gyrA:Gene Product(s)
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Nomenclature
See Help:Product_nomenclature for help entering or editing information in this section of EcoliWiki.
Standard name |
GyrA |
---|---|
Synonyms |
DNA gyrase (type II topoisomerase), subunit A[1], B2231[2][1], ParD[2][1], NorA[2][1], NfxA[2][1], NalA[2][1], HisW[2][1], GyrA[2][1] , ECK2223, hisW, JW2225, nalA, nfxA, norA, parD, b2231 |
Product description |
Component of DNA gyrase[3] DNA gyrase, subunit A; nalidixic acid resistance; cold shock regulon[4] |
EC number (for enzymes) | |
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Notes
Function
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Gene Ontology
See Help:Gene_ontology for help entering or editing GO terms and GO annotations in EcoliWiki.
Qualifier | GO ID | GO term name | Reference | Evidence Code | with/from | Aspect | Notes | Status |
---|---|---|---|---|---|---|---|---|
GO:0042493 |
response to drug |
IMP: Inferred from Mutant Phenotype |
P |
complete | ||||
GO:0000166 |
nucleotide binding |
GOA:spkw |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0003918 |
DNA topoisomerase (ATP-hydrolyzing) activity |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0003918 |
DNA topoisomerase (ATP-hydrolyzing) activity |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0003918 |
DNA topoisomerase (ATP-hydrolyzing) activity |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0003918 |
DNA topoisomerase (ATP-hydrolyzing) activity |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0003918 |
DNA topoisomerase (ATP-hydrolyzing) activity |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0003918 |
DNA topoisomerase (ATP-hydrolyzing) activity |
IDA: Inferred from Direct Assay |
F |
With GyrB Purified E. coli gyrase was shown to induce cleavage and supercoiling in ColE1 DNA in the presence of ATP, but not after the addition of novobiocin or coumermycin A1 (Figure 2). Supercoiling of DNA was monitored by agarose gel electrophoresis (Figure 2A), while the hydrolysis of ATP was measured by following the release of 32-Pi measured by thin layer chromatography (Figure 2B). |
complete | |||
GO:0003677 |
DNA binding |
IDA: Inferred from Direct Assay |
F |
E. coli gyrase incubated with radiolabeled ColE1 DNA and passed over nitrocellulose filters. The complexes were retained on the filters and radioactivity of the filters was measured and reported in Figure 1. |
complete | |||
GO:0003918 |
DNA topoisomerase (ATP-hydrolyzing) activity |
GOA:spec |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0042493 |
response to drug |
IMP: Inferred from Mutant Phenotype |
P |
Oxolinic acid (Quinolone) |
complete | |||
GO:0005524 |
ATP binding |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0005524 |
ATP binding |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0042493 |
response to drug |
IMP: Inferred from Mutant Phenotype |
P |
Naladixic Acid (Quinolone) |
complete | |||
GO:0003677 |
DNA binding |
IDA: Inferred from Direct Assay |
F |
The C-terminal domain of GyrA (572-857aa) was shown to bind and retard the movement of a 147bp fragment of ColE1 DNA through a 5% polyacrylamide gel (Figure 2). |
complete | |||
GO:0006351 |
transcription, DNA-dependent |
IDA: Inferred from Direct Assay |
P |
E. coli gyrase consists of the gene products of gyrA and gyrB genes (Figures 2 & 7). |
complete | |||
GO:0005524 |
ATP binding |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0008094 |
DNA-dependent ATPase activity |
IDA: Inferred from Direct Assay |
F |
GyrA and DNA (bound to GyrA) are required for ATPase activity of GyrB (Figure 1). |
complete | |||
GO:0005524 |
ATP binding |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0006265 |
DNA topological change |
IMP: Inferred from Mutant Phenotype |
P |
Nucleoids from E. coli cells containing DNA labeled with [methyl-3H]thymidine were isolated and separated using an ethidium bromide-containing sucrose density gradient. The sedimentation profiles were reported for gyrA and gyrB temperature-sensitive mutants at the permissive and non-permissive temperatures (Figure 1 & 2). The ethidium bromide concentration is proportional to superhelical density, meaning that less supercoiled DNA from a gyrase mutant grown at the non-permissive temperature requires a lower concentration of ethidium bromide. |
complete | |||
GO:0006351 |
transcription, DNA-dependent |
IMP: Inferred from Mutant Phenotype |
P |
The authors used 3 conditions (treatment with either a quinolone or coumarin anitbiotic or growth of a gyrAts mutant at non-permissive temperature) to alter negative supercoiling of DNA and measured the changes in gene expression by microarray analysis. More than 300 SSGs (supercoiling sensitive genes) were identified that responded rapidly to the experimental conditions. |
complete | |||
GO:0005524 |
ATP binding |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0005737 |
cytoplasm |
IDA: Inferred from Direct Assay |
C |
Immunogold labeling of cells with anti-GyrA antibodies indicated the presence of GyrA in the cytoplasm of E. coli. |
complete | |||
GO:0005524 |
ATP binding |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0005524 |
ATP binding |
