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Items: 1 to 20 of 32

1.

Cell surface antigen I/II C2 terminal domain

This is the second domain (C2) located in the C-terminal region found in antigen I/II type adhesin protein AspA from S. pyogenes. Together with C3, these two domains form an elongated structure, each domain adopts the DEv-IgG fold. Similar to the classical IgG folds, it is comprised of two major antiparallel beta-sheets, designated ABED and CFG. For the C2-domain, there are two additional strands on the CFG sheet. Furthermore, sheets ABED and CFG are interconnected by several cross-connecting loops and one alpha-helix (DH1). The side chains of D982 and N996 in the C2-domain are involved in hydrogen bonding with the side chains of R1264 and N1295 in the C3 domain. Main chain hydrogen bonding can also be observed between S992 in C2 and N1189/G1191 in C3, furthermore stabilizing the interaction between the domains. The C2 domain contains one bound metal ion, modeled as Ca2+, and both the C2- and C3-domains are stabilized by conserved isopeptide bonds, which connect the beta-sheets of the central DEv-IgG motifs [1].Other members of this family include Major cell-surface adhesin PAc from Streptococcus mutans and SspB from Streptococcus gordonii. [1]. 24918040. Structure of the C-terminal domain of AspA (antigen I/II-family). protein from Streptococcus pyogenes.. Hall M, Nylander S, Jenkinson HF, Persson K;. FEBS Open Bio. 2014;4:283-289. (from Pfam)

Date:
2024-08-14
Family Accession:
NF037164.5
Method:
HMM
2.

GbpC/Spa domain-containing protein

This domain is found in the Streptococcus Glucan-binding protein C (GbpC) and also in surface protein antigen (Spa)-family proteins which show sequence similarity to GbpC [1]. [1]. 9009329. Cloning and sequence analysis of the gbpC gene encoding a novel. glucan-binding protein of Streptococcus mutans.. Sato Y, Yamamoto Y, Kizaki H;. Infect Immun 1997;65:668-675. (from Pfam)

Date:
2024-08-14
Family Accession:
NF019962.5
Method:
HMM
3.

LPXTG cell wall anchor motif

Date:
2024-08-14
Family Accession:
NF012948.5
Method:
HMM
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