gyrA:Gene Product(s)

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Nomenclature Function Interactions Localization Sequence Domains Structure Resources Accessions Links References Suggestions

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

DNA gyrase, subunit A[2][3];

Component of DNA gyrase[3]

DNA gyrase, subunit A; nalidixic acid resistance; cold shock regulon[4]

EC number (for enzymes)

<protect></protect>

Notes

Function

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<protect> 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

PMID:6178722[5]

IMP: Inferred from Mutant Phenotype

P

complete

GO:0000166

nucleotide binding

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0547

F

Seeded from EcoCyc (v14.0)

complete

GO:0003918

DNA topoisomerase (ATP-hydrolyzing) activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR002205

F

Seeded from EcoCyc (v14.0)

complete

GO:0003918

DNA topoisomerase (ATP-hydrolyzing) activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR005743

F

Seeded from EcoCyc (v14.0)

complete

GO:0003918

DNA topoisomerase (ATP-hydrolyzing) activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR013757

F

Seeded from EcoCyc (v14.0)

complete

GO:0003918

DNA topoisomerase (ATP-hydrolyzing) activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR013758

F

Seeded from EcoCyc (v14.0)

complete

GO:0003918

DNA topoisomerase (ATP-hydrolyzing) activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR013760

F

Seeded from EcoCyc (v14.0)

complete

GO:0003918

DNA topoisomerase (ATP-hydrolyzing) activity

PMID:368801[6]

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

PMID:6294616[7]

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
GO_REF:0000003

IEA: Inferred from Electronic Annotation

EC:5.99.1.3

F

Seeded from EcoCyc (v14.0)

complete

GO:0042493

response to drug

PMID:770163[8]

IMP: Inferred from Mutant Phenotype

P

Oxolinic acid (Quinolone)

complete

GO:0005524

ATP binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR002205

F

Seeded from EcoCyc (v14.0)

complete

GO:0005524

ATP binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR005743

F

Seeded from EcoCyc (v14.0)

complete

GO:0042493

response to drug

PMID:4208771[9]

IMP: Inferred from Mutant Phenotype

P

Naladixic Acid (Quinolone)

complete

GO:0003677

DNA binding

PMID:1851291[10]

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

PMID:347446[11]

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
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR006691

F

Seeded from EcoCyc (v14.0)

complete

GO:0008094

DNA-dependent ATPase activity

PMID:6094559[12]

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
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR013757

F

Seeded from EcoCyc (v14.0)

complete

GO:0006265

DNA topological change

PMID:6327603[13]

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

PMID:15535863[14]

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
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR013758

F

Seeded from EcoCyc (v14.0)

complete

GO:0005737

cytoplasm

PMID:7952188[15]

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
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR013760

F

Seeded from EcoCyc (v14.0)

complete

GO:0005524

ATP binding

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0067

F

Seeded from EcoCyc (v14.0)

complete

GO:0005694

chromosome

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR002205

C

Seeded from EcoCyc (v14.0)

complete

GO:0005694

chromosome

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR005743

C

Seeded from EcoCyc (v14.0)

complete

GO:0005694

chromosome

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR006691

C

Seeded from EcoCyc (v14.0)

complete

GO:0005694

chromosome

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR013757

C

Seeded from EcoCyc (v14.0)

complete

GO:0005694

chromosome

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR013758

C

Seeded from EcoCyc (v14.0)

complete

GO:0005694

chromosome

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR013760

C

Seeded from EcoCyc (v14.0)

complete

GO:0005737

cytoplasm

PMID:7952188[15]

IDA: Inferred from Direct Assay

C

Seeded from EcoCyc (v14.0)

complete

GO:0006261

DNA-dependent DNA replication

PMID:227840[16]

IMP: Inferred from Mutant Phenotype

P

Seeded from EcoCyc (v14.0)

complete

GO:0006265

DNA topological change

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR002205

P

Seeded from EcoCyc (v14.0)

complete

GO:0006265

DNA topological change

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR005743

P

Seeded from EcoCyc (v14.0)

complete

GO:0006265

DNA topological change

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR006691

P

Seeded from EcoCyc (v14.0)

complete

GO:0006265

DNA topological change

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR013757

P

Seeded from EcoCyc (v14.0)

complete

GO:0006265

DNA topological change

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR013758

P

Seeded from EcoCyc (v14.0)

complete

GO:0006265

DNA topological change

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR013760

P

Seeded from EcoCyc (v14.0)

complete

GO:0009330

DNA topoisomerase complex (ATP-hydrolyzing)

PMID:347446[11]

IDA: Inferred from Direct Assay

C

Seeded from EcoCyc (v14.0)

complete

GO:0016020

membrane

PMID:16858726[17]

IDA: Inferred from Direct Assay

C

Seeded from EcoCyc (v14.0)

complete

GO:0046677

response to antibiotic

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0046

P

Seeded from EcoCyc (v14.0)

complete

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

Protein

ycgC

PMID:15690043[18]

Experiment(s):EBI-884206

Protein

aceF

PMID:15690043[18]

Experiment(s):EBI-884206

Protein

add

PMID:15690043[18]

Experiment(s):EBI-884206

Protein

clpA

PMID:15690043[18]

Experiment(s):EBI-884206

Protein

dnaJ

PMID:15690043[18]

Experiment(s):EBI-884206

Protein

dnaK

PMID:15690043[18]

Experiment(s):EBI-884206

Protein

ffh

PMID:15690043[18]

Experiment(s):EBI-884206

Protein

ftsZ

PMID:15690043[18]

Experiment(s):EBI-884206

Protein

glyS

PMID:15690043[18]

Experiment(s):EBI-884206

Protein

zraS

PMID:15690043[18]

Experiment(s):EBI-884206

Protein

lpdA

PMID:15690043[18]

Experiment(s):EBI-884206

Protein

malK

PMID:15690043[18]

Experiment(s):EBI-884206

Protein

metK

PMID:15690043[18]

Experiment(s):EBI-884206

Protein

pstB

PMID:15690043[18]

Experiment(s):EBI-884206

Protein

recA

PMID:15690043[18]

Experiment(s):EBI-884206

Protein

rho

PMID:15690043[18]

Experiment(s):EBI-884206

Protein

rpsB

PMID:15690043[18]

Experiment(s):EBI-884206

Protein

tufA

PMID:15690043[18]

Experiment(s):EBI-884206, EBI-891237

Protein

yjfZ

PMID:15690043[18]

Experiment(s):EBI-884206

Protein

argS

PMID:16606699[19]

Experiment(s):EBI-1142253

Protein

idnO

PMID:16606699[19]

Experiment(s):EBI-1142253

Protein

rpsB

PMID:16606699[19]

Experiment(s):EBI-1142253

Protein

yfaS

PMID:16606699[19]

Experiment(s):EBI-1142253

Protein

aspC

PMID:16606699[19]

Experiment(s):EBI-1142253

Protein

nrdI

PMID:16606699[19]

Experiment(s):EBI-1142253

Protein

rtcB

PMID:16606699[19]

Experiment(s):EBI-1142253

Protein

rho

PMID:19402753[20]

MALDI(Z-score):18.636092

Protein

clpA

PMID:19402753[20]

MALDI(Z-score):19.599720

Protein

pstB

PMID:19402753[20]

MALDI(Z-score):35.274106

Protein

recA

PMID:19402753[20]

MALDI(Z-score):29.421963

Protein

metK

PMID:19402753[20]

MALDI(Z-score):37.360726

Protein

add

PMID:19402753[20]

MALDI(Z-score):32.777259

Protein

dnaJ

PMID:19402753[20]

MALDI(Z-score):34.861527

Protein

tufB

PMID:19402753[20]

MALDI(Z-score):22.155359

Protein

mreB

PMID:19402753[20]

MALDI(Z-score):36.098785

Protein

GyrB

The binding of gyrase to DNA: analysis by retention by nitrocellulose filters. Higgins & Cozzarelli (1982)[7]
Purification of subunits of Escherichia coli DNA gyrase and reconstitution of enzymatic activity. Higgins et al. (1978) [11]

Small Molecule

Naladixic Acid

Studies on the mechanism of action of nalidixic acid. Bourguignon et al. (1973) [9]

Small Molecule

Oxolinic acid

Replication of Escherichia coli DNA in vitro: inhibition by oxolinic acid. Staudenbauer (1976) [8]

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]


</protect>

Notes

Localization

See Help:Product_localization for how to add or edit information in this section of EcoliWiki.

