protein interaction databases
BioGRIDi | 4259537, 175 interactors |
ComplexPortali | CPX-2177, GyrA-GyrB DNA Gyrase complex |
DIPi | DIP-48005N |
IntActi | P0AES6, 20 interactors |
STRINGi | 511145.b3699 |
Chemistry databases
BindingDBi | P0AES6 |
Structurei
Secondary structure
3D structure databases
BMRBi | P0AES6 |
SMRi | P0AES6 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P0AES6 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 418 – 533 | ToprimUniRule annotationAdd BLAST | 116 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 2 – 220 | ATPase domain2 PublicationsAdd BLAST | 219 | |
Regioni | 221 – 392 | Transducer domain2 PublicationsAdd BLAST | 172 |
Domaini
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG0187, Bacteria |
HOGENOMi | CLU_006146_4_1_6 |
InParanoidi | P0AES6 |
PhylomeDBi | P0AES6 |
Family and domain databases
CDDi | cd03366, TOPRIM_TopoIIA_GyrB, 1 hit |
Gene3Di | 3.30.230.10, 1 hit 3.30.565.10, 1 hit 3.40.50.670, 2 hits |
HAMAPi | MF_01898, GyrB, 1 hit |
InterProi | View protein in InterPro IPR002288, DNA_gyrase_B_C IPR011557, GyrB IPR041423, GyrB_insert IPR003594, HATPase_C IPR036890, HATPase_C_sf IPR020568, Ribosomal_S5_D2-typ_fold IPR014721, Ribosomal_S5_D2-typ_fold_subgr IPR001241, Topo_IIA IPR013760, Topo_IIA-like_dom_sf IPR013759, Topo_IIA_B_C IPR013506, Topo_IIA_bsu_dom2 IPR018522, TopoIIA_CS IPR006171, TOPRIM_domain IPR034160, TOPRIM_GyrB |
Pfami | View protein in Pfam PF00204, DNA_gyraseB, 1 hit PF00986, DNA_gyraseB_C, 1 hit PF18053, GyrB_insert, 1 hit PF02518, HATPase_c, 1 hit PF01751, Toprim, 1 hit |
SMARTi | View protein in SMART SM00387, HATPase_c, 1 hit SM00433, TOP2c, 1 hit |
SUPFAMi | SSF54211, SSF54211, 1 hit SSF55874, SSF55874, 1 hit SSF56719, SSF56719, 1 hit |
TIGRFAMsi | TIGR01059, gyrB, 1 hit |
PROSITEi | View protein in PROSITE PS00177, TOPOISOMERASE_II, 1 hit PS50880, TOPRIM, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 385 | A → P in AAA62050 (PubMed:7686882).Curated | 1 | |
Sequence conflicti | 436 | R → G in BAA20341 (PubMed:9148951).Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural varianti | 426 | D → 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 | 1 | |
Natural varianti | 447 | K → E in nal-31, nal-109, nal-115 and nal-120 mutants; resistant to nalidixic acid. 1 Publication | 1 | |
Natural varianti | 751 | W → R in microcin B17 resistant mutant. 1 Publication | 1 | |
Natural varianti | 759 – 760 | SR → RC in acriflavine susceptible mutant acrB, decreased supercoiling activity, ATPase activity no longer stimulated by DNA, decreased DNA-binding, bind GyrA normally. 1 Publication | 2 |
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 |
PIRi | D65172, ISECTB |
RefSeqi | WP_000072067.1, NZ_STEB01000015.1 YP_026241.1, NC_000913.3 |
Genome annotation databases
EnsemblBacteriai | AAT48201; AAT48201; b3699 BAE77595; BAE77595; BAE77595 |
GeneIDi | 66672403 948211 |
KEGGi | ecj:JW5625 eco:b3699 |
PATRICi | fig|511145.12.peg.3823 |
Similar proteinsi
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 |
PIRi | D65172, ISECTB |
RefSeqi | WP_000072067.1, NZ_STEB01000015.1 YP_026241.1, NC_000913.3 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1AJ6 | X-ray | 2.30 | A | 2-220 | [»] | |
1EI1 | X-ray | 2.30 | A/B | 2-392 | [»] | |
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 | [»] | |
4PRV | X-ray | 2.00 | A | 2-392 | [»] | |
4PRX | X-ray | 1.80 | A | 2-392 | [»] | |
4PU9 | X-ray | 2.40 | A | 2-392 | [»] | |
4WUB | X-ray | 1.75 | A | 2-393 | [»] | |
4WUC | X-ray | 1.90 | A | 2-393 | [»] | |
4WUD | X-ray | 1.95 | A | 2-393 | [»] | |
4XTJ | X-ray | 1.92 | A | 2-392 | [»] | |