GOA:spkw |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0005694 |
chromosome |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
C |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0005694 |
chromosome |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
C |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0005694 |
chromosome |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
C |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0005694 |
chromosome |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
C |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0005694 |
chromosome |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
C |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0005694 |
chromosome |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
C |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0005737 |
cytoplasm |
IDA: Inferred from Direct Assay |
C |
Seeded from EcoCyc (v14.0) |
complete | |||
GO:0006261 |
DNA-dependent DNA replication |
IMP: Inferred from Mutant Phenotype |
P |
Seeded from EcoCyc (v14.0) |
complete | |||
GO:0006265 |
DNA topological change |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
P |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0006265 |
DNA topological change |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
P |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0006265 |
DNA topological change |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
P |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0006265 |
DNA topological change |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
P |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0006265 |
DNA topological change |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
P |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0006265 |
DNA topological change |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
P |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0009330 |
DNA topoisomerase complex (ATP-hydrolyzing) |
IDA: Inferred from Direct Assay |
C |
Seeded from EcoCyc (v14.0) |
complete | |||
GO:0016020 |
membrane |
IDA: Inferred from Direct Assay |
C |
Seeded from EcoCyc (v14.0) |
complete | |||
GO:0046677 |
response to antibiotic |
GOA:spkw |
IEA: Inferred from Electronic Annotation |
P |
Seeded from EcoCyc (v14.0) |
complete | ||
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Interactions See Help:Product_interactions for help entering or editing information about gene product interactions in this section of EcoliWiki.
Partner Type | Partner | Notes | References | Evidence |
---|---|---|---|---|
Protein |
Subunits of DNA gyrase |
could be indirect |
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Protein |
ycgC |
Experiment(s):EBI-884206 | ||
Protein |
aceF |
Experiment(s):EBI-884206 | ||
Protein |
add |
Experiment(s):EBI-884206 | ||
Protein |
clpA |
Experiment(s):EBI-884206 | ||
Protein |
dnaJ |
Experiment(s):EBI-884206 | ||
Protein |
dnaK |
Experiment(s):EBI-884206 | ||
Protein |
ffh |
Experiment(s):EBI-884206 | ||
Protein |
ftsZ |
Experiment(s):EBI-884206 | ||
Protein |
glyS |
Experiment(s):EBI-884206 | ||
Protein |
zraS |
Experiment(s):EBI-884206 | ||
Protein |
lpdA |
Experiment(s):EBI-884206 | ||
Protein |
malK |
Experiment(s):EBI-884206 | ||
Protein |
metK |
Experiment(s):EBI-884206 | ||
Protein |
pstB |
Experiment(s):EBI-884206 | ||
Protein |
recA |
Experiment(s):EBI-884206 | ||
Protein |
rho |
Experiment(s):EBI-884206 | ||
Protein |
rpsB |
Experiment(s):EBI-884206 | ||
Protein |
tufA |
Experiment(s):EBI-884206, EBI-891237 | ||
Protein |
yjfZ |
Experiment(s):EBI-884206 | ||
Protein |
argS |
Experiment(s):EBI-1142253 | ||
Protein |
idnO |
Experiment(s):EBI-1142253 | ||
Protein |
rpsB |
Experiment(s):EBI-1142253 | ||
Protein |
yfaS |
Experiment(s):EBI-1142253 | ||
Protein |
aspC |
Experiment(s):EBI-1142253 | ||
Protein |
nrdI |
Experiment(s):EBI-1142253 | ||
Protein |
rtcB |
Experiment(s):EBI-1142253 | ||
Protein |
rho |
MALDI(Z-score):18.636092 | ||
Protein |
clpA |
MALDI(Z-score):19.599720 | ||
Protein |
pstB |
MALDI(Z-score):35.274106 | ||
Protein |
recA |
MALDI(Z-score):29.421963 | ||
Protein |
metK |
MALDI(Z-score):37.360726 | ||
Protein |
add |
MALDI(Z-score):32.777259 | ||
Protein |
dnaJ |
MALDI(Z-score):34.861527 | ||
Protein |
tufB |
MALDI(Z-score):22.155359 | ||
Protein |
mreB |
MALDI(Z-score):36.098785 | ||
Protein |
The binding of gyrase to DNA: analysis by retention by nitrocellulose filters. Higgins & Cozzarelli (1982)[7] |
|||
Small Molecule |
Naladixic Acid |
Studies on the mechanism of action of nalidixic acid. Bourguignon et al. (1973) [9] |
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Small Molecule |
Oxolinic acid |
Replication of Escherichia coli DNA in vitro: inhibition by oxolinic acid. Staudenbauer (1976) [8] |
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DNA |
DNA |
The C-terminal domain of GyrA is sufficient to bind DNA (residues 572-875). |
The C-terminal domain of the Escherichia coli DNA gyrase A subunit is a DNA-binding protein. Reece & Maxwell (1991) [10] |
|
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Notes
Localization
See Help:Product_localization for how to add or edit information in this section of EcoliWiki.
