Identification of two binding domains, one for peptidoglycan and another for a secondary cell wall polymer, on the N-terminal part of the S-layer protein SbsB from Bacillus stearothermophilus PV72/p2.
First studies on the structure-function relationship of the S-layer protein from B. stearothermophilus PV72/p2 revealed the coexistence of two binding domains on its N-terminal part, one for peptidoglycan and another for a secondary cell wall polymer (SCWP). The peptidoglycan binding domain is located between amino acids 1 to 138 of the mature S-layer protein comprising a typical S-layer homologous domain. The SCWP binding domain lies between amino acids 240 to 331 and possesses a high serine plus glycine content.
Sára
M
M
Zentrum für Ultrastrukturforschung und Ludwig Boltzmann-Institut f ur Molekulare Nanotechnologie, Universität für Bodenkultur, 1180 Vienna, Austria.
Egelseer
E M
EM
Dekitsch
C
C
Sleytr
U B
UB
D001426:Bacterial Proteins / Q000378:metabolism*; D001665:Binding Sites; D002473:Cell Wall / Q000378:metabolism; D001411:Geobacillus stearothermophilus / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism*; D010457:Peptidoglycan / Q000378:metabolism*; D011108:Polymers / Q000378:metabolism; D012697:Serine Endopeptidases / Q000378:metabolism
D001426:Bacterial Proteins; D008565:Membrane Proteins; D010457:Peptidoglycan; D011108:Polymers; C104635:SbsB protein, Bacillus stearothermophilus; D012697:Serine Endopeptidases; C028344:glutamyl endopeptidase