4ZVI | X-ray | 2.20 | A | 16-392 | [»] | |
5L3J | X-ray | 2.83 | A | 15-392 | [»] | |
5MMN | X-ray | 1.90 | A | 1-220 | [»] | |
5MMO | X-ray | 1.81 | A | 1-220 | [»] | |
5MMP | X-ray | 2.05 | A | 1-220 | [»] | |
5Z4H | X-ray | 2.00 | A/B | 15-221 | [»] | |
5Z4O | X-ray | 1.73 | A/B | 15-221 | [»] | |
5Z9B | X-ray | 2.10 | A/B | 15-221 | [»] | |
5Z9E | X-ray | 1.80 | A/B | 15-221 | [»] | |
5Z9F | X-ray | 1.76 | A/B | 15-221 | [»] | |
5Z9L | X-ray | 1.60 | A/B | 15-221 | [»] | |
5Z9M | X-ray | 2.74 | A/B | 15-221 | [»] | |
5Z9N | X-ray | 2.54 | A | 15-221 | [»] | |
5Z9Q | X-ray | 1.80 | A/B | 15-221 | [»] | |
6ENG | X-ray | 2.30 | A/B | 1-393 | [»] | |
6F86 | X-ray | 1.90 | A | 15-220 | [»] | |
6F8J | X-ray | 1.95 | A | 1-220 | [»] | |
6F94 | X-ray | 2.35 | A | 1-220 | [»] | |
6KZV | X-ray | 2.40 | A | 1-220 | [»] | |
6KZX | X-ray | 2.10 | A | 1-220 | [»] | |
6KZZ | X-ray | 2.00 | A | 1-220 | [»] | |
6L01 | X-ray | 2.60 | A | 1-220 | [»] | |
6RKS | electron microscopy | 4.00 | B/D | 1-804 | [»] | |
6RKU | electron microscopy | 4.00 | B/D | 1-804 | [»] | |
6RKV | electron microscopy | 4.60 | B/D | 1-804 | [»] | |
6RKW | electron microscopy | 6.60 | B/D | 1-804 | [»] | |
7C7N | X-ray | 2.30 | A | 1-220 | [»] | |
7C7O | X-ray | 1.80 | A | 1-220 | [»] | |
BMRBi | P0AES6 | |||||
SMRi | P0AES6 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4259537, 175 interactors |
ComplexPortali | CPX-2177, GyrA-GyrB DNA Gyrase complex |
DIPi | DIP-48005N |
IntActi | P0AES6, 20 interactors |
STRINGi | 511145.b3699 |
Chemistry databases
BindingDBi | P0AES6 |
ChEMBLi | CHEMBL1826 |
DrugBanki | DB03966, Clorobiocin DB04395, Phosphoaminophosphonic Acid-Adenylate Ester DB00817, Rosoxacin DB05488, Technetium Tc-99m ciprofloxacin |
DrugCentrali | P0AES6 |
Proteomic databases
jPOSTi | P0AES6 |
PaxDbi | P0AES6 |
PRIDEi | P0AES6 |
Genome annotation databases
EnsemblBacteriai | AAT48201; AAT48201; b3699 BAE77595; BAE77595; BAE77595 |
GeneIDi | 66672403 948211 |
KEGGi | ecj:JW5625 eco:b3699 |
PATRICi | fig|511145.12.peg.3823 |
Organism-specific databases
EchoBASEi | EB0419 |
Phylogenomic databases
eggNOGi | COG0187, Bacteria |
HOGENOMi | CLU_006146_4_1_6 |
InParanoidi | P0AES6 |
PhylomeDBi | P0AES6 |
Enzyme and pathway databases
BioCyci | EcoCyc:EG10424-MONOMER |
BRENDAi | 5.6.2.2, 2026 |
Miscellaneous databases
EvolutionaryTracei | P0AES6 |
PROi | PR:P0AES6 |
Family and domain databases
CDDi | cd03366, TOPRIM_TopoIIA_GyrB, 1 hit |
Gene3Di | 3.30.230.10, 1 hit 3.30.565.10, 1 hit 3.40.50.670, 2 hits |
HAMAPi | MF_01898, GyrB, 1 hit |
InterProi | View protein in InterPro IPR002288, DNA_gyrase_B_C IPR011557, GyrB IPR041423, GyrB_insert IPR003594, HATPase_C IPR036890, HATPase_C_sf IPR020568, Ribosomal_S5_D2-typ_fold IPR014721, Ribosomal_S5_D2-typ_fold_subgr IPR001241, Topo_IIA IPR013760, Topo_IIA-like_dom_sf IPR013759, Topo_IIA_B_C IPR013506, Topo_IIA_bsu_dom2 IPR018522, TopoIIA_CS IPR006171, TOPRIM_domain IPR034160, TOPRIM_GyrB |
Pfami | View protein in Pfam PF00204, DNA_gyraseB, 1 hit PF00986, DNA_gyraseB_C, 1 hit PF18053, GyrB_insert, 1 hit PF02518, HATPase_c, 1 hit PF01751, Toprim, 1 hit |
SMARTi | View protein in SMART SM00387, HATPase_c, 1 hit SM00433, TOP2c, 1 hit |
SUPFAMi | SSF54211, SSF54211, 1 hit SSF55874, SSF55874, 1 hit SSF56719, SSF56719, 1 hit |
TIGRFAMsi | TIGR01059, gyrB, 1 hit |
PROSITEi | View protein in PROSITE PS00177, TOPOISOMERASE_II, 1 hit PS50880, TOPRIM, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | GYRB_ECOLI | |
Accessioni | P0AES6Primary (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: | February 23, 2022 | |
This is version 151 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families