Q8ZL64 · SADA_SALTY
- ProteinAutotransporter adhesin SadA
- GenesadA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1461 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Involved in cell aggregation, biofilm formation, and adhesion to human intestinal epithelial cells.
Miscellaneous
Immunization of mice with folded, full-length, purified SadA elicits an IgG response which provides limited protection against bacterial challenge.
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 | |
Cellular Component | cell surface | |
Biological Process | protein transport |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAutotransporter adhesin SadA
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Salmonella
Accessions
- Primary accessionQ8ZL64
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Note: The C-terminal translocator domain is localized in the outer membrane and the passenger domain is at the cell surface (By similarity).
Proper surface expression requires SadB (PubMed:24369174).
Proper surface expression requires SadB (PubMed:24369174).
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 1407-1417 | Beta stranded | ||||
Sequence: GANMTSIAGGT | ||||||
Transmembrane | 1421-1431 | Beta stranded | ||||
Sequence: ESAVAIGVSMV | ||||||
Transmembrane | 1440-1446 | Beta stranded | ||||
Sequence: KLQGTSN | ||||||
Transmembrane | 1450-1461 | Beta stranded | ||||
Sequence: DYSAAIGAGFQW |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
In vitro, loss of sadA does not affect cell aggregation, biofilm formation and adhesion to epithelial cells. Disruption does not affect the course of infection.
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-54 | |||||
Sequence: MNRIFKVLWNAATGTFVVTSETAKSRGKKNGRRKLAVSALIGLSSIMVSADALA | ||||||
Chain | PRO_0000437739 | 55-1461 | Autotransporter adhesin SadA | |||
Sequence: NAGNDTGDGVTPTGTQTGGKGWIAIGTDATANTYTNVDGASAAMGYKASAMGKWSTAIGSYSQSTGDSSLALGVKSVSAGDRAIAMGASSSASGSYSMAMGVYANSSGAKSVALGYKSVASGATSSALGYQATASGDDSAAFGNGAKAIGTNSVALGSGSVAQEDNSVAVGNSTTQRQITYVAKGDINSTSTDAVTGAQIYSLSQSVADRLGGGASVNSDGTVNAPLYEVGTGIYNNVGSALSALNTSITNTEASVAGLAEDALLWDESISAFSASHTGNASKITNLAAGTLAADSTDAVNGSQLFDTNEKVDKNTADIATNTGSINQNTADITANTDSINQNTTDIAANTTSINQNTTDIATNTTNINSLSDSVTTLTDDALLWDAASGAFSAKHNGSDSKITNLAAGTLAADSTDAVNGSQLFDTNEKVDQNTADITTNTNSINQNTTDIATNTTNINNLSDSITTLTDDALLWDAASGAFSANHNGSASKITNLAAGTLAADSTDAVNGSQLFATNENVSQNTADITTNTNSINQNTTDIATNTTSINNLSDSITTLTDDALLWDAASGTFSASRSGSASKITNLAAGTLAADSTDAVNGSQLYETNQKVDQNTSAIADINTSITNLSSDNLSWNETTSSFSASHGSSTTNKITNVAAGELSEESTDAVNGSQLFETNEKVDQNTTDIAANTTNITQNSTAIENLNTSVSDINTSITGLTDNALLWDEDTGAFSANHGGSTSKITNVAAGALSEDSTDAVNGSQLYETNQKVDQNTSAIADINTSITNLGTDALSWDDEEGAFSASHGTSGTNKITNVAAGEIASDSTDAVNGSQLYETNMLISQYNESISQLAGDTSETYITENGTGVKYIRTNDNGLEGQDAYATGNGATAVGYDAVASGAGSLALGQNSSSSIEGSIALGSGSTSNRAITTGIRETSATSDGVVIGYNTTDRELLGALSLGTDGESYRQITNVADGSEAQDAVTVRQLQNAIGAVTTTPTKYYHANSTEEDSLAVGTDSLAMGAKTIVNADAGIGIGLNTLVMADAINGIAIGSNARANHANSIAMGNGSQTTRGAQTDYTAYNMDTPQNSVGEFSVGSEDGQRQITNVAAGSADTDAVNVGQLKVTDAQVSRNTQSITNLNTQVSNLDTRVTNIENGIGDIVTTGSTKYFKTNTDGADANAQGADSVAIGSGSIAAAENSVALGTNSVADEANTVSVGSSTQQRRITNVAAGVNNTDAVNVAQLKASEAGSVRYETNADGSVNYSVLNLGDGSGGTTRIGNVSAAVNDTDAVNYAQLKRSVEEANTYTDQKMGEMNSKIKGVENKMSGGIASAMAMAGLPQAYAPGANMTSIAGGTFNGESAVAIGVSMVSESGGWVYKLQGTSNSQGDYSAAIGAGFQW |
Proteomic databases
Interaction
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 55-1372 | Surface exposed passenger domain | ||||
Sequence: NAGNDTGDGVTPTGTQTGGKGWIAIGTDATANTYTNVDGASAAMGYKASAMGKWSTAIGSYSQSTGDSSLALGVKSVSAGDRAIAMGASSSASGSYSMAMGVYANSSGAKSVALGYKSVASGATSSALGYQATASGDDSAAFGNGAKAIGTNSVALGSGSVAQEDNSVAVGNSTTQRQITYVAKGDINSTSTDAVTGAQIYSLSQSVADRLGGGASVNSDGTVNAPLYEVGTGIYNNVGSALSALNTSITNTEASVAGLAEDALLWDESISAFSASHTGNASKITNLAAGTLAADSTDAVNGSQLFDTNEKVDKNTADIATNTGSINQNTADITANTDSINQNTTDIAANTTSINQNTTDIATNTTNINSLSDSVTTLTDDALLWDAASGAFSAKHNGSDSKITNLAAGTLAADSTDAVNGSQLFDTNEKVDQNTADITTNTNSINQNTTDIATNTTNINNLSDSITTLTDDALLWDAASGAFSANHNGSASKITNLAAGTLAADSTDAVNGSQLFATNENVSQNTADITTNTNSINQNTTDIATNTTSINNLSDSITTLTDDALLWDAASGTFSASRSGSASKITNLAAGTLAADSTDAVNGSQLYETNQKVDQNTSAIADINTSITNLSSDNLSWNETTSSFSASHGSSTTNKITNVAAGELSEESTDAVNGSQLFETNEKVDQNTTDIAANTTNITQNSTAIENLNTSVSDINTSITGLTDNALLWDEDTGAFSANHGGSTSKITNVAAGALSEDSTDAVNGSQLYETNQKVDQNTSAIADINTSITNLGTDALSWDDEEGAFSASHGTSGTNKITNVAAGEIASDSTDAVNGSQLYETNMLISQYNESISQLAGDTSETYITENGTGVKYIRTNDNGLEGQDAYATGNGATAVGYDAVASGAGSLALGQNSSSSIEGSIALGSGSTSNRAITTGIRETSATSDGVVIGYNTTDRELLGALSLGTDGESYRQITNVADGSEAQDAVTVRQLQNAIGAVTTTPTKYYHANSTEEDSLAVGTDSLAMGAKTIVNADAGIGIGLNTLVMADAINGIAIGSNARANHANSIAMGNGSQTTRGAQTDYTAYNMDTPQNSVGEFSVGSEDGQRQITNVAAGSADTDAVNVGQLKVTDAQVSRNTQSITNLNTQVSNLDTRVTNIENGIGDIVTTGSTKYFKTNTDGADANAQGADSVAIGSGSIAAAENSVALGTNSVADEANTVSVGSSTQQRRITNVAAGVNNTDAVNVAQLKASEAGSVRYETNADGSVNYSVLNLGDGSGGTTRIGNVSAAVNDTDAVNYAQLKRSVEEANTYTDQK | ||||||
Region | 1373-1461 | Translocator domain | ||||
Sequence: MGEMNSKIKGVENKMSGGIASAMAMAGLPQAYAPGANMTSIAGGTFNGESAVAIGVSMVSESGGWVYKLQGTSNSQGDYSAAIGAGFQW |
Domain
The signal peptide, cleaved at the inner membrane, guides the autotransporter protein to the periplasmic space. Then, insertion of the C-terminal translocator domain in the outer membrane forms a hydrophilic pore for the translocation of the passenger domain to the bacterial cell surface (By similarity).
The surface exposed region contains four YadA-like head domains and extended stalk regions, multiply segmented by FGG, HANS, DALL and neck motifs (PubMed:23213248).
The surface exposed region contains four YadA-like head domains and extended stalk regions, multiply segmented by FGG, HANS, DALL and neck motifs (PubMed:23213248).
Sequence similarities
Belongs to the autotransporter-2 (AT-2) (TC 1.B.40) family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length1,461
- Mass (Da)147,838
- Last updated2002-03-01 v1
- Checksum91C59A87E7282254
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE006468 EMBL· GenBank· DDBJ | AAL22550.1 EMBL· GenBank· DDBJ | Genomic DNA |