A3MWX6 · SRP54_PYRCJ

Function

function

Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP receptor FtsY.

Catalytic activity

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site105-112GTP (UniProtKB | ChEBI)
Binding site185-189GTP (UniProtKB | ChEBI)
Binding site243-246GTP (UniProtKB | ChEBI)

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 Componentsignal recognition particle
Molecular Function7S RNA binding
Molecular FunctionATP hydrolysis activity
Molecular FunctionGTP binding
Molecular FunctionGTPase activity
Biological ProcessSRP-dependent cotranslational protein targeting to membrane

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Signal recognition particle 54 kDa protein
  • EC number
  • Short names
    SRP54

Gene names

    • Name
      srp54
    • Ordered locus names
      Pcal_1726

Organism names

Accessions

  • Primary accession
    A3MWX6

Proteomes

Subcellular Location

Cytoplasm
Note: The SRP-RNC complex is targeted to the cytoplasmic membrane.

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00003222461-431Signal recognition particle 54 kDa protein

Interaction

Subunit

Part of the signal recognition particle protein translocation system, which is composed of SRP and FtsY. Archaeal SRP consists of a 7S RNA molecule of 300 nucleotides and two protein subunits: SRP54 and SRP19.

Protein-protein interaction databases

Structure

Family & Domains

Domain

Composed of three domains: the N-terminal N domain, which is responsible for interactions with the ribosome, the central G domain, which binds GTP, and the C-terminal M domain, which binds the RNA and the signal sequence of the RNC.

Sequence similarities

Belongs to the GTP-binding SRP family. SRP54 subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    431
  • Mass (Da)
    48,296
  • Last updated
    2007-04-03 v1
  • Checksum
    7AAAEA2C9C503D26
MKLSEVFSKLIEKIRGVDYIDEAVLQELSREIQRSLLKADVPLELVKAFTDSAVKRIREEKPPAGIPPREYLVYVLYEELVKLLGGEQPAEFKPTKKPYVVLLLGVEGSGKTTTAAKLAKYLAKRGYKVGLVETDTIRPAAFDQLKQLAEKIGVPFYGERDGKNAVEIAVRGVQNFKNMDVVIIDTAGRHRNEEELLKEVKAIYDAVKPDEVFLVIDATVGKLAAAQAEAFMKYLPIHSVIITKMDSTARGGGALAAVAKTGARVKFIGVGEDVDEFELFNPRKFVARVLGMGDLDALVEKIKAVFEEDKVLEELESGRLDLLTFKKQIDSLLKLGPLSKVFQLLPSNFAIKVSEEQIELSQKNLRKWKAILSSMTMEELKHPEVLNASRIRRIAMGAGVTPKDVKEMLTVFENMKKMSKMLKRQMRMKMR

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000561
EMBL· GenBank· DDBJ
ABO09143.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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