title: SptP106-136 plays a role in the complex formation with SptP-specific chaperone SicP.
abstract: SptP is a virulence effector protein of Salmonella that is involved in bacterial invasion into a host cell. For effective secretion, SptP forms a complex with SptP-specific chaperone SicP through its chaperone-binding domain, residues 35-139. Here, we suggest the possibility that residues 106-136 of SptP are important for complex formation with SicP by in vitro reconstitution experiments.
authors.affiliation: a Division of Molecular Science, Faculty of Science and Technology , Gunma University , Kiryu , Japan.
authors.forename: Fumio
authors.initials: F
authors.lastname: Hayashi
authors.forename: Yurie
authors.initials: Y
authors.lastname: Kawashima
authors.forename: Shinobu
authors.initials: S
authors.lastname: Takeuchi
authors.forename: Kensuke
authors.initials: K
authors.lastname: Okimori
authors.forename: Eri
authors.initials: E
authors.lastname: Inobe
authors.forename: Kenji
authors.initials: K
authors.lastname: Oosawa
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D054884:Host-Pathogen Interactions; D006801:Humans; D018832:Molecular Chaperones / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D017027:Protein Tyrosine Phosphatases / Q000737:chemistry* / Q000378:metabolism; D012480:Salmonella Infections / Q000235:genetics / Q000382:microbiology*; D012486:Salmonella typhimurium / Q000737:chemistry* / Q000472:pathogenicity
chemical_list: D001426:Bacterial Proteins; D018832:Molecular Chaperones; D017027:Protein Tyrosine Phosphatases; C439890:sptP protein, Salmonella typhimurium
keywords: Salmonella; Type III secretion system; chaperone; effector; urea