Q9XD84 · TIBA_ECOH1
- ProteinAutotransporter adhesin/invasin TibA
- GenetibA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids989 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
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).
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 annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cell outer membrane | |
Biological Process | cell adhesion |
Keywords
- Biological process
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameAutotransporter adhesin/invasin TibA
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionQ9XD84
- Secondary accessions
Subcellular Location
UniProt Annotation
GO Annotation
Cell outer membrane ; Multi-pass membrane protein
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-54 | |||||
Sequence: MNKVYNTVWNESTGTWVVTSELTRKGGLRPRQIKRTVLAGLIAGLLMPSMPALA | ||||||
Chain | PRO_0000387584 | 55-989 | Autotransporter adhesin/invasin TibA | |||
Sequence: AAYDNQTIGRGETSKSMHLSAGDTAKNTTINSGGKQYVSSGGSATSTTINIGGVQHVSSGGSATSSTINSGGHQHVSSGGSATNTTVNNGGRQTVFSGGSAMGTIINSGGDQYVISGGSATSASVTSGARQFVSSGGIVKATSVNSGGRQYVRDGGSATDTVLNNTGRQFVSSGGSAAKTTINSGGGMYLYGGSATGTSIYNGGRQYVSSGGSATNTTVYSGGRQHVYIDGNVTETTITSGGMLQVEAGGSASKVIQNSGGAVITNTSAAVSGTNDNGSFSIAGGSAVNMLLENGGYLTVFDGHQASDTMVGSDGTLDVRSGGVLYGTTTLTDKGALVGDVVTNEGNLYYLNNSTATFTGTLTGTGTLTQEGGNTRFSGLLSQDGGIFLQSGGAMTMDALQAKANVTTQSGTTLTLDNGTILTGNVAGDSTGAGDMAVKGASVWHLDGDSTVGALTLDNGTVDFRPSTTTRMTPAFQAVSLALGSLSGSGTFQMNTDIASHTGDMLNVAGNASGNFVLDIKNTGLEPVSAGAPLQVVQTGGGDAAFTLKGGKVDAGTWEYGLSKENTNWYLKADTPPPVTPPTNPDADNPDAGNPDAGNPDAGNPDAGNPDAGKPGTGKPDAGTSSSPVRRTTKSVDAVLGMATAPAYVFNSELDNLRFRHGDVMQNTRAPGGVWGRYTGSDNRISGGASSGYTLTQNGFETGADMVFDLSDSSLAVGTFFSYSDNSIKHARGGKSNVDSSGGGLYATWFDNDGYYVDGVLKYNRFNNELRTWMSDGTAVKGDYSQNGFGGSLEAGRTFSLNENAWAQPYVRTTAFRADKKEIRLNNGMKASIGATKSLQAEAGLKLGMTLDVAGKEVKPYLSAAVSHEFSDNNKVRINDTYDFRNDISGTTGKYGLGVNAQLTPNAGVWAEARYENGKQTESPITGGVGFRINF | ||||||
Glycosylation | 74 | O-alpha-linked (D-glycero-D-manno-heptose) serine | ||||
Sequence: S | ||||||
Glycosylation | 86 | O-alpha-linked (D-glycero-D-manno-heptose) serine | ||||
Sequence: S | ||||||
Glycosylation | 93 | O-alpha-linked (D-glycero-D-manno-heptose) serine | ||||
Sequence: S | ||||||
Glycosylation | 94 | O-alpha-linked (D-glycero-D-manno-heptose) serine | ||||
Sequence: S | ||||||
Glycosylation | 97 | O-alpha-linked (D-glycero-D-manno-heptose) serine | ||||
Sequence: S | ||||||
Glycosylation | 100 | O-alpha-linked (D-glycero-D-manno-heptose) serine | ||||
Sequence: S | ||||||
Glycosylation | 112 | O-alpha-linked (D-glycero-D-manno-heptose) serine | ||||
Sequence: S | ||||||
Glycosylation | 113 | O-alpha-linked (D-glycero-D-manno-heptose) serine | ||||
Sequence: S | ||||||
Glycosylation | 116 | O-alpha-linked (D-glycero-D-manno-heptose) serine | ||||
