IED ID | IndEnz0002014383 |
Enzyme Type ID | protease014383 |
Protein Name |
Trimeric autotransporter adhesin AtaA TAA AtaA Type 5 secretion system autotransporter AtaA |
Gene Name | ataA |
Organism | Acinetobacter sp. (strain Tol 5) |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Moraxellales Moraxellaceae Acinetobacter unclassified Acinetobacter Acinetobacter sp. (strain Tol 5) |
Enzyme Sequence | MNKIYKVIWNATLLAWVAVSELAKGKTKSTTSKSKAKSLSSSVIVGGIILTTPLSLIAATVQVGGGTNSGTTATASTNCADLYNYQNPENSGSGAAGNYNAGNPSVCSIAIGENAQGGTSGTGGSPGIAIGGNSKATGGLSVAIGGYAQATNVGSIALGTAALSSGFNSLAISRQAAATNNYSIAIGTTSVSKGVGSIAMGHSTNASGDQSIAIGSSDAVNSATATTTYDGTTNTQASGSKSIAIGASAKASTNNSIALGAGSVTSAQSGNSYLTGVGASATNGVVSVGTSTATRRIQNVADGSAASDAVTVAQLDKAYDDTNGRLAAALGTGSGAAYNAANNTYTAPTNIGGTGKNTIDDAIKATQRSVVAGSNIVVTPTTASDGSISYSVATSATPTFTSITVNNAPTAGTDATNKTYVDSKAAASRTEVAAGSNVSGVVKTTGANGQDVYTVNANGTTASAGSSAVTVTPGTKDANNVTDYKVDLSATTKTDIQKGVDAKNAVDTAGLKFKGDTATTSNTKKLGDTVSITGDTNISTVATTDGVQVKLNPNLDLGATGSVKTGNTTINNAGVTADQVTVGGVVINNTSGINAGGKAITNVAAPTNNTDAANKKYVDDAGTALTNLGFGLKAQDGTTVNKKLGEAVDIVGSNSNISTKVNAGKVEVALSNTLDLGTTGSVTTGSTVINNAGVTATQVTANKVTINNAPTAGTDATNKTYVDSKAAASRTEVAAGSNVSGVVKTTGANGQDIYAVNANGTTASAGSSAVTVTPGTKDANNVTDYKVDLSATTKTDIQKGVDAKNAVDTAGLKFKGDTATTSNTKKLGDTVSITGDTNISTVATTDGVQVKLNPNLDLGATGSVKTGNTTINNAGVTADQVTVGGVVINNTSGINAGGKAITNVAAPTNNTDAANKKYVDDAGTALTNLGFGLKAQDGTTVNKKLGEAVDIVGSNSNISTKVNAGKVEVALSNTLDLGTTGSVTTGSTVINNAGVTATQVTANKVTVNNAPTAGTDATNKTYVDSKAAASRTEVAAGSNVSGVVKTTGANGQDVYTVNANGTTASAGSSAVTVTPGTKDANNVTDYKVDLSATTKTDIQKGVDAKNAVDTAGLKFKGDTATTSNTKKLGDTVSITGDTNISTVATTDGVQVKLNPNLDLGATGSVKTGNTTINNAGVTADQVTVGGVVINNTSGINAGGKAITNVAAPTNNTDAANKKYVDDAGTALTNLGFGLKAQDGTTVNKKLGEAVEVVGADSNITTKVAGGQVAIELNKNLNNLTGITVNDGTNGTNGSTVIGKDGISVKDGSGNTIAGVDNTALTVKDGSGNTETSINQAINTLNAAQGETDKFAVKYDKNADGSVNYNNITLAGTTASSTQDATTGKITTTGGTSLNNVASAGDYKDVANASKGVNAGDLNNAVVDATNAATSKGFALQAADGAKVQKNLGEAVEVVGADSNITTKVAGGQVAIELNKNLNNLTGITVNDGTNGTNGSTVIGKDGISVKDGSGNTIAGVDNTALTVKDGSGNTETSINQAINTLNAAQGETDKFAVKYDKNTDGSTNYNSITAGNGNGTAATIGTDTAGNSVVTSGGTKISNVANGVNASDAVNKGQLDSLSTGLTNTGFGLKAADGNTVNKKLGEAVDVVGADSNITTKVAGGQVAIELNKNLNNLTGITVNDGTNGTNGSTVIGKDGISIKDGSGNTIAGVDNTALTVKDGSGNTETSINQAINTLNAAQGETDKFAVKYDKNADGSANYNNITLAGTTASSTQDATTGKITTTGGTSLNNVASAGDYKDVANASKGVNAGDLNNAVVDATNAATSKGFALQAADGAKVQKNLGEAVEVVGADSNITTKVVGGQVAIELNKNLNNLTGITVNDGTNGTNGSTVIGKDGISVKDGSGNTIAGVDNTALTVKDGSGNTETSINQAINTLNAAQGETDKFAVKYDKNADGSVNYNNITLAGTTASSTQDATTGKITTTGGTSLNNVASAGDYKDVANASKGVNAGDLNNAVVDATNAATSKGFALQAADGAKVQKNLGEAVEVVGADSNITTKVAGGQVAIELNKNLNNLTGITVNDGTNGTNGSTVIGKDGISVKDGSGNTIAGVDNTALTVKDGSGNTETSINQAINTLNAAQGETDKFAVKYDKNADGSVNYNNITLAGTTASSTQDATTGKITTTGGTSLNNVASAGDYKDVANASKGVNAGDLNNAVVDATNAATSKGFALQAADGAKVQKNLGEAVEVVGADSNITTKVAGGQVAIELNKNLNNLTGITVNDGTNGTNGSTVIGKDGISVKDGSGNTIAGVDNTALTVKDGSGNTETSINQAINTLNAAQGETDKFAVKYDKNADGSANYNNVTLAGTNGTIISNVKAGAVTSTSTDAINGSQLYGVANSVKNAIGGSTTIDATTGAITTTNIGGTGSNTIDGAISSIKDSATKAKTTVSAGDNVVVTSGTNADGSTNYEVATAKDVNFDKVTVGSVVVDKSSNTIKGLSNTTWNGTAVSGQAATEDQLKTVSDAQGETDKFAVKYDKNADGSANYNSITAGNGNGTAATIGTDTAGNSVVTSGGTKISNVANGVNASDAVNKGQLDSLSTGLTNTGFGLKAADGNTVNKKLGEAVDVVGADSNITTKVAGGQVAIELNKNLNNLTGITVNDGTNGTNGSTVIGKDGISIKDGSGNTIAGVDNTALTVKDSSGNTETSINQAINTLNAAQGETDKFAVKYDKNADGSVNYNNVTLAGTNGTIIRNVKAGAVTSTSTDAINGSQLYDIANSVKNAIGGSTTRDVTTGAITTTNIGGTGSNTIDGAISSIKDSATKAKTTISAGDNVVVTSGTNADGSTNYEVATAKDVNFDKVTVGNVVVDKANDTIQGLSNKDLNSTDFATKGRAATEEQLKAVITSNITEVVDGNGNKVNIIDQVVNTKPDNKNQDSLFLTYDKQGQETTDRLTIGQTVQKMNTDGIKFFHTNADTSKGDLGTTNDSSAGGLNSTAIGVNAIVANGADSSVALGHNTKVNGKQSIAIGSGAEALGNQSISIGTGNKVTGDHSGAIGDPTIVNGANSYSVGNNNQVLTDDTFVLGNNVTKTIAGSVVLGNGSAATTGAGEAGYALSVATNADKAAITKTTSSTGAVAVGDASSGIYRQITGVAAGSVDSDAVNVAQLKAVGNQVVTTQTTLVNSLGGNAKVNADGTITGPTYNVAQGNQTNVGDALTALDNAINTAATTSKSTVSNGQNIVVSKSKNADGSDNYEVSTAKDLTVDSVKAGDTVLNNAGITIGNNAVVLNNTGLTISGGPSVTLAGIDAGNKTIQNVANAVNATDAVNKGQLDSAINNVNNNVNELANNAVKYDDASKDKITLGGGATGTTITNVKDGTVAQGSKDAVNGGQLWNVQQQVDQNTTDISNIKNDINNGTVGLVQQAGKDAPVTVAKDTGGTTVNVAGTDGNRVVTGVKEGAVNATSKDAVNGSQLNTTNQAVVNYLGGGAGYDNITGSFTAPSYTVGDSKYNNVGGAIDALNQADQALNSKIDNVSNKLDNAFRITNNRIDDVEKKANAGIAAAMALESAPYVPGKYTYAAGAAYHGGENAVGVTLRKTADNGRWSITGGVAAASQGDASVRIGISGVID |
Enzyme Length | 3630 |
Uniprot Accession Number | K7ZP88 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | |
Enzyme Function | FUNCTION: Responsible for autoagglutination, and for adhesion to abiotic and biotic surfaces such as polystyrene (PS), type I collagen, polypropylene (PP), polyvinylchloride (PVC), glass and stainless steel (SS). Adhesion is much stronger than that mediated by Yersinia YadA in a comparative assay. Confers autoagglutination and binding to PS, type I collagen, PP, PVC, glass and SS upon expression in Acinetobacter baylyi strain ADP1 (PubMed:23155410). Involved in rapid, irreversible adherence to polyurethane (PubMed:17090933). Forms an unusual biofilm (PubMed:31972092). An extended, surface exposed fiber binds to quartz crystals, PS and glass. It can be removed by washing in distilled water (PubMed:27305955, PubMed:28720107). {ECO:0000269|PubMed:17090933, ECO:0000269|PubMed:23155410, ECO:0000269|PubMed:27305955, ECO:0000269|PubMed:28720107, ECO:0000269|PubMed:31972092}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Beta strand (40); Chain (1); Helix (12); Mutagenesis (5); Region (7); Signal peptide (1); Transmembrane (4); Turn (2) |
Keywords | 3D-structure;Cell adhesion;Cell outer membrane;Membrane;Protein transport;Signal;Transmembrane;Transmembrane beta strand;Transport |
Interact With | |
Induction | INDUCTION: Part of the ataA-tpgA operon. {ECO:0000269|PubMed:27074146}. |
Subcellular Location | SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:23155410, ECO:0000269|PubMed:27074146, ECO:0000269|PubMed:27305955}. Cell outer membrane {ECO:0000269|PubMed:23155410, ECO:0000269|PubMed:27074146}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A1JUB7}. Note=Localizes to thin, peritrichate nanofibers (200 nm long, 3.5 nm diameter) on the cell surface; an antibody against residues 699-1014 only labels the distal tip of these fibers (PubMed:23155410, PubMed:27074146). The C-terminal translocator domain is probably localized in the outer membrane (Probable). {ECO:0000269|PubMed:23155410, ECO:0000269|PubMed:27074146, ECO:0000305|PubMed:23155410}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000255 |
Structure 3D | X-ray crystallography (6) |
Cross Reference PDB | 3WP8; 3WPA; 3WPO; 3WPP; 3WPR; 3WQA; |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 359,309 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |