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P0AES4

- GYRA_ECOLI

UniProt

P0AES4 - GYRA_ECOLI

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Protein
DNA gyrase subunit A
Gene
gyrA, hisW, nalA, parD, b2231, JW2225
Organism
Escherichia coli (strain K12)
Status
Reviewed - 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.3 Publications

Catalytic activityi

ATP-dependent breakage, passage and rejoining of double-stranded DNA.4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei122 – 1221O-(5'-phospho-DNA)-tyrosine intermediate1 Publication

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. DNA binding Source: EcoliWiki
  3. DNA topoisomerase type II (ATP-hydrolyzing) activity Source: CACAO
  4. DNA-dependent ATPase activity Source: EcoliWiki
  5. identical protein binding Source: IntAct
  6. protein binding Source: IntAct
Complete GO annotation...

GO - Biological processi

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

Keywords - Molecular functioni

Isomerase, Topoisomerase

Keywords - Biological processi

Antibiotic resistance

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10423-MONOMER.
ECOL316407:JW2225-MONOMER.
MetaCyc:EG10423-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA gyrase subunit A (EC:5.99.1.3)
Gene namesi
Name:gyrA
Synonyms:hisW, nalA, parD
Ordered Locus Names:b2231, JW2225
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10423. gyrA.

Subcellular locationi

Cytoplasm Reviewed prediction UniRule annotation

GO - Cellular componenti

  1. DNA topoisomerase complex (ATP-hydrolyzing) Source: RefGenome
  2. chromosome Source: InterPro
  3. cytoplasm Source: UniProtKB
  4. membrane Source: UniProtKB
  5. nucleoid Source: RefGenome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi32 – 321R → A or Q: Nearly abolishes DNA supercoiling. Reduces DNA cleavage and relaxation. 1 Publication
Mutagenesisi47 – 471R → Q: Nearly abolishes DNA supercoiling. Reduces DNA cleavage. Slightly reduces DNA relaxation. 1 Publication
Mutagenesisi78 – 781H → A: Nearly abolishes DNA supercoiling. Reduces DNA cleavage and DNA relaxation. 1 Publication
Mutagenesisi80 – 801H → A: Reduces DNA supercoiling. Slightly reduces DNA cleavage. No effect on DNA relaxation. 1 Publication
Mutagenesisi83 – 831S → A: Resistant to fluoroquinolones. 1 Publication
Mutagenesisi106 – 1061Q → R: Resistant to fluoroquinolones. 1 Publication
Mutagenesisi462 – 4621R → C in gyrA462; resistant to cytotoxic protein CcdB, but not to the quinoline antibiotic enoxacin, has no effect on DNA supercoiling. Does not interact with CcdB. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedUniRule annotation
Chaini2 – 875874DNA gyrase subunit AUniRule annotation
PRO_0000145232Add
BLAST

Proteomic databases

PaxDbiP0AES4.
PRIDEiP0AES4.

2D gel databases

SWISS-2DPAGEP0AES4.

Expressioni

Gene expression databases

GenevestigatoriP0AES4.

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. Can form a 2:2 complex with toxin CcdB in which GyrA is inactive; rejuvenation of GyrA2CcdB2 is effected by CcdA.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-547129,EBI-547129
gyrBP0AES65EBI-547129,EBI-541911
marRP272452EBI-547129,EBI-6409744

Protein-protein interaction databases

DIPiDIP-36179N.
IntActiP0AES4. 51 interactions.
MINTiMINT-201682.
STRINGi511145.b2231.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni31 – 333
Turni37 – 393
Helixi43 – 5412
Beta strandi59 – 613
Helixi66 – 7611
Helixi82 – 9110
Turni95 – 973
Beta strandi102 – 1076
Turni120 – 1223
Beta strandi124 – 1274
Helixi131 – 1344
Turni136 – 1416
Beta strandi145 – 1473
Beta strandi151 – 1588
Helixi165 – 1695
Beta strandi171 – 1733
Beta strandi180 – 1823
Helixi187 – 19913
Helixi205 – 2084
Turni209 – 2113
Helixi227 – 2359
Beta strandi236 – 2438
Beta strandi245 – 2495
Beta strandi258 – 2636
Helixi270 – 28112
Turni282 – 2843
Beta strandi292 – 2943
Beta strandi298 – 3003
Beta strandi303 – 3053
Helixi314 – 32310
Beta strandi327 – 3337
Beta strandi335 – 3384
Beta strandi341 – 3444
Helixi347 – 38842
Helixi390 – 39910
Beta strandi400 – 4023
Helixi403 – 41210
Helixi419 – 4213
Beta strandi441 – 4499
Helixi452 – 4598
Helixi463 – 4664
Helixi468 – 49326
Helixi495 – 51319
Beta strandi519 – 5213
Beta strandi538 – 5447
Beta strandi547 – 5537
Beta strandi578 – 5858
Beta strandi589 – 5946
Beta strandi597 – 6037
Helixi604 – 6063
Beta strandi612 – 6143
Helixi619 – 6213
Beta strandi631 – 6388
Beta strandi645 – 6506
Beta strandi653 – 6597
Helixi660 – 6634
Beta strandi671 – 6744
Beta strandi682 – 6887
Beta strandi693 – 6986
Beta strandi701 – 7077
Helixi708 – 7103
Beta strandi732 – 7365
Beta strandi743 – 7486
Beta strandi751 – 7566
Helixi758 – 7603
Beta strandi771 – 7744
Turni778 – 7803
Beta strandi782 – 7898
Beta strandi794 – 8018
Beta strandi804 – 8085
Helixi809 – 8113
Beta strandi833 – 8386

