Protein Family Models

This family comprises lipoproteins from four gamma proteobacterial species: PulS protein of Klebsiella pneumoniae (P20440), the OutS protein of Erwinia chrysanthemi (Q01567) and Pectobacterium chrysanthemi, and the functionally uncharacterized E. coli protein EtpO. PulS and OutS have been shown to interact with and facilitate insertion of secretins into the outer membrane, suggesting a chaperone-like, or piloting function for members of this family [1,2]. In the pilotin from this four-helix protein from enterohemorrhagic Escherichia coli, the straight helix alpha2, the curved helix alpha3 and the bent helix alpha4 surround the central N-terminal helix alpha1. These helices create a prominent groove, mainly formed by side chains of helices 1,2 and 3 suggesting this groove is important as a binding site [3]. [1]. 2661532. Klebsiella pneumoniae pulS gene encodes an outer membrane lipoprotein required for pullulanase secretion. D'Enfert C, Pugsley AP;. J Bacteriol. 1989;171:3673-3679. [2]. 22466878. The type II secretion system: biogenesis, molecular architecture and mechanism. Korotkov KV, Sandkvist M, Hol WG;. Nat Rev Microbiol. 2012;10:336-351. [3]. 23458689. Crystal structure of the pilotin from the enterohemorrhagic Escherichia coli type II secretion system. Korotkov KV, Hol WG;. J Struct Biol. 2013;182:186-191. (from Pfam)

Date:

2024-10-16

GspS, called a pilot protein, or pilotin, is a lipoprotein and one of two outer membrane (OM) proteins of type II secretion systems (T2SS). It associates with and facilitates insertion of the other, the secretin GspD, to form the T2SS pore in the OM. Members of this family may have variant forms, or more specific names, in certain lineages; examples are PulS protein in Klebsiella pneumoniae, OutS protein in Erwinia chrysanthemi, and (formerly) EptO in an Escherichia coli virulence plasmid. Note that GspS is replaced in some lineages by a different pilot protein family, GspSbeta.

Gene:

gspS

Date:

2024-05-30