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GW dipeptide domain-containing protein
This is a GW domain found in the C-terminal of InlB proteins which belong to the extended family of internalin proteins found in Listeria [1]. These 80 residue GW domains are unique to InlB among the internalins but are present in other proteins of Gram-positive bacteria [2]. GW domains (named after a GlyTryp dipeptide) are structurally and evolutionary related to SH3 domains [1]. Despite of this, GW domains are unlikely to act as functional mimics of SH3 domains since their potential proline-binding sites are blocked or destroyed [2]. They are highly basic and interact with poly-anions. The GW domains are responsible for the non-covalent attachment to the bacterial cell surface through binding to lipoteichoic acid. The GW domains alone do not stimulate uptake, but they synergize with the Met-binding internalin domain [1]. [1]. 21242015. Structural insights into Met receptor activation. Niemann HH;. Eur J Cell Biol. 2011;90:972-981. [2]. 12411480. GW domains of the Listeria monocytogenes invasion protein InlB are SH3-like and mediate binding to host ligands. Marino M, Banerjee M, Jonquieres R, Cossart P, Ghosh P;. EMBO J. 2002;21:5623-5634. (from Pfam)
glucosaminidase domain-containing protein
This family includes Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase EC:3.2.1.96. As well as the flageller protein J Swiss:P75942 that has been shown to hydrolyse peptidoglycan [1]. [1]. 10049388. Peptidoglycan-hydrolyzing activity of the FlgJ protein, essential for flagellar rod formation in Salmonella typhimurium. Nambu T, Minamino T, Macnab RM, Kutsukake K;. J Bacteriol 1999;181:1555-1561. (from Pfam)
glycoside hydrolase family 73 protein
glycoside hydrolase family 73 protein similar to Listeria monocytogenes virulence-associated peptidoglycan hydrolase Auto and Leuconostoc citreum atypical peptidoglycan hydrolase Mur
GW domain-containing glycosaminoglycan-binding protein
The GW domain of Listeria belongs to the clan of SH3-like domains. A similar but broader model (PF13457) occurs in Pfam. The GW domain occurs as repeats on surface proteins of the cell-invading pathogenic bacterium Listeria monocytogenes, and is involved in binding to glycosaminoglycans. Members of this family include the GW-type internalin InlB and several paralogs.
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