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AB4X-ray2.80A30-522[»]
1X75X-ray2.80A/B363-494[»]
1ZI0X-ray2.60A/B535-841[»]
2Y3PX-ray2.62A/B2-523[»]
3NUHX-ray3.10A1-525[»]
4ELYX-ray1.93A/B363-497[»]
ProteinModelPortaliP0AES4.
SMRiP0AES4. Positions 13-522, 535-841.

Miscellaneous databases

EvolutionaryTraceiP0AES4.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0188.
HOGENOMiHOG000076278.
KOiK02469.
OMAiQTVFGIN.
OrthoDBiEOG661H5V.
PhylomeDBiP0AES4.

Family and domain databases

Gene3Di1.10.268.10. 1 hit.
3.30.1360.40. 1 hit.
3.90.199.10. 1 hit.
HAMAPiMF_01897. GyrA.
InterProiIPR024946. Arg_repress_C-like.
IPR005743. GyrA.
IPR006691. GyrA/parC_pinwhl.
IPR002205. Topo_IIA_A/C.
IPR013758. Topo_IIA_A/C_ab.
IPR013757. Topo_IIA_A_a.
IPR013760. Topo_IIA_like_dom.
[Graphical view]
PfamiPF03989. DNA_gyraseA_C. 6 hits.
PF00521. DNA_topoisoIV. 1 hit.
[Graphical view]
SMARTiSM00434. TOP4c. 1 hit.
[Graphical view]
SUPFAMiSSF56719. SSF56719. 1 hit.
TIGRFAMsiTIGR01063. gyrA. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P0AES4-1 [UniParc]FASTAAdd to Basket

