D7Y2H4 · CAP6_ECOM1

Function

function

Regulates complex assembly in a CBASS antivirus system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type III-C(AAA) CBASS system (PubMed:32839535).
Binds and disassembles an active CdnC:Cap7 (Cap7 is also called HORMA) complex, inhibiting the complex's ability to synthesize cyclic nucleotide second messengers (PubMed:31932165).
An AAA+-ATPase remodeler, in the absence of foreign threat Cap6 (also called Trip13) probably maintains the Cap7 protein in its open, inactive state. Once activated (presumably by a bacteriophage protein) Cap7 binds to and activates its cognate CD-NTase (CdnC in this bacteria) to synthesize cAAA, a cyclic nucleotide second messenger. cAAA activates the NucC endonuclease which degrades all DNA in the infected cell, causing cell death and abortive phage infection (Probable)
Protects E.coli strain JP313 against bacteriophage lambda cI- infection. When the cdnC-cap7-cap6-nucC operon is transformed into a susceptible E.coli strain it confers bacteriophage lambda cI- immunity. Mutations in the sensor (Cap7 also called HORMA) or effector proteins (CdnC, NucC) but not the disassembly protein (Cap6 also called Trip13) no longer confer immunity. The presence of the intact operon leads to culture collapse and cell death, which occurs before the phage has finished its replication cycle, thus protecting non-infected bacteria by aborting the phage infection and preventing its propagation.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site84-89ATP (UniProtKB | ChEBI)
Binding site215-216ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentmicrotubule cytoskeleton
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Biological Processdefense response to virus

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    CD-NTase-associated protein 6
  • Short names
    Cap6
  • Alternative names
    • CBASS disassembly protein Trip13
    • Probable ATPase Trip13

Gene names

    • Name
      cap6
    • Synonyms
      trip13
    • ORF names
      HMPREF9540_01760

Organism names

Accessions

  • Primary accession
    D7Y2H4

Subcellular Location

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis87Partially inhibits second messenger synthesis by CdnC:Cap7:DNA complex.
Mutagenesis159Stabilizes a 1:1:6 CdnC:Cap7:Cap6 complex, probably prevents ATP hydrolysis. Still confers phage immunity.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004518431-311CD-NTase-associated protein 6

Interaction

Subunit

Homohexamer. Forms a 1:1:6 CdnC:Cap7:Cap6 complex.

Family & Domains

Domain

In the disassembly complex (PDB:6P8V) Cap6 (this protein) crystallizes as a right-handed spiral; the top 4 subunits bind ATP while the bottom 2 do not. A CdnC monomer lies along the surface of the hexamer at the interface of subunits 5 and 6, with Cap7 (also called HORMA) at its tip, over the central hexamer pore. The N-terminus of Cap7 extends into the pore, contacting 5/6 Cap6 subunits.

Sequence similarities

Belongs to the AAA ATPase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    311
  • Mass (Da)
    34,358
  • Last updated
    2010-10-05 v1
  • Checksum
    745DAF9F1763971B
MNVKPSLDELFERRINFPDFEPQERLARLVGLDEHKDRLSKILGLLVNPYGIQEWAKKYHPDARAAVDTVLRRPPLVVLAGDVGSGKTELAETIGDAVARQEDIDITLYPLSLATRGQGRVGEMTQLVSAAFDYTIEAADKLKNTNGKARGAVLLLIDEADALAQSRENAQMHHEDRAGVNAFIRGIDRIANQKLPAAVLMCTNRLKALDPAVQRRAAEILTFSRPNDEQRHYLLHSKLTGLGLNSTAVEELVRLTGPRDPNSPGFTFSDITQRLIPSIILAAYPYNAVSVHSALQVVNKMTPTPAFIDRQ

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
ADTL01000141
EMBL· GenBank· DDBJ
EFJ98158.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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