type IV pilin protein [Rheinheimera mesophila]
type IV pilin protein( domain architecture ID 11471939)
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
List of domain hits
Name | Accession | Description | Interval | E-value | |||
PilE | COG4968 | Type IV pilus assembly protein PilE [Cell motility, Extracellular structures]; |
8-126 | 2.57e-25 | |||
Type IV pilus assembly protein PilE [Cell motility, Extracellular structures]; : Pssm-ID: 443994 [Multi-domain] Cd Length: 124 Bit Score: 92.44 E-value: 2.57e-25
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Name | Accession | Description | Interval | E-value | |||
PilE | COG4968 | Type IV pilus assembly protein PilE [Cell motility, Extracellular structures]; |
8-126 | 2.57e-25 | |||
Type IV pilus assembly protein PilE [Cell motility, Extracellular structures]; Pssm-ID: 443994 [Multi-domain] Cd Length: 124 Bit Score: 92.44 E-value: 2.57e-25
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ComP_DUS | pfam16732 | Type IV minor pilin ComP, DNA uptake sequence receptor; ComP-DUS is the DNA-uptake sequence ... |
35-83 | 1.15e-08 | |||
Type IV minor pilin ComP, DNA uptake sequence receptor; ComP-DUS is the DNA-uptake sequence receptor of pathogenic Proteobacteria. ComP is a type IV minor pilin -site on the minor type IV pilin, C one of three minor (low abundance) pilins in pathogenic Proteobacteria Neisseria species (with PilV and PilX). These modulate Tfp-mediated properties without affecting Tfp biogenesis. ComP plays a prominent role in competence at the level of DNA uptake. Comp is exposed on the surface of Neisseria filaments, and it is this that recognizes homotypic DNA through genus-specific DNA uptake sequence (DUS) motifs. Pssm-ID: 435546 Cd Length: 83 Bit Score: 48.46 E-value: 1.15e-08
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PRK10574 | PRK10574 | putative major pilin subunit; Provisional |
8-36 | 1.39e-08 | |||
putative major pilin subunit; Provisional Pssm-ID: 236718 [Multi-domain] Cd Length: 146 Bit Score: 49.65 E-value: 1.39e-08
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IV_pilin_GFxxxE | TIGR02532 | prepilin-type N-terminal cleavage/methylation domain; This model describes many but not all ... |
8-29 | 1.82e-04 | |||
prepilin-type N-terminal cleavage/methylation domain; 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). [Cell envelope, Surface structures, Protein fate, Protein and peptide secretion and trafficking] Pssm-ID: 274182 [Multi-domain] Cd Length: 24 Bit Score: 36.13 E-value: 1.82e-04
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Name | Accession | Description | Interval | E-value | |||
PilE | COG4968 | Type IV pilus assembly protein PilE [Cell motility, Extracellular structures]; |
8-126 | 2.57e-25 | |||
Type IV pilus assembly protein PilE [Cell motility, Extracellular structures]; Pssm-ID: 443994 [Multi-domain] Cd Length: 124 Bit Score: 92.44 E-value: 2.57e-25
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PilA | COG4969 | Type IV pilus assembly protein, major pilin PilA [Cell motility, Extracellular structures]; |
8-67 | 2.64e-13 | |||
Type IV pilus assembly protein, major pilin PilA [Cell motility, Extracellular structures]; Pssm-ID: 443995 [Multi-domain] Cd Length: 134 Bit Score: 62.03 E-value: 2.64e-13
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PulG | COG2165 | Type II secretory pathway, pseudopilin PulG [Cell motility, Intracellular trafficking, ... |
8-80 | 1.97e-11 | |||
Type II secretory pathway, pseudopilin PulG [Cell motility, Intracellular trafficking, secretion, and vesicular transport, Extracellular structures]; Pssm-ID: 441768 [Multi-domain] Cd Length: 99 Bit Score: 56.07 E-value: 1.97e-11
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FimT | COG4970 | Type IV pilus assembly protein FimT [Cell motility, Extracellular structures]; |
8-54 | 9.65e-11 | |||
