gyrB: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

GyrB

Synonyms

DNA gyrase, subunit B[1], B3699[2][1], NalC[2][1], ParA[2][1], PcbA[2][1], PcpA[2][1], HopA[2][1], Cou[2][1], HisU[2][1], HimB[2][1], GyrB[2][1]

Product description

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

Component of DNA gyrase[3]

DNA gyrase, subunit B; novobiocin, coumermycin resistance[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(s) Evidence Code with/from Aspect Notes Status
GO:0000166

nucleotide binding

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0547

F

Seeded from EcoCyc [5]

complete

GO:0003676

nucleic acid binding

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR006171

F

Seeded from EcoCyc 12.5 [6]

complete

GO:0003916

DNA topoisomerase activity

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0799

F

Seeded from EcoCyc [5]

complete

GO:0003918

DNA topoisomerase (ATP-hydrolyzing) activity

GO_REF:0000002
GO_REF:0000002
GO_REF:0000002
GO_REF:0000002
GO_REF:0000002
GO_REF:0000002
GO_REF:0000002
GO_REF:0000003

IEA: Inferred from Electronic Annotation

InterPro:IPR001241
InterPro:IPR002288
InterPro:IPR011557
InterPro:IPR011558
InterPro:IPR013506
InterPro:IPR013759
InterPro:IPR013760
EC:5.99.1.3

F

Seeded from EcoCyc 12.5 [6]

complete

GO:0005524

ATP binding

GO_REF:0000002
GO_REF:0000002
GO_REF:0000002
GO_REF:0000002
GO_REF:0000002
GO_REF:0000002
GO_REF:0000002
GO_REF:0000002
GO_REF:0000004

IEA: Inferred from Electronic Annotation

InterPro:IPR001241
InterPro:IPR002288
InterPro:IPR003594
InterPro:IPR011557
InterPro:IPR011558
InterPro:IPR013506
InterPro:IPR013759
InterPro:IPR013760
SP_KW:KW-0067

F

Seeded from EcoCyc 12.5 [6]

complete

GO:0005694

chromosome

GO_REF:0000002
GO_REF:0000002
GO_REF:0000002
GO_REF:0000002
GO_REF:0000002
GO_REF:0000002
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR001241
InterPro:IPR002288
InterPro:IPR011557
InterPro:IPR011558
InterPro:IPR013506
InterPro:IPR013759
InterPro:IPR013760

C

Seeded from EcoCyc 12.5 [6]

complete

GO:0006265

DNA topological change

GO_REF:0000002
GO_REF:0000002
GO_REF:0000002
GO_REF:0000002
GO_REF:0000002
GO_REF:0000002
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR001241
InterPro:IPR002288
InterPro:IPR011557
InterPro:IPR011558
InterPro:IPR013506
InterPro:IPR013759
InterPro:IPR013760

P

Seeded from EcoCyc 12.5 [6]

complete

GO:0006304

DNA modification

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR006171

P

Seeded from EcoCyc 12.5 [6]

complete

GO:0016853

isomerase activity

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0413

F

Seeded from EcoCyc [5]

complete

GO:0046677

response to antibiotic

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0046

P

Seeded from EcoCyc [5]

complete

GO:0005737

cytoplasm

C

Seeded from EcoCyc 11.1[3].

required fields missing

GO:0006261

DNA-dependent DNA replication

PMID:6194415[7]

IMP: Inferred from Mutant Phenotype

P

Seeded from EcoCyc 11.1[3].

gyrB(ts)

complete

GO:0006350

transcription

P

Seeded from EcoCyc 11.1[3].

required fields missing

GO:0008094

DNA-dependent ATPase activity

PMID:6094559[8]

IDA: Inferred from Direct Assay

F

ATPase activity of the GyrB subunit was followed by measuring the release of 32P-labeled phosphate from reactions containing [y-32P]-ATP in the presence of GyrA and DNA (Figure 1). Omission of DNA or GyrA (which binds DNA) resulted in dramatically reduced ATPase activity of GyrB.

complete

GO:0003677

DNA binding

PMID:10764756[9]

IMP: Inferred from Mutant Phenotype

F

A truncated mutant of GyrB that lacks the C-terminal 160 residues has a reduced ability to retard the movement of DNA through a 5% polyacrylamide gel indicating a deficiency in DNA binding (Figure 5).

complete

GO:0009330

DNA topoisomerase complex (ATP-hydrolyzing)

PMID:347446[10]

IDA: Inferred from Direct Assay

C

E. coli gyrase consists of the gene products of gyrA and gyrB genes (Figures 2 & 7).

complete

GO:0006265

DNA topological change

PMID:6327603[11]

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:0005524

ATP binding

PMID:9756859[12]

IDA: Inferred from Direct Assay

F

Using gel filtration and equilibrium ultracentrifugation, the authors showed that the 43kDa N-terminal fragment of GyrB binds to ADPNP, or [32-P]ADPNP, and ATP (Figure 7 and Table 1).

complete

GO:0042493

response to drug

PMID:9144789[13]

IDA: Inferred from Direct Assay

P

Coumarin antibiotic sensitivity, including clorobiocin, novobiocin, and coumermycin A1.

complete

GO:0003918

DNA topoisomerase (ATP-hydrolyzing) activity

PMID:368801[14]

IDA: Inferred from Direct Assay

F

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[15]

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:0006350

transcription

PMID:15535863[16]

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:0005737

cytoplasm

PMID:7952188[17]

IDA: Inferred from Direct Assay

C

Immunogold labeling of cells with anti-GyrB antibodies indicated the presence of GyrB in the cytoplasm of E. coli.

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

Protein

prsA

PMID:15690043[18]

Experiment(s):EBI-884130

Protein

bglJ

PMID:15690043[18]

Experiment(s):EBI-884130

Protein

deaD

PMID:15690043[18]

Experiment(s):EBI-884130

Protein

glyS

PMID:15690043[18]

Experiment(s):EBI-884130

Protein

gyrA

PMID:15690043[18]

Experiment(s):EBI-884130, EBI-884206, EBI-891214, EBI-891237

Protein

metK

PMID:15690043[18]

Experiment(s):EBI-884130

Protein

rplJ

PMID:15690043[18]

Experiment(s):EBI-884130

Protein

rpsB

PMID:15690043[18]

Experiment(s):EBI-884130

Protein

tufA

PMID:15690043[18]

Experiment(s):EBI-884130, EBI-891214

Protein

yacG

PMID:15690043[18]

Experiment(s):EBI-884130, EBI-879073, EBI-882474, EBI-891214

Protein

parE

PMID:15690043[18]

Experiment(s):EBI-891214

Protein

rplW

PMID:15690043[18]

Experiment(s):EBI-891214

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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 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.

Sequence

at EcoCyc

MSNSYDSSSI KVLKGLDAVR KRPGMYIGDT DDGTGLHHMV FEVVDNAIDE ALAGHCKEII
VTIHADNSVS VQDDGRGIPT GIHPEEGVSA AEVIMTVLHA GGKFDDNSYK VSGGLHGVGV
SVVNALSQKL ELVIQREGKI HRQIYEHGVP QAPLAVTGET EKTGTMVRFW PSLETFTNVT
EFEYEILAKR LRELSFLNSG VSIRLRDKRD GKEDHFHYEG GIKAFVEYLN KNKTPIHPNI
FYFSTEKDGI GVEVALQWND GFQENIYCFT NNIPQRDGGT HLAGFRAAMT RTLNAYMDKE
GYSKKAKVSA TGDDAREGLI AVVSVKVPDP KFSSQTKDKL VSSEVKSAVE QQMNELLAEY
LLENPTDAKI VVGKIIDAAR AREAARRARE MTRRKGALDL AGLPGKLADC QERDPALSEL
YLVEGDSAGG SAKQGRNRKN QAILPLKGKI LNVEKARFDK MLSSQEVATL ITALGCGIGR
DEYNPDKLRY HSIIIMTDAD VDGSHIRTLL LTFFYRQMPE IVERGHVYIA QPPLYKVKKG
KQEQYIKDDE AMDQYQISIA LDGATLHTNA SAPALAGEAL EKLVSEYNAT QKMINRMERR
YPKAMLKELI YQPTLTEADL SDEQTVTRWV NALVSELNDK EQHGSQWKFD VHTNAEQNLF
EPIVRVRTHG VDTDYPLDHE FITGGEYRRI CTLGEKLRGL LEEDAFIERG ERRQPVASFE
QALDWLVKES RRGLSIQRYK GLGEMNPEQL WETTMDPESR RMLRVTVKDA IAADQLFTTL
MGDAVEPRRA FIEENALKAA NIDI
Length

804

Mol. Wt

89.951 kDa

pI

6.0 (calculated)

Extinction coefficient

71,740 - 72,365 (calc based on 26 Y, 6 W, and 5 C residues)

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Domains/Motifs/Modification Sites

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Type Residues Description Notes

Initiator Methionine

1

Removed

UniProt:P0AES6

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<motif_map/>

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

Structures

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

Models

View models at:

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Structure figures

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
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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

EcoCyc (EcoliWiki Page)

EcoCyc:EG10424-MONOMER

SwissModel (EcoliWiki Page)

SwissModel:P0AES6

UniProt (EcoliWiki Page)

UniProt:P0AES6

PFAM (EcoliWiki Page)

PFAM:PF02518

RefSeq (EcoliWiki Page)

RefSeq:YP_026241

PDB (EcoliWiki Page)

PDB:1AJ6


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Notes

Links

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Name URL Comments
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References

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

  1. ↑ 1.00 1.01 1.02 1.03 1.04 1.05 1.06 1.07 1.08 1.09 1.10 1.11 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
  2. ↑ 2.00 2.01 2.02 2.03 2.04 2.05 2.06 2.07 2.08 2.09 2.10 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. ↑ 3.0 3.1 3.2 3.3 3.4 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. ↑ 5.0 5.1 5.2 5.3 EcoCyc (release 13.0; 2009) Keseler, IM et al. (2009) Nucleic Acids Res. 37(Database issue):D464-70
  6. ↑ 6.0 6.1 6.2 6.3 6.4 6.5 EcoCyc (release 12.5; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  7. ↑ Filutowicz, M & Jonczyk, P (1983) The gyrB gene product functions in both initiation and chain polymerization of Escherichia coli chromosome replication: suppression of the initiation deficiency in gyrB-ts mutants by a class of rpoB mutations. Mol. Gen. Genet. 191 282-7 PubMed
  8. ↑ Maxwell, A & Gellert, M (1984) The DNA dependence of the ATPase activity of DNA gyrase. J. Biol. Chem. 259 14472-80 PubMed
  9. ↑ Chatterji, M et al. (2000) The additional 165 amino acids in the B protein of Escherichia coli DNA gyrase have an important role in DNA binding. J. Biol. Chem. 275 22888-94 PubMed
  10. ↑ 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
  11. ↑ Steck, TR et al. (1984) DNA supercoiling in gyrase mutants. J. Bacteriol. 158 397-403 PubMed
  12. ↑ Kampranis, SC & Maxwell, A (1998) Hydrolysis of ATP at only one GyrB subunit is sufficient to promote supercoiling by DNA gyrase. J. Biol. Chem. 273 26305-9 PubMed
  13. ↑ Tsai, FT et al. (1997) The high-resolution crystal structure of a 24-kDa gyrase B fragment from E. coli complexed with one of the most potent coumarin inhibitors, clorobiocin. Proteins 28 41-52 PubMed
  14. ↑ 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
  15. ↑ Higgins, NP & Cozzarelli, NR (1982) The binding of gyrase to DNA: analysis by retention by nitrocellulose filters. Nucleic Acids Res. 10 6833-47 PubMed
  16. ↑ Peter, BJ et al. (2004) Genomic transcriptional response to loss of chromosomal supercoiling in Escherichia coli. Genome Biol. 5 R87 PubMed
  17. ↑ Thornton, M et al. (1994) Immunogold localization of GyrA and GyrB proteins in Escherichia coli. Microbiology (Reading, Engl.) 140 ( Pt 9) 2371-82 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 Butland, G et al. (2005) Interaction network containing conserved and essential protein complexes in Escherichia coli. Nature 433 531-7 PubMed

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