Identification of a novel penicillin-binding protein from Helicobacter pylori.
The Helicobacter pylori genome encodes four penicillin-binding proteins (PBPs). PBPs 1, 2, and 3 exhibit similarities to known PBPs. The sequence of PBP 4 is unique in that it displays a novel combination of two highly conserved PBP motifs and an absence of a third motif. Expression of PBP 4, but not PBP 1, 2, or 3, is significantly increased during mid- to late-log-phase growth.
Krishnamurthy
P
P
Department of Pathology, Medical College of Wisconsin, Milwaukee, Wisconsin, USA.
Parlow
M H
MH
Schneider
J
J
Burroughs
S
S
Wickland
C
C
Vakil
N B
NB
Dunn
B E
BE
Phadnis
S H
SH
D000595:Amino Acid Sequence; D001426:Bacterial Proteins; D002352:Carrier Proteins / Q000737:chemistry* / Q000235:genetics* / Q000302:isolation & purification; D016680:Genome, Bacterial; D016480:Helicobacter pylori / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D006602:Hexosyltransferases; D007536:Isomerism; D008969:Molecular Sequence Data; D008970:Molecular Weight; D002267:Muramoylpentapeptide Carboxypeptidase / Q000737:chemistry* / Q000235:genetics* / Q000302:isolation & purification; D046915:Penicillin-Binding Proteins; D010406:Penicillins / Q000378:metabolism* / Q000494:pharmacology; D010458:Peptidyl Transferases; D011485:Protein Binding / Q000187:drug effects
D001426:Bacterial Proteins; D002352:Carrier Proteins; D046915:Penicillin-Binding Proteins; D010406:Penicillins; D010458:Peptidyl Transferases; D006602:Hexosyltransferases; D002267:Muramoylpentapeptide Carboxypeptidase