Q104Q5 · Q104Q5_ALIFS

Function

function

Plays an essential role in type IV pili and type II pseudopili formation by proteolytically removing the leader sequence from substrate proteins and subsequently monomethylating the alpha-amino group of the newly exposed N-terminal phenylalanine.

Catalytic activity

  • Typically cleaves a -Gly-|-Phe- bond to release an N-terminal, basic peptide of 5-8 residues from type IV prepilin, and then N-methylates the new N-terminal amino group, the methyl donor being S-adenosyl-L-methionine.
    EC:3.4.23.43 (UniProtKB | ENZYME | Rhea)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentplasma membrane
Molecular Functionaspartic-type endopeptidase activity
Molecular Functionmethyltransferase activity
Biological Processmethylation
Biological Processsignal peptide processing

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Prepilin leader peptidase/N-methyltransferase
  • EC number

Gene names

    • Name
      pilD

Organism names

Accessions

  • Primary accession
    Q104Q5

Subcellular Location

Cell inner membrane
; Multi-pass membrane protein
Cell membrane
; Multi-pass membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane6-33Helical
Transmembrane132-150Helical
Transmembrane162-180Helical
Transmembrane186-206Helical
Transmembrane235-253Helical
Transmembrane265-287Helical

Keywords

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain17-126Prepilin peptidase A24 N-terminal
Domain138-248Prepilin type IV endopeptidase peptidase

Sequence similarities

Belongs to the peptidase A24 family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    295
  • Mass (Da)
    33,248
  • Last updated
    2006-08-22 v1
  • Checksum
    0A6FCBFF95107E77
MAVFDYYPWLFPLFATLFGLLVGSFLNVVIYRLPIMMEKEWKKDCIDCFPDLAPEKTNEEKEETFNLSVPRSRCPKCQTQIKFYDNIPVISWLLLKGKCRQCSNPISFRYPAIELLSGAMCFAVSYLLPFSYFAVAAILFTLVLIALTFIDIDTMLLPDQITLPLLWSGLYLALVGWNSVSLVDSVVGAMAGYLILWSIYWCFKLLTGKEGMGYGDFKLLAALGAWLGWQQLPLIILLSSVVGAIIGVIMLTAQKKGFDKAIPFGPYLAIAGWVCLLWGQNISQWYFNHILGLPL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DQ093341
EMBL· GenBank· DDBJ
ABC11883.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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