A0A161I7L9 · A0A161I7L9_9MICO

Function

function

A helicase/nuclease that prepares dsDNA breaks (DSB) for recombinational DNA repair. Binds to DSBs and unwinds DNA via a highly rapid and processive ATP-dependent bidirectional helicase activity. Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator) sequence from the 3' direction. Cuts ssDNA a few nucleotides 3' to the Chi site. The properties and activities of the enzyme are changed at Chi. The Chi-altered holoenzyme produces a long 3'-ssDNA overhang and facilitates RecA-binding to the ssDNA for homologous DNA recombination and repair. Holoenzyme degrades any linearized DNA that is unable to undergo homologous recombination. In the holoenzyme this subunit contributes ATPase, 3'-5' helicase, exonuclease activity and loads RecA onto ssDNA.

Miscellaneous

In the RecBCD complex, RecB has a slow 3'-5' helicase, an exonuclease activity and loads RecA onto ssDNA, RecD has a fast 5'-3' helicase activity, while RecC stimulates the ATPase and processivity of the RecB helicase and contributes to recognition of the Chi site.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 1 Mg2+ ion per subunit.

Features

Showing features for binding site, active site.

Type
IDPosition(s)Description
Binding site47-54ATP (UniProtKB | ChEBI)
Binding site903Mg2+ (UniProtKB | ChEBI)
Binding site1058Mg2+ (UniProtKB | ChEBI)
Active site1076For nuclease activity
Binding site1076Mg2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Cellular Componentexodeoxyribonuclease V complex
Molecular Function3'-5' DNA helicase activity
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular FunctionDNA binding
Molecular Functionexodeoxyribonuclease V activity
Molecular Functionisomerase activity
Molecular Functionmagnesium ion binding
Biological Processdouble-strand break repair via homologous recombination

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    RecBCD enzyme subunit RecB
  • EC number
  • Alternative names
    • DNA 3'-5' helicase subunit RecB
    • Exonuclease V subunit RecB
      (ExoV subunit RecB
      )
    • Helicase/nuclease RecBCD subunit RecB

Gene names

    • Name
      recB
    • ORF names
      I598_2055

Organism names

  • Taxonomic identifier
  • Strain
    • DS-3
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Micrococcales > Promicromonosporaceae > Isoptericola

Accessions

  • Primary accession
    A0A161I7L9

Proteomes

Subcellular Location

Interaction

Subunit

Heterotrimer of RecB, RecC and RecD. All subunits contribute to DNA-binding. Interacts with RecA.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-31Disordered
Region1-764DNA-binding and helicase activity, interacts with RecC
Domain26-358UvrD-like helicase ATP-binding
Domain377-646UvrD-like helicase C-terminal
Region815-1191Nuclease activity, interacts with RecD and RecA
Region838-885Disordered

Domain

The C-terminal domain has nuclease activity and interacts with RecD. It interacts with RecA, facilitating its loading onto ssDNA.
The N-terminal DNA-binding domain is a ssDNA-dependent ATPase and has ATP-dependent 3'-5' helicase function. This domain interacts with RecC.

Sequence similarities

Belongs to the helicase family. UvrD subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,191
  • Mass (Da)
    125,340
  • Last updated
    2016-07-06 v1
  • Checksum
    055EDC9927CC814D
MTFDADAPGTPDEPTAGAHRGAPSFGAERPVFDVHGPLPQGTTVLEASAGTGKTFTIAALATRYVAEGAAELRDLMLVTFGRAATSELRDRVRERLVRTERALRADDPASDPDPLVALLADVDPDELARRRQRLAVALSQLDAATITTTHGFCQQMLVALGIAADVDPAATFLPDVADLVREVSDDLYVRRFADEARPALTPSLAGDVGRAAVSDHQARLVPAEPGGGEPTSGGTLRHRVALDTRTETLRRKRAQHLMDYDDLLVLLRDTLADPVHGPTAAERVRSRYRVVMVDEFQDTDPVQWEILRTAFHGHRTLVLIGDPKQAIYAFRGADVVAYLDAQADATAVATLGTSYRSDRPLLQALHTVLGDVALGDPRIVVRAVEAAHGARFEGGAPLRLRHVASRSLGLKAGSVPAVGTPRTHVAQDVAADVVTRLGRDLIDDDGARRALEPRDVAVLTRTNVQAELVRLALTDRGVPAVVSGLSSVFATPAARDWLTLLDALEQPGAHGRAAALALTPFVGWDAARLAGAGDAAHDELSDTVRRWSRLLTTRGVAALHEAVTREGLAERLLRLTTGERQLTDLRHVGEVLHAAALAEGLGAQSLTAWLRRRIAEAKVDFDEERSRRLETDAAAVQVVTVHASKGLEFGVVYVPYAWDRWEPSTPDVLRFHDDHGLRTLHVGGPASPGYDAALDRSRAEEAGEDLRLLYVALTRARHQVVAHWAPSKANSAKGALTRVLLADRLLGGEPEKHATPRQMRDEDARAALDAVAARSGGTVVVEEVPDAVSTDRWQPPAQDLPALGVSALDRLPDASWRRASYTALTAGAHHGPAGAGFGAAPAAGAPGVTSEPEDTVVEDEPAEQAADALPVGAADAARSGPGADLPSPMSDLPAGAAFGTLVHEVLEYVDTAAADLDAELLAHCTRAAASSRLPGADPARLAAALAVVARTPLGPLAGGATLADVLPRDRLAELEFELPLAGGDGLAGGGGSTARGGPVAPAGRAGTGGATLADVAALLGRHLADDDPFTAYPAMLAELAAADPHPAVLRGYLTGSIDAVLRVIGADGVPRFLVVDYKTNRLGVPDTPLTAHDYRPSATVDAMLHAHYPLQLVLYLVGLHRYLRWRLPGYDPDVHLGGGLYLFVRGMCGPATPAGADGAPHGVVAWVPPSGLVPALSDLLDRGTLSAEEAA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP014209
EMBL· GenBank· DDBJ
ANC31598.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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