Sequence: S | ||||||
Glycosylation | 119 | O-alpha-linked (D-glycero-D-manno-heptose) serine | ||||
Sequence: S | ||||||
Glycosylation | 124 | O-alpha-linked (D-glycero-D-manno-heptose) serine | ||||
Sequence: S | ||||||
Glycosylation | 131 | O-alpha-linked (D-glycero-D-manno-heptose) serine | ||||
Sequence: S | ||||||
Glycosylation | 132 | O-alpha-linked (D-glycero-D-manno-heptose) serine | ||||
Sequence: S | ||||||
Glycosylation | 135 | O-alpha-linked (D-glycero-D-manno-heptose) serine | ||||
Sequence: S | ||||||
Glycosylation | 151 | O-alpha-linked (D-glycero-D-manno-heptose) serine | ||||
Sequence: S | ||||||
Glycosylation | 154 | O-alpha-linked (D-glycero-D-manno-heptose) serine | ||||
Sequence: S | ||||||
Glycosylation | 162 | O-alpha-linked (D-glycero-D-manno-heptose) serine | ||||
Sequence: S | ||||||
Glycosylation | 170 | O-alpha-linked (D-glycero-D-manno-heptose) serine | ||||
Sequence: S | ||||||
Glycosylation | 176 | O-alpha-linked (D-glycero-D-manno-heptose) serine | ||||
Sequence: S | ||||||
Glycosylation | 181 | O-alpha-linked (D-glycero-D-manno-heptose) serine | ||||
Sequence: S | ||||||
Glycosylation | 188 | O-alpha-linked (D-glycero-D-manno-heptose) serine | ||||
Sequence: S | ||||||
Glycosylation | 189 | O-alpha-linked (D-glycero-D-manno-heptose) serine | ||||
Sequence: S | ||||||
Glycosylation | 200 | O-alpha-linked (D-glycero-D-manno-heptose) serine | ||||
Sequence: S | ||||||
Glycosylation | 226 | O-alpha-linked (D-glycero-D-manno-heptose) serine | ||||
Sequence: S | ||||||
Glycosylation | 227 | O-alpha-linked (D-glycero-D-manno-heptose) serine | ||||
Sequence: S | ||||||
Glycosylation | 230 | O-alpha-linked (D-glycero-D-manno-heptose) serine | ||||
Sequence: S | ||||||
Glycosylation | 238 | O-alpha-linked (D-glycero-D-manno-heptose) serine | ||||
Sequence: S | ||||||
Glycosylation | 248 | O-alpha-linked (D-glycero-D-manno-heptose) serine | ||||
Sequence: S | ||||||
Glycosylation | 263 | O-alpha-linked (D-glycero-D-manno-heptose) serine | ||||
Sequence: S | ||||||
Glycosylation | 264 | O-alpha-linked (D-glycero-D-manno-heptose) serine | ||||
Sequence: S | ||||||
Glycosylation | 275 | O-alpha-linked (D-glycero-D-manno-heptose) serine | ||||
Sequence: S | ||||||
Glycosylation | 294 | O-alpha-linked (D-glycero-D-manno-heptose) serine | ||||
Sequence: S | ||||||
Glycosylation | 305 | O-alpha-linked (D-glycero-D-manno-heptose) serine | ||||
Sequence: S | ||||||
Glycosylation | 313 | O-alpha-linked (D-glycero-D-manno-heptose) serine | ||||
Sequence: S | ||||||
Glycosylation | 322 | O-alpha-linked (D-glycero-D-manno-heptose) serine | ||||
Sequence: S |
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).
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
PTM databases
Interaction
Subunit
Homohexamer.
