Protein Family Models

The T2SJ proteins are pseudopilins, which are targeted to the membrane in E. Coli. T2SJ forms a complex with T2SI (Pfam:PF02501) and T2SK (Pfam:PF03934) which is part of the Type II secretion apparatus involved in the translocation of proteins across the outer membrane in E.coli. The T2SK-I-J complex has quasihelical characteristics [1]. [1]. 18438417. Structure of the GspK-GspI-GspJ complex from the enterotoxigenic Escherichia coli type 2 secretion system. Korotkov KV, Hol WG;. Nat Struct Mol Biol. 2008;15:462-468. [2]. 15533433. The structure of the cytoplasmic domain of EpsL, an inner membrane component of the type II secretion system of Vibrio cholerae: an unusual member of the actin-like ATPase superfamily. Abendroth J, Bagdasarian M, Sandkvist M, Hol WG;. J Mol Biol 2004;344:619-633. [2]. 15223057. The general secretory pathway: a general misnomer?. Desvaux M, Parham NJ, Scott-Tucker A, Henderson IR;. Trends Microbiol. 2004;12:306-309. [3]. 14600218. Type II protein secretion and its relationship to bacterial type IV pili and archaeal flagella. Peabody CR, Chung YJ, Yen MR, Vidal-Ingigliardi D, Pugsley AP, Saier MH Jr;. Microbiology. 2003;149:3051-3072. [4]. 19299134. Secretion and subcellular localizations of bacterial proteins: a semantic awareness issue. Desvaux M, Hebraud M, Talon R, Henderson IR;. Trends Microbiol. 2009;17:139-145. (from Pfam)

Date:

2024-10-16

This short motif directs methylation of the conserved phenylalanine residue. It is most often found at the N-terminus of pilins and other proteins involved in secretion, see Pfam:PF00114, Pfam:PF05946, Pfam:PF02501 and Pfam:PF07596. (from Pfam)

Date:

2024-08-14

This HMM represents GspJ, one of two proteins highly conserved at their N-termini and described by PF02501 but easily separable phylogenetically. The other is GspI. Both GspI and GspJ are proteins of the type II secretion pathway (T2SS), previously called the main terminal branch of the General Secretion Pathway.

Gene:

gspJ

Date:

2021-05-12

This model describes many but not all examples of the N-terminal region of bacterial proteins that resemble type IV pilins at their N-terminus, with a cleavage site G^FxxxE followed by a hydrophobic stretch. The new N-terminal residue, usually Phe, is methylated. Separate domains of the prepilin peptidase appear responsible for cleavage and methylation. Proteins with this N-terminal region include type IV pilins and other components of pilus biogenesis, competence proteins, and type II secretion proteins. Typically several proteins in a single operon have this N-terminal domain. The N-terminal cleavage and methylation site is described by PROSITE motif PS00409 as [KRHEQSTAG]-G-[FYLIVM]-[ST]-[LT]-[LIVP]-E-[LIVMFWSTAG](14).

Date:

2019-09-10