« Hide

MSDLAREITP VNIEEELKSS YLDYAMSVIV GRALPDVRDG LKPVHRRVLY    50
AMNVLGNDWN KAYKKSARVV GDVIGKYHPH GDSAVYDTIV RMAQPFSLRY 100
MLVDGQGNFG SIDGDSAAAM RYTEIRLAKI AHELMADLEK ETVDFVDNYD 150
GTEKIPDVMP TKIPNLLVNG SSGIAVGMAT NIPPHNLTEV INGCLAYIDD 200
EDISIEGLME HIPGPDFPTA AIINGRRGIE EAYRTGRGKV YIRARAEVEV 250
DAKTGRETII VHEIPYQVNK ARLIEKIAEL VKEKRVEGIS ALRDESDKDG 300
MRIVIEVKRD AVGEVVLNNL YSQTQLQVSF GINMVALHHG QPKIMNLKDI 350
IAAFVRHRRE VVTRRTIFEL RKARDRAHIL EALAVALANI DPIIELIRHA 400
PTPAEAKTAL VANPWQLGNV AAMLERAGDD AARPEWLEPE FGVRDGLYYL 450
TEQQAQAILD LRLQKLTGLE HEKLLDEYKE LLDQIAELLR ILGSADRLME 500
VIREELELVR EQFGDKRRTE ITANSADINL EDLITQEDVV VTLSHQGYVK 550
YQPLSEYEAQ RRGGKGKSAA RIKEEDFIDR LLVANTHDHI LCFSSRGRVY 600
SMKVYQLPEA TRGARGRPIV NLLPLEQDER ITAILPVTEF EEGVKVFMAT 650
ANGTVKKTVL TEFNRLRTAG KVAIKLVDGD ELIGVDLTSG EDEVMLFSAE 700
GKVVRFKESS VRAMGCNTTG VRGIRLGEGD KVVSLIVPRG DGAILTATQN 750
GYGKRTAVAE YPTKSRATKG VISIKVTERN GLVVGAVQVD DCDQIMMITD 800
AGTLVRTRVS EISIVGRNTQ GVILIRTAED ENVVGLQRVA EPVDEEDLDT 850
IDGSAAEGDD EIAPEVDVDD EPEEE 875
Length:875
Mass (Da):96,964
Last modified:December 20, 2005 - v1
Checksum:i3FD5BD52A5969069
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti67 – 671A → S in PPA-10; quinolone-resistant.
Natural varianti81 – 811G → C in NAL-97; quinolone-resistant.
Natural varianti83 – 831S → L in NAL-51, NAL-112, NAL-118 and NAL-119; quinolone-resistant.
Natural varianti83 – 831S → W in PPA-18 and strain 227; quinolone-resistant.
Natural varianti84 – 841A → P in PPA-05; quinolone-resistant.
Natural varianti87 – 871D → N in NAL-113 and KL-16; quinolone-resistant.
Natural varianti87 – 871D → V in strain: 202; quinolone-resistant.
Natural varianti106 – 1061Q → H in NAL-89; quinolone-resistant.
Natural varianti678 – 6781D → E in strain: 227.
Natural varianti798 – 7981I → IMMI in KL-16; quinolone-resistant.
Natural varianti828 – 8281A → S in strain: 227.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X06373 Genomic DNA. Translation: CAA29676.1.
X06744 Genomic DNA. Translation: CAA29919.1.
M15631 Genomic DNA. Translation: AAA23948.1.
U00096 Genomic DNA. Translation: AAC75291.1.
AP009048 Genomic DNA. Translation: BAA16048.1.
Y00544 Genomic DNA. Translation: CAA68611.1.
PIRiS02340. ITECAP.
RefSeqiNP_416734.1. NC_000913.3.
YP_490470.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75291; AAC75291; b2231.
BAA16048; BAA16048; BAA16048.
GeneIDi12933138.
946614.
KEGGiecj:Y75_p2193.
eco:b2231.
PATRICi32119821. VBIEscCol129921_2320.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X06373 Genomic DNA. Translation: CAA29676.1 .
X06744 Genomic DNA. Translation: CAA29919.1 .
M15631 Genomic DNA. Translation: AAA23948.1 .
U00096 Genomic DNA. Translation: AAC75291.1 .
AP009048 Genomic DNA. Translation: BAA16048.1 .
Y00544 Genomic DNA. Translation: CAA68611.1 .
PIRi S02340. ITECAP.
RefSeqi NP_416734.1. NC_000913.3.
YP_490470.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AB4 X-ray 2.80 A 30-522 [» ]
1X75 X-ray 2.80 A/B 363-494 [» ]
1ZI0 X-ray 2.60 A/B 535-841 [» ]
2Y3P X-ray 2.62 A/B 2-523 [» ]
3NUH X-ray 3.10 A 1-525 [» ]
4ELY X-ray 1.93 A/B 363-497 [» ]
ProteinModelPortali P0AES4.
SMRi P0AES4. Positions 13-522, 535-841.
ModBasei Search...

Protein-protein interaction databases

DIPi DIP-36179N.
IntActi P0AES4. 51 interactions.
MINTi MINT-201682.
STRINGi 511145.b2231.

Chemistry

BindingDBi P0AES4.
ChEMBLi CHEMBL1858.

2D gel databases

SWISS-2DPAGE P0AES4.

Proteomic databases

PaxDbi P0AES4.
PRIDEi P0AES4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC75291 ; AAC75291 ; b2231 .
BAA16048 ; BAA16048 ; BAA16048 .
GeneIDi 12933138.
946614.
KEGGi ecj:Y75_p2193.
eco:b2231.
PATRICi 32119821. VBIEscCol129921_2320.

Organism-specific databases

EchoBASEi EB0418.
EcoGenei EG10423. gyrA.

Phylogenomic databases

eggNOGi COG0188.
HOGENOMi HOG000076278.
KOi K02469.
OMAi QTVFGIN.
OrthoDBi EOG661H5V.
PhylomeDBi P0AES4.

Enzyme and pathway databases

BioCyci EcoCyc:EG10423-MONOMER.
ECOL316407:JW2225-MONOMER.
MetaCyc:EG10423-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0AES4.
PROi P0AES4.

Gene expression databases

Genevestigatori P0AES4.

Family and domain databases

Gene3Di 1.10.268.10. 1 hit.
3.30.1360.40. 1 hit.
3.90.199.10. 1 hit.
HAMAPi MF_01897. GyrA.
InterProi IPR024946. Arg_repress_C-like.
IPR005743. GyrA.
IPR006691. GyrA/parC_pinwhl.
IPR002205. Topo_IIA_A/C.
IPR013758. Topo_IIA_A/C_ab.
IPR013757. Topo_IIA_A_a.
IPR013760. Topo_IIA_like_dom.
[Graphical view ]
Pfami PF03989. DNA_gyraseA_C. 6 hits.
PF00521. DNA_topoisoIV. 1 hit.
[Graphical view ]
SMARTi SM00434. TOP4c. 1 hit.
[Graphical view ]
SUPFAMi SSF56719. SSF56719. 1 hit.
TIGRFAMsi TIGR01063. gyrA. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and sequencing of the Escherichia coli gyrA gene coding for the A subunit of DNA gyrase."
    Swanberg S.L., Wang J.C.
    J. Mol. Biol. 197:729-736(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Quinolone-resistant mutations of the gyrA gene of Escherichia coli."
    Yoshida H., Kojima T., Yamagishi J., Nakamura S.
    Mol. Gen. Genet. 211:1-7(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 / KL16.
  3. "The parD- mutant of Escherichia coli also carries a gyrAam mutation. The complete sequence of gyrA."
    Hussain K., Elliott E.J., Salmond G.P.C.
    Mol. Microbiol. 1:259-273(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: OV6.
  4. "Cloning and characterization of a DNA gyrase A gene from Escherichia coli that confers clinical resistance to 4-quinolones."
    Cullen M.E., Wyke A.W., Kuroda R., Fisher L.M.
    Antimicrob. Agents Chemother. 33:886-894(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 227.
  5. "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
    Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T.
    , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
    DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  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. "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 1-88, PARTIAL PROTEIN SEQUENCE.
  9. "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: ACTIVE SITE TYR-122.
  10. "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.
  11. "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, MUTAGENESIS OF ARG-32; ARG-47; HIS-78 AND HIS-80.
  12. "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: CATALYTIC ACTIVITY, FUNCTION, COFACTOR, SUBUNIT.
  13. "A superhelical spiral in the Escherichia coli DNA gyrase A C-terminal domain imparts unidirectional supercoiling bias."
    Ruthenburg A.J., Graybosch D.M., Huetsch J.C., Verdine G.L.
    J. Biol. Chem. 280:26177-26184(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 535-841.
  14. "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: X-RAY CRYSTALLOGRAPHY (2.62 ANGSTROMS) OF 2-523 IN COMPLEX WITH ANTIBIOTIC SIMOCYCLINONE D8, CATALYTIC ACTIVITY, SUBUNIT, FUNCTION.
  15. "Quinolone resistance-determining region in the DNA gyrase gyrA gene of Escherichia coli."
    Yoshida H., Bogaki M., Nakamura M., Nakamura S.
    Antimicrob. Agents Chemother. 34:1271-1272(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS QUINOLONE-RESISTANT.
  16. "4-quinolone resistance mutations in the DNA gyrase of Escherichia coli clinical isolates identified by using the polymerase chain reaction."
    Oram M., Fisher L.M.
    Antimicrob. Agents Chemother. 35:387-389(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS QUINOLONE-RESISTANT.
  17. "Novel quinolone resistance mutations of the Escherichia coli DNA gyrase A protein: enzymatic analysis of the mutant proteins."
    Hallett P., Maxwell A.
    Antimicrob. Agents Chemother. 35:335-340(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF SER-83 AND GLN-106.
    Strain: K12.
  18. "Cell killing by the F plasmid CcdB protein involves poisoning of DNA-topoisomerase II complexes."
    Bernard P., Couturier M.
    J. Mol. Biol. 226:735-745(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: INHIBITION BY TOXIN PROTEIN CCDB, MUTAGENESIS OF ARG-462.
    Strain: K12.
  19. "The F plasmid CcdB protein induces efficient ATP-dependent DNA cleavage by gyrase."
    Bernard P., Kezdy K.E., Van Melderen L., Steyaert J., Wyns L., Pato M.L., Higgins P.N., Couturier M.
    J. Mol. Biol. 234:534-541(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ARG-462.
  20. "Partner switching mechanisms in inactivation and rejuvenation of Escherichia coli DNA gyrase by F plasmid proteins LetD (CcdB) and LetA (CcdA)."
    Maki S., Takiguchi S., Horiuchi T., Sekimizu K., Miki T.
    J. Mol. Biol. 256:473-482(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INHIBITION BY TOXIN PROTEIN CCDB, REJUVENATION BY CCDA, SUBUNIT.
  21. "Crystal structure of the breakage-reunion domain of DNA gyrase."
    Cabral J.H., Jackson A.P., Smith C.V., Shikotra N., Maxwell A., Liddington R.C.
    Nature 388:903-906(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 30-522, CATALYTIC ACTIVITY.
  22. "Molecular basis of gyrase poisoning by the addiction toxin CcdB."
    Dao-Thi M.H., Van Melderen L., De Genst E., Afif H., Buts L., Wyns L., Loris R.
    J. Mol. Biol. 348:1091-1102(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 363-494 IN COMPLEX WITH CCBD.

Entry informationi

Entry nameiGYRA_ECOLI
AccessioniPrimary (citable) accession number: P0AES4
Secondary accession number(s): P09097
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: September 3, 2014
This is version 89 of the entry and version 1 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. This enzyme-DNA intermediate is the target of a number of topoisomerase poisons, including toxin CcdB.

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

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