Compartment | Description | Evidence | Reference/Source | Notes |
---|---|---|---|---|
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Notes
Structure and Physical Properties
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Physical Properties
See Help:Product_physical_properties for help entering or editing information about the physical properties of this gene product.
Name | |
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Sequence |
MSDLAREITP VNIEEELKSS YLDYAMSVIV GRALPDVRDG LKPVHRRVLY AMNVLGNDWN KAYKKSARVV GDVIGKYHPH GDSAVYDTIV RMAQPFSLRY MLVDGQGNFG SIDGDSAAAM RYTEIRLAKI AHELMADLEK ETVDFVDNYD GTEKIPDVMP TKIPNLLVNG SSGIAVGMAT NIPPHNLTEV INGCLAYIDD EDISIEGLME HIPGPDFPTA AIINGRRGIE EAYRTGRGKV YIRARAEVEV DAKTGRETII VHEIPYQVNK ARLIEKIAEL VKEKRVEGIS ALRDESDKDG MRIVIEVKRD AVGEVVLNNL YSQTQLQVSF GINMVALHHG QPKIMNLKDI IAAFVRHRRE VVTRRTIFEL RKARDRAHIL EALAVALANI DPIIELIRHA PTPAEAKTAL VANPWQLGNV AAMLERAGDD AARPEWLEPE FGVRDGLYYL TEQQAQAILD LRLQKLTGLE HEKLLDEYKE LLDQIAELLR ILGSADRLME VIREELELVR EQFGDKRRTE ITANSADINL EDLITQEDVV VTLSHQGYVK YQPLSEYEAQ RRGGKGKSAA RIKEEDFIDR LLVANTHDHI LCFSSRGRVY SMKVYQLPEA TRGARGRPIV NLLPLEQDER ITAILPVTEF EEGVKVFMAT ANGTVKKTVL TEFNRLRTAG KVAIKLVDGD ELIGVDLTSG EDEVMLFSAE GKVVRFKESS VRAMGCNTTG VRGIRLGEGD KVVSLIVPRG DGAILTATQN GYGKRTAVAE YPTKSRATKG VISIKVTERN GLVVGAVQVD DCDQIMMITD AGTLVRTRVS EISIVGRNTQ GVILIRTAED ENVVGLQRVA EPVDEEDLDT IDGSAAEGDD EIAPEVDVDD EPEEE |
Length |
875 |
Mol. Wt |
96.964 kDa |
pI |
5.0 (calculated) |
Extinction coefficient |
52,260 - 52,760 (calc based on 24 Y, 3 W, and 4 C residues) |
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Domains/Motifs/Modification Sites
See Help:Product_domains_motifs for help entering or editing information in this section of EcoliWiki.
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Structure
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Structure figures<protect> | ||||||
Notes
Gene Product Resources
See Help:Product_resources for help with entering or editing information in this section of EcoliWiki.
Resource type | Source | Notes/Reference |
---|---|---|
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Notes
Accessions in Other Databases
See Help:Gene_accessions for help with entering information into the Gene Accessions table.
Database | Accession | Notes |
---|---|---|
Escherichia coli str. K-12 substr. MG1655 | ||
Escherichia coli str. K-12 substr. MG1655 | ||
Escherichia coli str. K-12 substr. MG1655 | ||
Escherichia coli str. K-12 substr. MG1655 | ||
Escherichia coli str. K-12 substr. MG1655 | ||
Escherichia coli str. K-12 substr. MG1655 | ||
Escherichia coli str. K-12 substr. MG1655 | ||
Escherichia coli str. K-12 substr. MG1655 | ||
Escherichia coli str. K-12 substr. MG1655 | ||
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Notes
Links
Name | URL | Comments |
---|---|---|
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References
See Help:References for how to manage references in EcoliWiki.
