P37923 · FIMC_SALTY

Function

function

Required for the biogenesis of type 1 fimbriae. Binds and interact with FimH.

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 Componentouter membrane-bounded periplasmic space
Biological Processcell wall organization
Biological Processchaperone-mediated protein folding

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Chaperone protein FimC

Gene names

    • Name
      fimC
    • Ordered locus names
      STM0545

Organism names

Accessions

  • Primary accession
    P37923

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, chain.

TypeIDPosition(s)Description
Signal1-23
ChainPRO_000000927624-230Chaperone protein FimC

Proteomic databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the periplasmic pilus chaperone family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    230
  • Mass (Da)
    24,868
  • Last updated
    1994-10-01 v1
  • Checksum
    9CC193826E92A712
MLNSIKVGFIVLLTLFTSLNVQAAGGIALGATRVIYPSAAKQTSLAISNSDTQERYLVNSWIENNAGQKEKTFIVTPPLFVSEPKSENTLRIIYAGQPLPGDRESLFWMNVKAIPSVDKSHIEGKNVLQLAILSRIKLFVRPANLPQTPEDAPTLLKFSRVGNHLKITNPSAYYLTLVNISVGAKKIDNVMIAPKSDMQIPLPTGAQGNVTFQSVNDYGALTSATTASLG

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
L19338
EMBL· GenBank· DDBJ
AAA75418.1
EMBL· GenBank· DDBJ
Genomic DNA
AE006468
EMBL· GenBank· DDBJ
AAL19499.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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