Compartment Description Evidence Reference/Source Notes

<protect></protect>

Notes

Structure and Physical Properties

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<protect> Physical Properties See Help:Product_physical_properties for help entering or editing information about the physical properties of this gene product.

Name
Sequence

at EcoCyc

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)


Domains/Motifs/Modification Sites

See Help:Product_domains_motifs for help entering or editing information in this section of EcoliWiki.

Type Residues Description Notes References

Domain

537..586

PF03989 DNA gyrase C-terminal domain, beta-propeller

PMID:19920124[21]

Domain

587..639

PF03989 DNA gyrase C-terminal domain, beta-propeller

PMID:19920124[21]

Domain

643..690

PF03989 DNA gyrase C-terminal domain, beta-propeller

PMID:19920124[21]

Domain

691..740

PF03989 DNA gyrase C-terminal domain, beta-propeller

PMID:19920124[21]

Domain

741..791

PF03989 DNA gyrase C-terminal domain, beta-propeller

PMID:19920124[21]

Domain

793..841

PF03989 DNA gyrase C-terminal domain, beta-propeller

PMID:19920124[21]

Domain

32..507

PF00521 DNA gyrase/topoisomerase IV, subunit A

PMID:19920124[21]

<motif_map/>

Structure
See Help:Product_structure for help entering or editing information in this section of EcoliWiki.

Structures

<beststructure> gene=gyrA taxon=562,83333 </beststructure>

Models

View models at:

</protect>

Structure figures

<protect>

</protect>

Notes

Gene Product Resources

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See Help:Product_resources for help with entering or editing information in this section of EcoliWiki.

Resource type Source Notes/Reference

<protect></protect>

Notes

Accessions in Other Databases

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See Help:Gene_accessions for help with entering information into the Gene Accessions table.

Database Accession Notes

NCBI (Protein) (EcoliWiki Page)

GI:16130166

Escherichia coli str. K-12 substr. MG1655

NCBI (Protein) (EcoliWiki Page)

GeneID:946614

Escherichia coli str. K-12 substr. MG1655

ASAP

ASAP:ABE-0007370

Escherichia coli str. K-12 substr. MG1655

UniProt (EcoliWiki Page)

UniProtKB/Swiss-Prot:P0AES4

Escherichia coli str. K-12 substr. MG1655

EcoCyc

EcoCyc:EG10423

Escherichia coli str. K-12 substr. MG1655

EcoGene

EcoGene:EG10423

Escherichia coli str. K-12 substr. MG1655

NCBI (Gene) (EcoliWiki Page)

GeneID:946614

Escherichia coli str. K-12 substr. MG1655

RegulonDB

RegulonDB:ECK120000416

Escherichia coli str. K-12 substr. MG1655

EchoBASE

EchoBASE:EB0418

Escherichia coli str. K-12 substr. MG1655

<protect></protect>

Notes

Links

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References

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See Help:References for how to manage references in EcoliWiki.

  1. 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. 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. 3.0 3.1 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  4. EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
  5. 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
  6. 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. 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. 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. 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. 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. 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
  12. Maxwell, A & Gellert, M (1984) The DNA dependence of the ATPase activity of DNA gyrase. J. Biol. Chem. 259 14472-80 PubMed
  13. Steck, TR et al. (1984) DNA supercoiling in gyrase mutants. J. Bacteriol. 158 397-403 PubMed
  14. Peter, BJ et al. (2004) Genomic transcriptional response to loss of chromosomal supercoiling in Escherichia coli. Genome Biol. 5 R87 PubMed
  15. 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
  16. 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
  17. 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. 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. 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. 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. 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

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