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Links from Protein

Items: 10

1.
new record, indexing in progress
Family Accession:
2.
new record, indexing in progress
Family Accession:
3.

prepilin-type N-terminal cleavage/methylation domain-containing protein

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:
2025-02-03
Family Accession:
NF019575.5
Method:
HMM
4.

pilin

Proteins with only the short N-terminal methylation site are not separated from the noise. The Prosite pattern detects those better. (from Pfam)

GO Terms:
Biological Process:
cell adhesion (GO:0007155)
Cellular Component:
pilus (GO:0009289)
Date:
2025-02-01
Family Accession:
NF012342.5
Method:
HMM
5.
new record, indexing in progress
Family Accession:
6.
new record, indexing in progress
Family Accession:
7.
new record, indexing in progress
Family Accession:
8.
new record, indexing in progress
Family Accession:
9.

type IV pilin protein

type IV pilin protein similar to Pseudomonas aeruginosa type IV pilus (T4P) non-core minor pilin PilE, an ssential component of the T4P that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, twitching, adhesion, and retraction of T4P fibers

Date:
2025-01-06
Family Accession:
11471939
Method:
Sparcle
10.

prepilin-type N-terminal cleavage/methylation domain-containing protein

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
Family Accession:
TIGR02532.1
Method:
HMM
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