Literature summary for 2.3.2.18 extracted from

Ton-That, H.; Labischinski, H.; Berger-Bachi, B.; Schneewind, O.
Anchor structure of staphylococcal surface proteins. III. Role of the FemA, FemB, and FemX factors in anchoring surface proteins to the bacterial cell wall (1998), J. Biol. Chem., 273, 29143-29149.

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Protein Variants

Protein Variants	Comment	Organism
additional information	in strains carrying mutations of FemA, femAB, or the femAX genes, the sorting reaction of surface proteins is significantly slowed. Strains carrying mutations in the fem genes display a decreased rate of surface protein precursor cleavage as compared with the wildtype strains, suggesting that the altered cross-bridges slow the anchoring of surface proteins	Staphylococcus aureus

Organism

Organism	UniProt	Comment	Textmining
Staphylococcus aureus	-	-	-

General Information

General Information	Comment	Organism
physiological function	surface protein is linked to tri- and monoglycyl cross-bridges of peptidoglycan isolated from femB and femA mutant staphylococci, respectively. Peptidoglycan analysis of a femAB mutant strain reveals the presence of pentaglycyl, tetraglycyl-monoseryl, and monoglycyl as well as small amounts of triglycyl cross-bridges. Analysis of anchor peptides shows that surface proteins are mostly linked to tetraglycylmonoseryl as well as pentaglycyl. The sortase activity of Staphylococcus aureus prefers cross-bridges containing five residues, but altered cell-wall cross-bridges can be linked to the COOH-terminal end of surface proteins	Staphylococcus aureus

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Release 2023.1 (January 2023)