Structure
Family & Domains
Features
Showing features for repeat, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 82-100 | 1-1 | ||||
Sequence: TTINSGGKQYVSSGGSATS | ||||||
Region | 82-308 | 12 X 19 AA approximate repeats | ||||
Sequence: TTINSGGKQYVSSGGSATSTTINIGGVQHVSSGGSATSSTINSGGHQHVSSGGSATNTTVNNGGRQTVFSGGSAMGTIINSGGDQYVISGGSATSASVTSGARQFVSSGGIVKATSVNSGGRQYVRDGGSATDTVLNNTGRQFVSSGGSAAKTTINSGGGMYLYGGSATGTSIYNGGRQYVSSGGSATNTTVYSGGRQHVYIDGNVTETTITSGGMLQVEAGGSASK | ||||||
Repeat | 101-119 | 1-2 | ||||
Sequence: TTINIGGVQHVSSGGSATS | ||||||
Region | 110-146 | Disordered | ||||
Sequence: HVSSGGSATSSTINSGGHQHVSSGGSATNTTVNNGGR | ||||||
Repeat | 120-138 | 1-3 | ||||
Sequence: STINSGGHQHVSSGGSATN | ||||||
Repeat | 139-157 | 1-4 | ||||
Sequence: TTVNNGGRQTVFSGGSAMG | ||||||
Repeat | 158-176 | 1-5 | ||||
Sequence: TIINSGGDQYVISGGSATS | ||||||
Repeat | 177-195 | 1-6 | ||||
Sequence: ASVTSGARQFVSSGGIVKA | ||||||
Repeat | 196-214 | 1-7 | ||||
Sequence: TSVNSGGRQYVRDGGSATD | ||||||
Repeat | 215-233 | 1-8 | ||||
Sequence: TVLNNTGRQFVSSGGSAAK | ||||||
Repeat | 234-251 | 1-9 | ||||
Sequence: TTINSGGGMYLYGGSATG | ||||||
Repeat | 252-270 | 1-10 | ||||
Sequence: TSIYNGGRQYVSSGGSATN | ||||||
Repeat | 271-289 | 1-11 | ||||
Sequence: TTVYSGGRQHVYIDGNVTE | ||||||
Repeat | 290-308 | 1-12 | ||||
Sequence: TTITSGGMLQVEAGGSASK | ||||||
Region | 623-686 | Disordered | ||||
Sequence: WYLKADTPPPVTPPTNPDADNPDAGNPDAGNPDAGNPDAGNPDAGKPGTGKPDAGTSSSPVRRT | ||||||
Repeat | 639-643 | 2-1 | ||||
Sequence: PDADN | ||||||
Region | 639-678 | 8 X 5 AA repeats of P-[DG]-[AGT]-[DGA]-[NKT] | ||||
Sequence: PDADNPDAGNPDAGNPDAGNPDAGNPDAGKPGTGKPDAGT | ||||||
Repeat | 644-648 | 2-2 | ||||
Sequence: PDAGN | ||||||
Repeat | 649-653 | 2-3 | ||||
Sequence: PDAGN | ||||||
Repeat | 654-658 | 2-4 | ||||
Sequence: PDAGN | ||||||
Repeat | 659-663 | 2-5 | ||||
Sequence: PDAGN | ||||||
Repeat | 664-668 | 2-6 | ||||
Sequence: PDAGK | ||||||
Repeat | 669-673 | 2-7 | ||||
Sequence: PGTGK | ||||||
Repeat | 674-678 | 2-8 | ||||
Sequence: PDAGT | ||||||
Domain | 721-989 | Autotransporter | ||||
Sequence: NTRAPGGVWGRYTGSDNRISGGASSGYTLTQNGFETGADMVFDLSDSSLAVGTFFSYSDNSIKHARGGKSNVDSSGGGLYATWFDNDGYYVDGVLKYNRFNNELRTWMSDGTAVKGDYSQNGFGGSLEAGRTFSLNENAWAQPYVRTTAFRADKKEIRLNNGMKASIGATKSLQAEAGLKLGMTLDVAGKEVKPYLSAAVSHEFSDNNKVRINDTYDFRNDISGTTGKYGLGVNAQLTPNAGVWAEARYENGKQTESPITGGVGFRINF |
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)
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
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length989
- Mass (Da)101,112
- Last updated1999-11-01 v1
- Checksum6A925466416E63BE
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF109215 EMBL· GenBank· DDBJ | AAD41751.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
FN649414 EMBL· GenBank· DDBJ | CBJ01643.1 EMBL· GenBank· DDBJ | Genomic DNA |