Q9XD84 · TIBA_ECOH1

Function

function

Mediates both adhesion to and invasion of human intestine epithelial cells (PubMed:11119488, PubMed:8039917).
Also mediates bacterial cell aggregation via intercellular TibA-TibA interaction (PubMed:15784535).
Enhances biofilm formation (PubMed:15784535).

Miscellaneous

TibA-mediated aggregation is blocked upon capsule expression and fimbriation and is sensitive to pH extremes.

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 Componentcell outer membrane
Biological Processcell adhesion

Keywords

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Autotransporter adhesin/invasin TibA

Gene names

    • Name
      tibA
    • Ordered locus names
      ETEC_2141

Organism names

Accessions

  • Primary accession
    Q9XD84
  • Secondary accessions
    • E3PBM3

Subcellular Location

Cell outer membrane
; Multi-pass membrane protein

Keywords

PTM/Processing

Features

Showing features for signal, chain, glycosylation.

TypeIDPosition(s)Description
Signal1-54
ChainPRO_000038758455-989Autotransporter adhesin/invasin TibA
Glycosylation74O-alpha-linked (D-glycero-D-manno-heptose) serine
Glycosylation86O-alpha-linked (D-glycero-D-manno-heptose) serine
Glycosylation93O-alpha-linked (D-glycero-D-manno-heptose) serine
Glycosylation94O-alpha-linked (D-glycero-D-manno-heptose) serine
Glycosylation97O-alpha-linked (D-glycero-D-manno-heptose) serine
Glycosylation100O-alpha-linked (D-glycero-D-manno-heptose) serine
Glycosylation112O-alpha-linked (D-glycero-D-manno-heptose) serine
Glycosylation113O-alpha-linked (D-glycero-D-manno-heptose) serine
Glycosylation116O-alpha-linked (D-glycero-D-manno-heptose) serine
Glycosylation119O-alpha-linked (D-glycero-D-manno-heptose) serine
Glycosylation124O-alpha-linked (D-glycero-D-manno-heptose) serine
Glycosylation131O-alpha-linked (D-glycero-D-manno-heptose) serine
Glycosylation132O-alpha-linked (D-glycero-D-manno-heptose) serine
Glycosylation135O-alpha-linked (D-glycero-D-manno-heptose) serine
Glycosylation151O-alpha-linked (D-glycero-D-manno-heptose) serine
Glycosylation154O-alpha-linked (D-glycero-D-manno-heptose) serine
Glycosylation162O-alpha-linked (D-glycero-D-manno-heptose) serine
Glycosylation170O-alpha-linked (D-glycero-D-manno-heptose) serine
Glycosylation176O-alpha-linked (D-glycero-D-manno-heptose) serine
Glycosylation181O-alpha-linked (D-glycero-D-manno-heptose) serine
Glycosylation188O-alpha-linked (D-glycero-D-manno-heptose) serine
Glycosylation189O-alpha-linked (D-glycero-D-manno-heptose) serine
Glycosylation200O-alpha-linked (D-glycero-D-manno-heptose) serine
Glycosylation226O-alpha-linked (D-glycero-D-manno-heptose) serine
Glycosylation227O-alpha-linked (D-glycero-D-manno-heptose) serine
Glycosylation230O-alpha-linked (D-glycero-D-manno-heptose) serine
Glycosylation238O-alpha-linked (D-glycero-D-manno-heptose) serine
Glycosylation248O-alpha-linked (D-glycero-D-manno-heptose) serine
Glycosylation263O-alpha-linked (D-glycero-D-manno-heptose) serine
Glycosylation264O-alpha-linked (D-glycero-D-manno-heptose) serine
Glycosylation275O-alpha-linked (D-glycero-D-manno-heptose) serine
Glycosylation294O-alpha-linked (D-glycero-D-manno-heptose) serine
Glycosylation305O-alpha-linked (D-glycero-D-manno-heptose) serine
Glycosylation313O-alpha-linked (D-glycero-D-manno-heptose) serine
Glycosylation322O-alpha-linked (D-glycero-D-manno-heptose) serine

Post-translational modification

Glycosylated by TibC (PubMed:10417177, PubMed:15784535, PubMed:25211077, PubMed:25310236).
Glycosylation is required for adhesion to and invasion of host cells (PubMed:15784535).
Glycosylation is dispensable for bacterial autoaggregation and biofilm formation (PubMed:15784535).

