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 family corresponds to the B-like domain from the SdrD protein. This domain has three calcium binding sites within a greek key beta sandwich fold. (from Pfam)

Date:

2024-08-14

This HMM described a domain that is often repeated in pilins such as SpaA, and that often forms isopeptide bonds cross-linking amino acid side chains, giving the pilins added strength.

Date:

2024-10-16

Date:

2024-08-14

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

Date:

2024-08-14