recQ: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

RecQ

Synonyms

ATP-dependent DNA helicase[1], B3822[2][1], RecQ[2][1]

Product description

ATP-dependent DNA helicase[2][3]

DNA helicase involved in recombination, replication, repair; ATP-dependent; monomeric[4]

EC number (for enzymes)


Notes

  • A mutant of the human homolog of RecQ, known as BLM, is responsible for Bloom syndrome. See BLM on GONUTS.

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:0044237

cellular metabolic process

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR010997

P

Seeded from EcoCyc [5]

complete

GO:0016787

hydrolase activity

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0378

F

Seeded from EcoCyc [5]

complete

GO:0009432

SOS response

GO_REF:0000002
GO_REF:0000004

IEA: Inferred from Electronic Annotation

InterPro:IPR006293
SP_KW:KW-0742

P

Seeded from EcoCyc [5]

complete

GO:0008270

zinc ion binding

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR002857

F

Seeded from EcoCyc 12.5 [6]

complete

GO:0008026

ATP-dependent helicase activity

GO_REF:0000002
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR004589
InterPro:IPR011545

F

Seeded from EcoCyc [5]

complete

GO:0006974

response to DNA damage stimulus

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0227

P

Seeded from EcoCyc [5]

complete

GO:0006310

DNA recombination

GO_REF:0000002
GO_REF:0000002
GO_REF:0000004

IEA: Inferred from Electronic Annotation

InterPro:IPR004589
InterPro:IPR006293
SP_KW:KW-0233

P

Seeded from EcoCyc [5]

complete

GO:0006281

DNA repair

GO_REF:0000004
GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0234
SP_KW:KW-0742

P

Seeded from EcoCyc [5]

complete

GO:0005622

intracellular

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR002121

C

Seeded from EcoCyc [5]

complete

GO:0005524

ATP binding

GO_REF:0000002
GO_REF:0000002
GO_REF:0000004

IEA: Inferred from Electronic Annotation

InterPro:IPR001650
InterPro:IPR011545
SP_KW:KW-0067

F

Seeded from EcoCyc [5]

complete

GO:0004386

helicase activity

GO_REF:0000002
GO_REF:0000004

IEA: Inferred from Electronic Annotation

InterPro:IPR001650
SP_KW:KW-0347

F

Seeded from EcoCyc [5]

complete

GO:0004003

ATP-dependent DNA helicase activity

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR006293

F

Seeded from EcoCyc [5]

complete

GO:0003824

catalytic activity

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR010997

F

Seeded from EcoCyc [5]

complete

GO:0003677

DNA binding

GO_REF:0000002
GO_REF:0000004

IEA: Inferred from Electronic Annotation

InterPro:IPR002857
SP_KW:KW-0238

F

Seeded from EcoCyc 12.5 [6]

complete

GO:0003676

nucleic acid binding

GO_REF:0000002
GO_REF:0000002
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR001650
InterPro:IPR002121
InterPro:IPR011545

F

Seeded from EcoCyc [5]

complete

GO:0000166

nucleotide binding

GO_REF:0000002
GO_REF:0000004

IEA: Inferred from Electronic Annotation

InterPro:IPR010997
SP_KW:KW-0547

F

Seeded from EcoCyc [5]

complete

GO:0005737

cytoplasm

C

Seeded from EcoCyc 11.1[3].

required fields missing

GO:0006261

DNA-dependent DNA replication

P

Seeded from EcoCyc 11.1[3].

required fields missing

GO:0046914

transition metal ion binding

PMID:2164680[7]

IDA: Inferred from Direct Assay

F

complete

GO:0016887

ATPase activity

PMID:2164680[7]

IDA: Inferred from Direct Assay

F

complete

GO:0008094

DNA-dependent ATPase activity

PMID:2164680[7]

IDA: Inferred from Direct Assay

F

complete

GO:0004003

ATP-dependent DNA helicase activity

PMID:2164680[7]

IDA: Inferred from Direct Assay

F

complete

GO:0005737

cytoplasm

PMID:2164680[7]

IDA: Inferred from Direct Assay

C

complete

GO:0003677

DNA binding

PMID:14665634[8]

IDA: Inferred from Direct Assay

F

complete

GO:0008270

zinc ion binding

PMID:15292213[9]

IMP: Inferred from Mutant Phenotype

F

complete

GO:0005524

ATP binding

PMID:15292213[9]

IPI: Inferred from Physical Interaction

F

complete

GO:0017116

single-stranded DNA-dependent ATP-dependent DNA helicase activity

PMID:12805371[10]

IDA: Inferred from Direct Assay

F

complete

GO:0017117

single-stranded DNA-dependent ATP-dependent DNA helicase complex

PMID:12805371[10]

IDA: Inferred from Direct Assay

C

complete

GO:0006310

DNA recombination

PMID:7868608[11]

IMP: Inferred from Mutant Phenotype

P

complete

GO:0006281

DNA repair

PMID:7868608[11]

IGI: Inferred from Genetic Interaction

EcoliWiki:recB|EcoliWiki:recC|EcoliWiki:sbcB|EcoliWiki:sbcC

P

complete

GO:0006974

response to DNA damage stimulus

PMID:7868608[11]

IGI: Inferred from Genetic Interaction

EcoliWiki:recB|EcoliWiki:recC|EcoliWiki:sbcB|EcoliWiki:sbcC

P

complete

GO:0006310

DNA recombination

PMID:9553043[12]