Type IV pilus assembly protein FimT [Cell motility, Extracellular structures]; Pssm-ID: 443996 [Multi-domain] Cd Length: 73 Bit Score: 53.70 E-value: 9.65e-11
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ComP_DUS | pfam16732 | Type IV minor pilin ComP, DNA uptake sequence receptor; ComP-DUS is the DNA-uptake sequence ... |
35-83 | 1.15e-08 | |||
Type IV minor pilin ComP, DNA uptake sequence receptor; ComP-DUS is the DNA-uptake sequence receptor of pathogenic Proteobacteria. ComP is a type IV minor pilin -site on the minor type IV pilin, C one of three minor (low abundance) pilins in pathogenic Proteobacteria Neisseria species (with PilV and PilX). These modulate Tfp-mediated properties without affecting Tfp biogenesis. ComP plays a prominent role in competence at the level of DNA uptake. Comp is exposed on the surface of Neisseria filaments, and it is this that recognizes homotypic DNA through genus-specific DNA uptake sequence (DUS) motifs. Pssm-ID: 435546 Cd Length: 83 Bit Score: 48.46 E-value: 1.15e-08
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PRK10574 | PRK10574 | putative major pilin subunit; Provisional |
8-36 | 1.39e-08 | |||
putative major pilin subunit; Provisional Pssm-ID: 236718 [Multi-domain] Cd Length: 146 Bit Score: 49.65 E-value: 1.39e-08
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PulJ | COG4795 | Type II secretory pathway, PulJ/GspJ component [Intracellular trafficking, secretion, and ... |
8-65 | 1.21e-05 | |||
Type II secretory pathway, PulJ/GspJ component [Intracellular trafficking, secretion, and vesicular transport]; Pssm-ID: 443823 [Multi-domain] Cd Length: 118 Bit Score: 41.54 E-value: 1.21e-05
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PilW | COG4966 | Type IV pilus assembly protein PilW [Cell motility, Extracellular structures]; |
8-113 | 1.78e-05 | |||
Type IV pilus assembly protein PilW [Cell motility, Extracellular structures]; Pssm-ID: 443992 [Multi-domain] Cd Length: 158 Bit Score: 41.70 E-value: 1.78e-05
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ComGC | COG4537 | Competence protein ComGC [Mobilome: prophages, transposons]; |
8-40 | 2.21e-05 | |||
Competence protein ComGC [Mobilome: prophages, transposons]; Pssm-ID: 443603 [Multi-domain] Cd Length: 108 Bit Score: 40.68 E-value: 2.21e-05
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N_methyl | pfam07963 | Prokaryotic N-terminal methylation motif; This short motif directs methylation of the ... |
8-29 | 6.21e-05 | |||
Prokaryotic N-terminal methylation motif; 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 pfam00114, pfam05946, pfam02501 and pfam07596. Pssm-ID: 429756 [Multi-domain] Cd Length: 27 Bit Score: 37.35 E-value: 6.21e-05
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IV_pilin_GFxxxE | TIGR02532 | prepilin-type N-terminal cleavage/methylation domain; This model describes many but not all ... |
8-29 | 1.82e-04 | |||
prepilin-type N-terminal cleavage/methylation domain; 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). [Cell envelope, Surface structures, Protein fate, Protein and peptide secretion and trafficking] Pssm-ID: 274182 [Multi-domain] Cd Length: 24 Bit Score: 36.13 E-value: 1.82e-04
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typeII_sec_gspG | TIGR01710 | type II secretion system protein G; This model represents GspG, protein G of the main terminal ... |
8-56 | 4.31e-03 | |||
type II secretion system protein G; This model represents GspG, protein G of the main terminal branch of the general secretion pathway, also called type II secretion. It transports folded proteins across the bacterial outer membrane and is widely distributed in Gram-negative pathogens. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis] Pssm-ID: 130771 [Multi-domain] Cd Length: 134 Bit Score: 34.71 E-value: 4.31e-03
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Blast search parameters | ||||
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