P9WGD6 · SRP54_MYCTO

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.

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TypeIDPosition(s)Description
Binding site107-114GTP (UniProtKB | ChEBI)
Binding site196-200GTP (UniProtKB | ChEBI)
Binding site254-257GTP (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 protein
  • EC number
  • Alternative names
    • Fifty-four homolog

Gene names

    • Name
      ffh
    • Ordered locus names
      MT2984

Organism names

Accessions

  • Primary accession
    P9WGD6
  • Secondary accessions
    • L0TDR8
    • P66844
    • Q10963

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_00004283801-525Signal recognition particle protein

Interaction

Subunit

Part of the signal recognition particle protein translocation system, which is composed of SRP and FtsY.

Structure

Family & Domains

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region437-525Disordered
Compositional bias449-469Basic residues

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
    525
  • Mass (Da)
    55,002
  • Last updated
    2014-04-16 v1
  • Checksum
    36F6227BC367817C
MFESLSDRLTAALQGLRGKGRLTDADIDATTREIRLALLEADVSLPVVRAFIHRIKERARGAEVSSALNPAQQVVKIVNEELISILGGETRELAFAKTPPTVVMLAGLQGSGKTTLAGKLAARLRGQGHTPLLVACDLQRPAAVNQLQVVGERAGVPVFAPHPGASPESGPGDPVAVAAAGLAEARAKHFDVVIVDTAGRLGIDEELMAQAAAIRDAINPDEVLFVLDAMIGQDAVTTAAAFGEGVGFTGVALTKLDGDARGGAALSVREVTGVPILFASTGEKLEDFDVFHPDRMASRILGMGDVLSLIEQAEQVFDAQQAEEAAAKIGAGELTLEDFLEQMLAVRKMGPIGNLLGMLPGAAQMKDALAEVDDKQLDRVQAIIRGMTPQERADPKIINASRRLRIANGSGVTVSEVNQLVERFFEARKMMSSMLGGMGIPGIGRKSATRKSKGAKGKSGKKSKKGTRGPTPPKVKSPFGVPGMPGLAGLPGGLPDLSQMPKGLDELPPGLADFDLSKLKFPGKK

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias449-469Basic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE000516
EMBL· GenBank· DDBJ
AAK47310.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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