Protein Family Models

This is a family of Gram-negative bacterial outer membrane lipoproteins. LpoB is required for the function of the major peptidoglycan synthase enzyme PBP1B. It interacts with PBP1B protein via the UvrB-like non-catalytic domain on that protein. LpoB has a 54-aa-long flexible N-terminal stretch followed by a globular domain with similarity to the N-terminal domain of the prevalent periplasmic protein TolB. The long, flexible N-terminal region of LpoB enables it to span the periplasm and reach its docking site in PBP1B. Peptidoglycan is the essential polymer within the sacculus that surrounds the cytoplasmic membrane of bacteria [1]. [1]. 24821816. Outer-membrane lipoprotein LpoB spans the periplasm to stimulate the peptidoglycan synthase PBP1B. Egan AJ, Jean NL, Koumoutsi A, Bougault CM, Biboy J, Sassine J, Solovyova AS, Breukink E, Typas A, Vollmer W, Simorre JP;. Proc Natl Acad Sci U S A. 2014;111:8197-8202. (from Pfam)

Date:

2024-10-16

Members of this protein family are restricted to the Proteobacteria, and all are predicted lipoproteins. In genomes that contain the thiK gene for the salvage enzyme thiamin kinase, the member of this family is encoded nearby.

Gene:

lpoB

Date:

2019-09-10

penicillin-binding protein activator LpoB is a regulator of peptidoglycan synthesis that is essential for the function of penicillin-binding protein 1B, stimulating its transpeptidase and transglycosylase activities

Date:

2020-05-18