| IED ID | IndEnz0002005732 |
| Enzyme Type ID | protease005732 |
| Protein Name |
Type IV major fimbrial protein FimA 198 antigen Pilin Serogroup A1 |
| Gene Name | fimA |
| Organism | Dichelobacter nodosus (Bacteroides nodosus) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Cardiobacteriales Cardiobacteriaceae Dichelobacter Dichelobacter nodosus (Bacteroides nodosus) |
| Enzyme Sequence | MKSLQKGFTLIELMIVVAIIGILAAFAIPAYNDYIARSQAAEGLTLADGLKVRISDHLESGECKGDANPASGSLGNDDKGKYALATIDGDYNKDAKTADEKNGCKVVITYGQGTAGEKISKLIVGKKLVLDQFVNGSYKYNEGETDLELKFIPNAVKN |
| Enzyme Length | 158 |
| Uniprot Accession Number | P02975 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Major component of the type IV fimbriae that plays an essential role in twitching motility, natural transformation, and protease secretion. {ECO:0000250|UniProtKB:A5EWR9}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (5); Chain (1); Disulfide bond (1); Helix (4); Modified residue (1); Propeptide (1); Sequence conflict (3); Transmembrane (1); Turn (4) |
| Keywords | 3D-structure;Direct protein sequencing;Disulfide bond;Fimbrium;Membrane;Methylation;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Fimbrium {ECO:0000250|UniProtKB:A5EWR9}. Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. |
| Modified Residue | MOD_RES 8; /note="N-methylphenylalanine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01070, ECO:0000269|PubMed:6653780" |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 3SOK; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 16,863 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |