| IED ID | IndEnz0002004637 |
| Enzyme Type ID | protease004637 |
| Protein Name |
Major fimbrium subunit FimA type-1 Fimbrillin Fimbrilin Major fimbrial subunit protein type I |
| Gene Name | fimA PGN_0180 |
| Organism | Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561) |
| Taxonomic Lineage | cellular organisms Bacteria FCB group Bacteroidetes/Chlorobi group Bacteroidetes Bacteroidia Bacteroidales Porphyromonadaceae Porphyromonas Porphyromonas gingivalis Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561) |
| Enzyme Sequence | MKKTKFFLLGLAALAMTACNKDNEAEPVTEGNATISVVLKTSNSNRAFGVGDDESKVAKLTVMVYNGEQQEAIKSAENATKVEDIKCSAGQRTLVVMANTGAMELVGKTLAEVKALTTELTAENQEAAGLIMTAEPKTIVLKAGKNYIGYSGTGEGNHIENDPLKIKRVHARMAFTEIKVQMSAAYDNIYTFVPEKIYGLIAKKQSNLFGATLVNADANYLTGSLTTFNGAYTPANYANVPWLSRNYVAPAADAPQGFYVLENDYSANGGTIHPTILCVYGKLQKNGADLAGADLAAAQAANWVDAEGKTYYPVLVNFNSNNYTYDSNYTPKNKIERNHKYDIKLTITGPGTNNPENPITESAHLNVQCTVAEWVLVGQNATW |
| Enzyme Length | 383 |
| Uniprot Accession Number | B2RH54 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Structural subunit of the major fimbriae. These long, filamentous pili are attached to the cell surface; they mediate biofilm formation, adhesion onto host cells and onto other bacteria that are part of the oral microbiome (PubMed:9786913, PubMed:12593606, PubMed:15165251, PubMed:17675496, PubMed:17526848, PubMed:20530728, PubMed:27062925). They play an important role in the invasion of periodontal tissues (PubMed:12593606). Fimbriae and their constituents are major virulence factors. FimA proteins from different strains have highly divergent sequences, and this has been used for classification (PubMed:23809984). The sequence-based classification correlates with pathogenicity (PubMed:17675496). {ECO:0000269|PubMed:12593606, ECO:0000269|PubMed:15165251, ECO:0000269|PubMed:17526848, ECO:0000269|PubMed:17675496, ECO:0000269|PubMed:20530728, ECO:0000269|PubMed:23809984, ECO:0000269|PubMed:27062925, ECO:0000269|PubMed:9786913}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (24); Chain (1); Erroneous initiation (1); Helix (6); Lipidation (2); Mutagenesis (3); Propeptide (1); Region (1); Signal peptide (1); Site (1); Turn (1) |
| Keywords | 3D-structure;Cell adhesion;Cell outer membrane;Direct protein sequencing;Fimbrium;Lipoprotein;Membrane;Palmitate;Signal;Virulence |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Fimbrium {ECO:0000269|PubMed:15165251, ECO:0000269|PubMed:17526848, ECO:0000269|PubMed:17675496, ECO:0000269|PubMed:20530728, ECO:0000269|PubMed:9786913}. Cell outer membrane {ECO:0000269|PubMed:15165251}. Note=Synthesized as palmitoylated precursor. The lipidated propeptide is removed during processing to the mature protein. {ECO:0000269|PubMed:15165251}. |
| Modified Residue | |
| Post Translational Modification | PTM: Synthesized as palmitoylated precursor (PubMed:15165251). Efficient export to the outer membrane and integration into fimbriae requires lipidation and subsequent proteolytic removal of the lipidated propeptide (PubMed:8778568, PubMed:9786913, PubMed:15165251). {ECO:0000269|PubMed:15165251, ECO:0000269|PubMed:8778568, ECO:0000269|PubMed:9786913}. |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255|PROSITE-ProRule:PRU00303 |
| Structure 3D | Electron microscopy (1); X-ray crystallography (1) |
| Cross Reference PDB | 6JZK; 6KMF; |
| Mapped Pubmed ID | 32284566; |
| Motif | |
| Gene Encoded By | |
| Mass | 41,367 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |