Open AccessRegion X, the cell‐wall‐attachment part of staphylococcal protein A
Author(s) -
GUSS Bengt,
UHLÉN Mathias,
NILSSON Björn,
LINDBERG Martin,
SJÖQUIST John,
SJÖDAHL Jörgen
Publication year - 1984
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1984.tb07931.x
Subject(s) - peptidoglycan , edman degradation , homology (biology) , peptide sequence , nucleic acid sequence , amino acid , sequence (biology) , biology , cell wall , protein sequencing , protein primary structure , staphylococcus aureus , sequence homology , sequence alignment , gene , genetics , biochemistry , bacteria
The sequence of region X of staphylococcal protein A has been determined. The hypothesis has been put forward that this region spans the Staphylococcus aureus cell wall and is responsible for the binding to the peptidoglycan. The primary amino acid sequence of region X was determined for two strains exhibiting cell‐wall‐bound protein A, Cowan I and 8325–4. The sequence determination of the Cowan I material is partial and was performed by Edman degradation, in contrast to the sequence of the 8325–4 material which was completely analyzed by nucleotide sequencing of the corresponding gene. The region consists of two structurally different domains, a highly repetitive region (X r ), with an octapeptide structure repeated approximately 12 times, and a C‐terminal domain (X c ) with an unique sequence. A comparison between the two strains reveals a high mutual homology as well as a high internal homology between the octapeptide structures. Six out of eight amino acids are identical in the repetition of this structure throughout region X r in both proteins and the other two are changed in a rather regular pattern.