Protein Family Models

This entry represents a bacterial Ig-fold domain that is found in a wide range of bacterial cell surface adherence proteins. [1]. 21280131. Crystal structure of the functional region of Uro-adherence factor A from Staphylococcus saprophyticus reveals participation of the B domain in ligand binding. Matsuoka E, Tanaka Y, Kuroda M, Shouji Y, Ohta T, Tanaka I, Yao M;. Protein Sci. 2011;20:406-416. [2]. 19043557. A structural model of the Staphylococcus aureus ClfA-fibrinogen interaction opens new avenues for the design of anti-staphylococcal therapeutics. Ganesh VK, Rivera JJ, Smeds E, Ko YP, Bowden MG, Wann ER, Gurusiddappa S, Fitzgerald JR, Hook M;. PLoS Pathog. 2008;4:e1000226. [3]. 17392280. The Enterococcus faecalis MSCRAMM ACE binds its ligand by the Collagen Hug model. Liu Q, Ponnuraj K, Xu Y, Ganesh VK, Sillanpaa J, Murray BE, Narayana SV, Hook M;. J Biol Chem. 2007;282:19629-19637. [4]. 24627488. Evidence for steric regulation of fibrinogen binding to Staphylococcus aureus fibronectin-binding protein A (FnBPA). Stemberk V, Jones RP, Moroz O, Atkin KE, Edwards AM, Turkenburg JP, Leech AP, Massey RC, Potts JR;. J Biol Chem. 2014;289:12842-12851. (from Pfam)

Date:

2024-10-16

This is the C-terminal half of a bacterial fibrinogen-binding adhesin SdrG. SdrG is a Gram-positive cell-wall-anchored adhesin that allows attachment of the bacterium to host tissues via specific binding to the beta-chain of human fibrinogen (Fg). SdrG binds to its ligand with a dynamic "dock, lock, and latch" mechanism which represents a general mode of ligand-binding for structurally related cell wall-anchored proteins in most Gram-positive bacteria. The C-terminal part of SdrG(276-596) is integral to the folding of the immunoglobulin-like whole to create the docking grooves necessary for Fg binding. The domain is associated with families of Cna_B, Pfam:PF05738 [1]. [1]. 14567919. A "dock, lock, and latch" structural model for a staphylococcal adhesin binding to fibrinogen. Ponnuraj K, Bowden MG, Davis S, Gurusiddappa S, Moore D, Choe D, Xu Y, Hook M, Narayana SV;. Cell. 2003;115:217-228. (from Pfam)

Date:

2024-10-16

Many surface proteins found in Streptococcus, Staphylococcus, and related lineages share apparently homologous signal sequences. A motif resembling [YF]SIRKxxxGxxS[VIA] appears at the start of the transmembrane domain. The GxxS motif appears perfectly conserved, suggesting a specific function and not just homology. There is a strong correlation between proteins carrying this region at the N-terminus and those carrying the Gram-positive anchor domain with the LPXTG sortase processing site at the C-terminus. (from Pfam)

Date:

2024-08-14

The ability of bacteria to bind fibronectin is thought to enable the colonisation of wound tissue and blood clots. The fibronectin binding repeat is found in bacterial fibronectin binding proteins and serum opacity factor. Bacterial fibronectin binding proteins are surface proteins that covalently link to the bacterial cell wall, mediate adherence of the bacteria to host cells [2] and trigger the fibronectin/integrin-mediated uptake of bacteria by host cells [3]. Each fibronectin binding repeat is an array of short motifs that bind to fibronectin type I domains [4]. Fibronectin binding repeats are natively unfolded in the absence of fibronectin and are thought to adopt a well-defined conformation (tandem beta-zipper) upon binding [5]. [1]. 7822031. DNA sequence of the serum opacity factor of group A streptococci: identification of a fibronectin-binding repeat domain. Rakonjac JV, Robbins JC, Fischetti VA;. Infect Immun 1995;63:622-631. [2]. 1386839. Fibronectin-binding protein of Streptococcus pyogenes: sequence of the binding domain involved in adherence of streptococci to epithelial cells. Talay SR, Valentin-Weigand P, Jerlstrom PG, Timmis KN, Chhatwal GS;. Infect Immun. 1992;60:3837-3844. [3]. 9822827. Roles of integrins and fibronectin in the entry of Streptococcus pyogenes into cells via protein F1. Ozeri V, Rosenshine I, Mosher DF, Fassler R, Hanski E;. Mol Microbiol. 1998;30:625-637. [4]. 15247227. High affinity streptococcal binding to human fibronectin requires specific recognition of sequential F1 modules. Schwarz-Linek U, Pilka ES, Pickford AR, Kim JH, Hook M, Campbell ID, Potts JR;. J Biol Chem. 2004;279:3901. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-10-16

The [YF]SIRKxxxGxxS type of signal peptide appears at the start of many proteins of Streptococcus, Staphylococcus, and Enterococcus, but not in other lineages such as Bacillus. Recent work in Staphylococcus aureus has shown that septal secretion (targeting to the crosswall in dividing cells) of the YSIRK-containing staphylococcal protein A depends on SecA, SecDF, and the lipoteichoic acid synthase LtaS, all of which co-purify when the motif is modified to YSIRKxxxGxxL to block processing.

Date:

2024-12-19