- ↑ 1.0 1.1 1.2 1.3 1.4 1.5 1.6 1.7 1.8 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
- ↑ 2.0 2.1 2.2 2.3 2.4 2.5 2.6 2.7 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ 3.0 3.1 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
- ↑ Chao, L & Tillman, DM (1982) Enhanced resistance to nitrosoguanidine killing and mutagenesis in a DNA gyrase mutant of Escherichia coli. J. Bacteriol. 151 764-70 PubMed
- ↑ Sugino, A et al. (1978) Energy coupling in DNA gyrase and the mechanism of action of novobiocin. Proc. Natl. Acad. Sci. U.S.A. 75 4838-42 PubMed
- ↑ 7.0 7.1 Higgins, NP & Cozzarelli, NR (1982) The binding of gyrase to DNA: analysis by retention by nitrocellulose filters. Nucleic Acids Res. 10 6833-47 PubMed
- ↑ 8.0 8.1 Staudenbauer, WL (1976) Replication of Escherichia coli DNA in vitro: inhibition by oxolinic acid. Eur. J. Biochem. 62 491-7 PubMed
- ↑ 9.0 9.1 Bourguignon, GJ et al. (1973) Studies on the mechanism of action of nalidixic acid. Antimicrob. Agents Chemother. 4 479-86 PubMed
- ↑ 10.0 10.1 Reece, RJ & Maxwell, A (1991) The C-terminal domain of the Escherichia coli DNA gyrase A subunit is a DNA-binding protein. Nucleic Acids Res. 19 1399-405 PubMed
- ↑ 11.0 11.1 11.2 Higgins, NP et al. (1978) Purification of subunits of Escherichia coli DNA gyrase and reconstitution of enzymatic activity. Proc. Natl. Acad. Sci. U.S.A. 75 1773-7 PubMed
- ↑ Maxwell, A & Gellert, M (1984) The DNA dependence of the ATPase activity of DNA gyrase. J. Biol. Chem. 259 14472-80 PubMed
- ↑ Steck, TR et al. (1984) DNA supercoiling in gyrase mutants. J. Bacteriol. 158 397-403 PubMed
- ↑ Peter, BJ et al. (2004) Genomic transcriptional response to loss of chromosomal supercoiling in Escherichia coli. Genome Biol. 5 R87 PubMed
- ↑ 15.0 15.1 Thornton, M et al. (1994) Immunogold localization of GyrA and GyrB proteins in Escherichia coli. Microbiology (Reading, Engl.) 140 ( Pt 9) 2371-82 PubMed
- ↑ Kreuzer, KN & Cozzarelli, NR (1979) Escherichia coli mutants thermosensitive for deoxyribonucleic acid gyrase subunit A: effects on deoxyribonucleic acid replication, transcription, and bacteriophage growth. J. Bacteriol. 140 424-35 PubMed
- ↑ Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed
- ↑ 18.00 18.01 18.02 18.03 18.04 18.05 18.06 18.07 18.08 18.09 18.10 18.11 18.12 18.13 18.14 18.15 18.16 18.17 18.18 Butland, G et al. (2005) Interaction network containing conserved and essential protein complexes in Escherichia coli. Nature 433 531-7 PubMed
- ↑ 19.0 19.1 19.2 19.3 19.4 19.5 19.6 Arifuzzaman, M et al. (2006) Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res. 16 686-91 PubMed
- ↑ 20.0 20.1 20.2 20.3 20.4 20.5 20.6 20.7 20.8 Hu, P et al. (2009) Global functional atlas of Escherichia coli encompassing previously uncharacterized proteins. PLoS Biol. 7 e96 PubMed
- ↑ 21.0 21.1 21.2 21.3 21.4 21.5 21.6 Finn, RD et al. (2010) The Pfam protein families database. Nucleic Acids Res. 38 D211-22 PubMed
Categories
- GO:0042493 ! response to drug
- GO:0000166 ! nucleotide binding
- GO:0003918 ! DNA topoisomerase type II (ATP-hydrolyzing) activity
- GO:0003677 ! DNA binding
- GO:0005524 ! ATP binding
- GO:0006351 ! transcription, DNA-templated
- GO:0008094 ! DNA-dependent ATPase activity
- GO:0006265 ! DNA topological change
- GO:0005737 ! cytoplasm
- GO:0005694 ! chromosome
- GO:0006261 ! DNA-dependent DNA replication
- GO:0009330 ! DNA topoisomerase complex (ATP-hydrolyzing)
- GO:0016020 ! membrane
- GO:0046677 ! response to antibiotic
- Proteins