Keywords

PTM databases

Interaction

Subunit

Homohexamer.

Family & Domains

Features

Showing features for repeat, region, domain.

TypeIDPosition(s)Description
Repeat82-1001-1
Region82-30812 X 19 AA approximate repeats
Repeat101-1191-2
Region110-146Disordered
Repeat120-1381-3
Repeat139-1571-4
Repeat158-1761-5
Repeat177-1951-6
Repeat196-2141-7
Repeat215-2331-8
Repeat234-2511-9
Repeat252-2701-10
Repeat271-2891-11
Repeat290-3081-12
Region623-686Disordered
Repeat639-6432-1
Region639-6788 X 5 AA repeats of P-[DG]-[AGT]-[DGA]-[NKT]
Repeat644-6482-2
Repeat649-6532-3
Repeat654-6582-4
Repeat659-6632-5
Repeat664-6682-6
Repeat669-6732-7
Repeat674-6782-8
Domain721-989Autotransporter

Domain

The signal peptide, cleaved at the inner membrane, guides the autotransporter protein to the periplasmic space (By similarity).
Then, insertion of the C-terminal translocator domain (or beta-domain) in the outer membrane forms a hydrophilic pore for the translocation of the passenger domain to the bacterial cell surface (By similarity).
Unlike autotransporter AIDA-I, appears that there is no cleavage between the N-terminus and the C-terminus translocator domain (Probable)

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    989
  • Mass (Da)
    101,112
  • Last updated
    1999-11-01 v1
  • Checksum
    6A925466416E63BE
MNKVYNTVWNESTGTWVVTSELTRKGGLRPRQIKRTVLAGLIAGLLMPSMPALAAAYDNQTIGRGETSKSMHLSAGDTAKNTTINSGGKQYVSSGGSATSTTINIGGVQHVSSGGSATSSTINSGGHQHVSSGGSATNTTVNNGGRQTVFSGGSAMGTIINSGGDQYVISGGSATSASVTSGARQFVSSGGIVKATSVNSGGRQYVRDGGSATDTVLNNTGRQFVSSGGSAAKTTINSGGGMYLYGGSATGTSIYNGGRQYVSSGGSATNTTVYSGGRQHVYIDGNVTETTITSGGMLQVEAGGSASKVIQNSGGAVITNTSAAVSGTNDNGSFSIAGGSAVNMLLENGGYLTVFDGHQASDTMVGSDGTLDVRSGGVLYGTTTLTDKGALVGDVVTNEGNLYYLNNSTATFTGTLTGTGTLTQEGGNTRFSGLLSQDGGIFLQSGGAMTMDALQAKANVTTQSGTTLTLDNGTILTGNVAGDSTGAGDMAVKGASVWHLDGDSTVGALTLDNGTVDFRPSTTTRMTPAFQAVSLALGSLSGSGTFQMNTDIASHTGDMLNVAGNASGNFVLDIKNTGLEPVSAGAPLQVVQTGGGDAAFTLKGGKVDAGTWEYGLSKENTNWYLKADTPPPVTPPTNPDADNPDAGNPDAGNPDAGNPDAGNPDAGKPGTGKPDAGTSSSPVRRTTKSVDAVLGMATAPAYVFNSELDNLRFRHGDVMQNTRAPGGVWGRYTGSDNRISGGASSGYTLTQNGFETGADMVFDLSDSSLAVGTFFSYSDNSIKHARGGKSNVDSSGGGLYATWFDNDGYYVDGVLKYNRFNNELRTWMSDGTAVKGDYSQNGFGGSLEAGRTFSLNENAWAQPYVRTTAFRADKKEIRLNNGMKASIGATKSLQAEAGLKLGMTLDVAGKEVKPYLSAAVSHEFSDNNKVRINDTYDFRNDISGTTGKYGLGVNAQLTPNAGVWAEARYENGKQTESPITGGVGFRINF

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF109215
EMBL· GenBank· DDBJ
AAD41751.1
EMBL· GenBank· DDBJ
Genomic DNA
FN649414
EMBL· GenBank· DDBJ
CBJ01643.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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