This bacterial family of proteins shows structural similarity to other pectin lyase families. Although structures from this family align with acetyl-transferases, there is no conservation of catalytic residues found. It is likely that the function is one of cell-adhesion. In PDB:3jx8, it is interesting to note that the sequence of contains several well defined sequence repeats, centred around GSG motifs defining the tight beta turn between the two sheets of the super-helix; there are 8 such repeats in the C-terminal half of the protein, which could be grouped into 4 repeats of two. It seems likely that this family belongs to the superfamily of trimeric auto-transporter adhesins (TAAs), which are important virulence factors in Gram-negative pathogens [[cite:PUB00029784]] [[cite:PUB00051306]]. In the case of Parabacteroides distasonis, which is a component of the normal distal human gut microbiota, TAA-like complexes probably modulate adherence to the host (information derived from TOPSAN).
","llm":false,"checked":false,"updated":false}],"wikipedia":[{"title":"Bacterial_adhesin","extract":"Bacterial adhesins are cell-surface components or appendages of bacteria that facilitate adhesion or adherence to other cells or to surfaces, usually in the host they are infecting or living in. Adhesins are a type of virulence factor.
","thumbnail":null}],"literature":{"PUB00029784":{"PMID":14765110,"ISBN":null,"volume":"23","issue":"4","year":2004,"title":"The Yersinia adhesin YadA collagen-binding domain structure is a novel left-handed parallel beta-roll.","URL":null,"raw_pages":"701-11","medline_journal":"EMBO J","ISO_journal":"EMBO J.","authors":["Nummelin H","Merckel MC","Leo JC","Lankinen H","Skurnik M","Goldman A."],"DOI_URL":"http://dx.doi.org/10.1038/sj.emboj.7600100"},"PUB00051306":{"PMID":18688279,"ISBN":null,"volume":"4","issue":"8","year":2008,"title":"Structure of the head of the Bartonella adhesin BadA.","URL":null,"raw_pages":"e1000119","medline_journal":"PLoS Pathog","ISO_journal":"PLoS Pathog.","authors":["Szczesny P","Linke D","Ursinus A","Bar K","Schwarz H","Riess TM","Kempf VA","Lupas AN","Martin J","Zeth K."],"DOI_URL":"http://dx.doi.org/10.1371/journal.ppat.1000119"}},"set_info":{"accession":"CL0268","name":"Pec_lyase-like"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":34,"interactions":0,"matches":11258,"pathways":0,"proteins":10865,"proteomes":3662,"sets":1,"structural_models":{"alphafold":7045},"structures":14,"taxa":5354},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":40,"alignment:full":6116},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"4opw","name":"Crystal structure of a putative adhesin (PARMER_02777) from Parabacteroides merdae ATCC 43184 at 1.75 A resolution"}}}