DNA gyrase subunit A

Details

Name
DNA gyrase subunit A
Synonyms
  • 5.99.1.3
  • hisW
  • nalA
  • parD
Gene Name
gyrA
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0021233|DNA gyrase subunit A
MSDLAREITPVNIEEELKSSYLDYAMSVIVGRALPDVRDGLKPVHRRVLYAMNVLGNDWN
KAYKKSARVVGDVIGKYHPHGDSAVYDTIVRMAQPFSLRYMLVDGQGNFGSIDGDSAAAM
RYTEIRLAKIAHELMADLEKETVDFVDNYDGTEKIPDVMPTKIPNLLVNGSSGIAVGMAT
NIPPHNLTEVINGCLAYIDDEDISIEGLMEHIPGPDFPTAAIINGRRGIEEAYRTGRGKV
YIRARAEVEVDAKTGRETIIVHEIPYQVNKARLIEKIAELVKEKRVEGISALRDESDKDG
MRIVIEVKRDAVGEVVLNNLYSQTQLQVSFGINMVALHHGQPKIMNLKDIIAAFVRHRRE
VVTRRTIFELRKARDRAHILEALAVALANIDPIIELIRHAPTPAEAKTALVANPWQLGNV
AAMLERAGDDAARPEWLEPEFGVRDGLYYLTEQQAQAILDLRLQKLTGLEHEKLLDEYKE
LLDQIAELLRILGSADRLMEVIREELELVREQFGDKRRTEITANSADINLEDLITQEDVV
VTLSHQGYVKYQPLSEYEAQRRGGKGKSAARIKEEDFIDRLLVANTHDHILCFSSRGRVY
SMKVYQLPEATRGARGRPIVNLLPLEQDERITAILPVTEFEEGVKVFMATANGTVKKTVL
TEFNRLRTAGKVAIKLVDGDELIGVDLTSGEDEVMLFSAEGKVVRFKESSVRAMGCNTTG
VRGIRLGEGDKVVSLIVPRGDGAILTATQNGYGKRTAVAEYPTKSRATKGVISIKVTERN
GLVVGAVQVDDCDQIMMITDAGTLVRTRVSEISIVGRNTQGVILIRTAEDENVVGLQRVA
EPVDEEDLDTIDGSAAEGDDEIAPEVDVDDEPEEE
Number of residues
875
Molecular Weight
96962.63
Theoretical pI
Not Available
GO Classification
Functions
ATP binding / DNA binding / DNA topoisomerase type II (ATP-hydrolyzing) activity / DNA-dependent ATPase activity / identical protein binding
Processes
DNA topological change / DNA-dependent DNA replication / response to antibiotic / response to drug / transcription, DNA-templated
Components
chromosome / cytoplasm / cytosol / membrane
General Function
Identical protein binding
Specific Function
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.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0021234|DNA gyrase subunit A (gyrA)
ATGAGCGACCTTGCGAGAGAAATTACACCGGTCAACATTGAGGAAGAGCTGAAGAGCTCC
TATCTGGATTATGCGATGTCGGTCATTGTTGGCCGTGCGCTGCCAGATGTCCGAGATGGC
CTGAAGCCGGTACACCGTCGCGTACTTTACGCCATGAACGTACTAGGCAATGACTGGAAC
AAAGCCTATAAAAAATCTGCCCGTGTCGTTGGTGACGTAATCGGTAAATACCATCCCCAT
GGTGACTCGGCGGTCTATGACACGATCGTCCGCATGGCGCAGCCATTCTCGCTGCGTTAT
ATGCTGGTAGACGGTCAGGGTAACTTCGGTTCTATCGACGGCGACTCTGCGGCGGCAATG
CGTTATACGGAAATCCGTCTGGCGAAAATTGCCCATGAACTGATGGCCGATCTCGAAAAA
GAGACGGTCGATTTCGTTGATAACTATGACGGCACGGAAAAAATTCCGGACGTCATGCCA
ACCAAAATTCCTAACCTGCTGGTGAACGGTTCTTCCGGTATCGCCGTAGGTATGGCAACC
AACATCCCGCCGCACAACCTGACGGAAGTCATCAACGGTTGTCTGGCGTATATTGATGAT
GAAGACATCAGCATTGAAGGGCTGATGGAACACATCCCGGGGCCGGACTTCCCGACGGCG
GCAATCATTAACGGTCGTCGCGGTATTGAAGAAGCTTACCGTACCGGTCGCGGCAAGGTG
TATATCCGCGCTCGCGCAGAAGTGGAAGTTGACGCCAAAACCGGTCGTGAAACCATTATC
GTCCACGAAATTCCGTATCAGGTAAACAAAGCGCGCCTGATCGAGAAGATTGCGGAACTG
GTAAAAGAAAAACGCGTGGAAGGCATCAGCGCGCTGCGTGACGAGTCTGACAAAGACGGT
ATGCGCATCGTGATTGAAGTGAAACGCGATGCGGTCGGTGAAGTTGTGCTCAACAACCTC
TACTCCCAGACCCAGTTGCAGGTTTCTTTCGGTATCAACATGGTGGCATTGCACCATGGT
CAGCCGAAGATCATGAACCTGAAAGACATCATCGCGGCGTTTGTTCGTCACCGCCGTGAA
GTGGTGACCCGTCGTACTATTTTCGAACTGCGTAAAGCTCGCGATCGTGCTCATATCCTT
GAAGCATTAGCCGTGGCGCTGGCGAACATCGACCCGATCATCGAACTGATCCGTCATGCG
CCGACGCCTGCAGAAGCGAAAACTGCGCTGGTTGCTAATCCGTGGCAGCTGGGCAACGTT
GCCGCGATGCTCGAACGTGCTGGCGACGATGCTGCGCGTCCGGAATGGCTGGAGCCAGAG
TTCGGCGTGCGTGATGGTCTGTACTACCTGACCGAACAGCAAGCTCAGGCGATTCTGGAT
CTGCGTTTGCAGAAACTGACCGGTCTTGAGCACGAAAAACTGCTCGACGAATACAAAGAG
CTGCTGGATCAGATCGCGGAACTGTTGCGTATTCTTGGTAGCGCCGATCGTCTGATGGAA
GTGATCCGTGAAGAGCTGGAGCTGGTTCGTGAACAGTTCGGTGACAAACGTCGTACTGAA
ATCACCGCCAACAGCGCAGACATCAACCTGGAAGATCTGATCACCCAGGAAGATGTGGTC
GTGACGCTCTCTCACCAGGGCTACGTTAAGTATCAGCCGCTTTCTGAATACGAAGCGCAG
CGTCGTGGCGGGAAAGGTAAATCTGCCGCACGTATTAAAGAAGAAGACTTTATCGACCGA
CTGCTGGTGGCGAACACTCACGACCATATTCTGTGCTTCTCCAGCCGTGGTCGCGTCTAT
TCGATGAAAGTTTATCAGTTGCCGGAAGCCACTCGTGGCGCGCGCGGTCGTCCGATCGTC
AACCTGCTGCCGCTGGAGCAGGACGAACGTATCACTGCGATCCTGCCAGTGACCGAGTTT
GAAGAAGGCGTGAAAGTCTTCATGGCGACCGCTAACGGTACCGTGAAGAAAACTGTCCTC
ACCGAGTTCAACCGTCTGCGTACCGCCGGTAAAGTGGCGATCAAACTGGTTGACGGCGAT
GAGCTGATCGGCGTTGACCTGACCAGCGGCGAAGACGAAGTAATGCTGTTCTCCGCTGAA
GGTAAAGTGGTGCGCTTTAAAGAGTCTTCTGTCCGTGCGATGGGCTGCAACACCACCGGT
GTTCGCGGTATTCGCTTAGGTGAAGGCGATAAAGTCGTCTCTCTGATCGTGCCTCGTGGC
GATGGCGCAATCCTCACCGCAACGCAAAACGGTTACGGTAAACGTACCGCAGTGGCGGAA
TACCCAACCAAGTCGCGTGCGACGAAAGGGGTTATCTCCATCAAGGTTACCGAACGTAAC
GGTTTAGTTGTTGGCGCGGTACAGGTAGATGACTGCGACCAGATCATGATGATCACCGAT
GCCGGTACGCTGGTACGTACTCGCGTTTCGGAAATCAGCATCGTGGGCCGTAACACCCAG
GGCGTGATCCTCATCCGTACTGCGGAAGATGAAAACGTAGTGGGTCTGCAACGTGTTGCT
GAACCGGTTGACGAGGAAGATCTGGATACCATCGACGGCAGTGCCGCGGAAGGGGACGAT
GAAATCGCTCCGGAAGTGGACGTTGACGACGAGCCAGAAGAAGAATAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP0AES4
UniProtKB Entry NameGYRA_ECOLI
General References
  1. Swanberg SL, Wang JC: Cloning and sequencing of the Escherichia coli gyrA gene coding for the A subunit of DNA gyrase. J Mol Biol. 1987 Oct 20;197(4):729-36. [PubMed:2828631]
  2. Yoshida H, Kojima T, Yamagishi J, Nakamura S: Quinolone-resistant mutations of the gyrA gene of Escherichia coli. Mol Gen Genet. 1988 Jan;211(1):1-7. [PubMed:2830458]
  3. Hussain K, Elliott EJ, Salmond GP: The parD- mutant of Escherichia coli also carries a gyrAam mutation. The complete sequence of gyrA. Mol Microbiol. 1987 Nov;1(3):259-73. [PubMed:2834621]
  4. Cullen ME, Wyke AW, Kuroda R, Fisher LM: Cloning and characterization of a DNA gyrase A gene from Escherichia coli that confers clinical resistance to 4-quinolones. Antimicrob Agents Chemother. 1989 Jun;33(6):886-94. [PubMed:2548439]
  5. 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, Horiuchi T, et al.: 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. DNA Res. 1997 Apr 28;4(2):91-113. [PubMed:9205837]
  6. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [PubMed:9278503]
  7. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [PubMed:16738553]
  8. Menzel R, Gellert M: Fusions of the Escherichia coli gyrA and gyrB control regions to the galactokinase gene are inducible by coumermycin treatment. J Bacteriol. 1987 Mar;169(3):1272-8. [PubMed:3029031]
  9. Horowitz DS, Wang JC: Mapping the active site tyrosine of Escherichia coli DNA gyrase. J Biol Chem. 1987 Apr 15;262(11):5339-44. [PubMed:3031051]
  10. VanBogelen RA, Abshire KZ, Moldover B, Olson ER, Neidhardt FC: Escherichia coli proteome analysis using the gene-protein database. Electrophoresis. 1997 Aug;18(8):1243-51. [PubMed:9298644]
  11. Hockings SC, Maxwell A: Identification of four GyrA residues involved in the DNA breakage-reunion reaction of DNA gyrase. J Mol Biol. 2002 Apr 26;318(2):351-9. [PubMed:12051842]
  12. Sissi C, Chemello A, Vazquez E, Mitchenall LA, Maxwell A, Palumbo M: DNA gyrase requires DNA for effective two-site coordination of divalent metal ions: further insight into the mechanism of enzyme action. Biochemistry. 2008 Aug 19;47(33):8538-45. doi: 10.1021/bi800480j. Epub 2008 Jul 22. [PubMed:18642932]
  13. Ruthenburg AJ, Graybosch DM, Huetsch JC, Verdine GL: A superhelical spiral in the Escherichia coli DNA gyrase A C-terminal domain imparts unidirectional supercoiling bias. J Biol Chem. 2005 Jul 15;280(28):26177-84. Epub 2005 May 15. [PubMed:15897198]
  14. Edwards MJ, Flatman RH, Mitchenall LA, Stevenson CE, Le TB, Clarke TA, McKay AR, Fiedler HP, Buttner MJ, Lawson DM, Maxwell A: A crystal structure of the bifunctional antibiotic simocyclinone D8, bound to DNA gyrase. Science. 2009 Dec 4;326(5958):1415-8. doi: 10.1126/science.1179123. [PubMed:19965760]
  15. Yoshida H, Bogaki M, Nakamura M, Nakamura S: Quinolone resistance-determining region in the DNA gyrase gyrA gene of Escherichia coli. Antimicrob Agents Chemother. 1990 Jun;34(6):1271-2. [PubMed:2168148]
  16. Oram M, Fisher LM: 4-Quinolone resistance mutations in the DNA gyrase of Escherichia coli clinical isolates identified by using the polymerase chain reaction. Antimicrob Agents Chemother. 1991 Feb;35(2):387-9. [PubMed:1850972]
  17. Hallett P, Maxwell A: Novel quinolone resistance mutations of the Escherichia coli DNA gyrase A protein: enzymatic analysis of the mutant proteins. Antimicrob Agents Chemother. 1991 Feb;35(2):335-40. [PubMed:1850970]
  18. Bernard P, Couturier M: Cell killing by the F plasmid CcdB protein involves poisoning of DNA-topoisomerase II complexes. J Mol Biol. 1992 Aug 5;226(3):735-45. [PubMed:1324324]
  19. Bernard P, Kezdy KE, Van Melderen L, Steyaert J, Wyns L, Pato ML, Higgins PN, Couturier M: The F plasmid CcdB protein induces efficient ATP-dependent DNA cleavage by gyrase. J Mol Biol. 1993 Dec 5;234(3):534-41. [PubMed:8254658]
  20. Maki S, Takiguchi S, Horiuchi T, Sekimizu K, Miki T: Partner switching mechanisms in inactivation and rejuvenation of Escherichia coli DNA gyrase by F plasmid proteins LetD (CcdB) and LetA (CcdA). J Mol Biol. 1996 Mar 1;256(3):473-82. [PubMed:8604132]
  21. Morais Cabral JH, Jackson AP, Smith CV, Shikotra N, Maxwell A, Liddington RC: Crystal structure of the breakage-reunion domain of DNA gyrase. Nature. 1997 Aug 28;388(6645):903-6. [PubMed:9278055]
  22. Dao-Thi MH, Van Melderen L, De Genst E, Afif H, Buts L, Wyns L, Loris R: Molecular basis of gyrase poisoning by the addiction toxin CcdB. J Mol Biol. 2005 May 20;348(5):1091-102. Epub 2005 Apr 7. [PubMed:15854646]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB00537Ciprofloxacinapproved, investigationalunknownDetails
DB11943Delafloxacinapproved, investigationalyesinhibitorDetails