IDA: Inferred from Direct Assay

P

With RecA & SSB.

complete

GO:0005515

protein binding

PMID:19150358[13]

IPI: Inferred from Physical Interaction

UniProtKB:P0AGE0

F

SSB (Single-stranded DNA-binding protein)

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

ssb

PMID:15690043[14]

Experiment(s):EBI-882208, EBI-885071, EBI-889737

Protein

aceE

PMID:15690043[14]

Experiment(s):EBI-882208

Protein

aceF

PMID:15690043[14]

Experiment(s):EBI-882208, EBI-889737

Protein

lpdA

PMID:15690043[14]

Experiment(s):EBI-882208, EBI-889737

Protein

topA

PMID:15690043[14]

Experiment(s):EBI-882208, EBI-888130

Protein

rpmB

PMID:15690043[14]

Experiment(s):EBI-889737

Protein

rpsN

PMID:15690043[14]

Experiment(s):EBI-889737


Notes

Localization

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

Compartment Description Evidence Source Notes


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

MAQAEVLNLE SGAKQVLQET FGYQQFRPGQ EEIIDTVLSG RDCLVVMPTG GGKSLCYQIP
ALLLNGLTVV VSPLISLMKD QVDQLQANGV AAACLNSTQT REQQLEVMTG CRTGQIRLLY
IAPERLMLDN FLEHLAHWNP VLLAVDEAHC ISQWGHDFRP EYAALGQLRQ RFPTLPFMAL
TATADDTTRQ DIVRLLGLND PLIQISSFDR PNIRYMLMEK FKPLDQLMRY VQEQRGKSGI
IYCNSRAKVE DTAARLQSKG ISAAAYHAGL ENNVRADVQE KFQRDDLQIV VATVAFGMGI
NKPNVRFVVH FDIPRNIESY YQETGRAGRD GLPAEAMLFY DPADMAWLRR CLEEKPQGQL
QDIERHKLNA MGAFAEAQTC RRLVLLNYFG EGRQEPCGNC DICLDPPKQY DGSTDAQIAL
STIGRVNQRF GMGYVVEVIR GANNQRIRDY GHDKLKVYGM GRDKSHEHWV SVIRQLIHLG
LVTQNIAQHS ALQLTEAARP VLRGESSLQL AVPRIVALKP KAMQKSFGGN YDRKLFAKLR
KLRKSIADES NVPPYVVFND ATLIEMAEQM PITASEMLSV NGVGMRKLER FGKPFMALIR
AHVDGDDEE
Length

609

Mol. Wt

68.364 kDa

pI

7.3 (calculated)

Extinction coefficient

48,820 - 50,195 (calc based on 18 Y, 4 W, and 11 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

Initiator Methionine

1

Removed

UniProt:P15043

<motif_map/>

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

Structures

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

Models

View models at:

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


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:EG10833-MONOMER

UniProt (EcoliWiki Page)

UniProt:P15043

PFAM (EcoliWiki Page)

PFAM:PF00270

RefSeq (EcoliWiki Page)

RefSeq:YP_026263



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 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
  2. ↑ 2.0 2.1 2.2 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 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. ↑ 5.00 5.01 5.02 5.03 5.04 5.05 5.06 5.07 5.08 5.09 5.10 5.11 5.12 5.13 EcoCyc (release 13.0; 2009) Keseler, IM et al. (2009) Nucleic Acids Res. 37(Database issue):D464-70
  6. ↑ 6.0 6.1 EcoCyc (release 12.5; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  7. ↑ 7.0 7.1 7.2 7.3 7.4 Umezu, K et al. (1990) Escherichia coli RecQ protein is a DNA helicase. Proc. Natl. Acad. Sci. U.S.A. 87 5363-7 PubMed
  8. ↑ Dou, SX et al. (2004) The DNA binding properties of the Escherichia coli RecQ helicase. J. Biol. Chem. 279 6354-63 PubMed
  9. ↑ 9.0 9.1 Liu, JL et al. (2004) The zinc finger motif of Escherichia coli RecQ is implicated in both DNA binding and protein folding. J. Biol. Chem. 279 42794-802 PubMed
  10. ↑ 10.0 10.1 Xu, HQ et al. (2003) The Escherichia coli RecQ helicase functions as a monomer. J. Biol. Chem. 278 34925-33 PubMed
  11. ↑ 11.0 11.1 11.2 Mendonca, VM et al. (1995) DNA helicases in recombination and repair: construction of a delta uvrD delta helD delta recQ mutant deficient in recombination and repair. J. Bacteriol. 177 1326-35 PubMed
  12. ↑ Harmon, FG & Kowalczykowski, SC (1998) RecQ helicase, in concert with RecA and SSB proteins, initiates and disrupts DNA recombination. Genes Dev. 12 1134-44 PubMed
  13. ↑ Shereda, RD et al. (2009) Identification of the SSB binding site on E. coli RecQ reveals a conserved surface for binding SSB's C terminus. J. Mol. Biol. 386 612-25 PubMed
  14. ↑ 14.0 14.1 14.2 14.3 14.4 14.5 14.6 Butland, G et al. (2005) Interaction network containing conserved and essential protein complexes in Escherichia coli. Nature 433 531-7 PubMed

Categories

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