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Conserved domains on  [gi|501579058|ref|WP_012583390|]
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MULTISPECIES: type II secretion system protein [Dictyoglomus]

Protein Classification

type II secretion system protein( domain architecture ID 11450365)

type II secretion system protein similar to Pseudomonas aeruginosa type II secretion system protein H, which is involved in a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of proteins; required for the translocation of a variety of enzymes across the outer membrane; pilin similar to fimbrial protein PilE, which is required for pilus biogenesis, as well as fimbrial protein PilA, which is responsible for the adhesive property of the pilus

Gene Ontology:  GO:0005886|GO:0015628|GO:0015627
PubMed:  30767847|1365398

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PulG COG2165
Type II secretory pathway, pseudopilin PulG [Cell motility, Intracellular trafficking, ...
 3-40 3.54e-07

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: 46.06  E-value: 3.54e-07
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 501579058   3 NRGFTLIELLLTFVILGIIATITLNFSLAIIDERKMLQ 40
Cdd:COG2165   10 QRGFTLIELLVVIAIIGILAALALPALQGARERARRAE 47
 
Name Accession Description Interval E-value
PulG COG2165
Type II secretory pathway, pseudopilin PulG [Cell motility, Intracellular trafficking, ...
 3-40 3.54e-07

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: 46.06  E-value: 3.54e-07
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 501579058   3 NRGFTLIELLLTFVILGIIATITLNFSLAIIDERKMLQ 40
Cdd:COG2165   10 QRGFTLIELLVVIAIIGILAALALPALQGARERARRAE 47
N_methyl pfam07963
Prokaryotic N-terminal methylation motif; This short motif directs methylation of the ...
 1-26 2.14e-04

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: 36.58  E-value: 2.14e-04
                          10        20
                  ....*....|....*....|....*.
gi 501579058    1 MYNRGFTLIELLLTFVILGIIATITL 26
Cdd:pfam07963   2 RKQRGFTLIELLVALAILAILLAAAL 27
IV_pilin_GFxxxE TIGR02532
prepilin-type N-terminal cleavage/methylation domain; This model describes many but not all ...
 3-26 2.42e-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: 36.51  E-value: 2.42e-04
                          10        20
                  ....*....|....*....|....
gi 501579058    3 NRGFTLIELLLTFVILGIIATITL 26
Cdd:TIGR02532   1 QRGFTLIELLVVLAILGILALIAL 24
 
Name Accession Description Interval E-value
PulG COG2165
Type II secretory pathway, pseudopilin PulG [Cell motility, Intracellular trafficking, ...
 3-40 3.54e-07

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: 46.06  E-value: 3.54e-07
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 501579058   3 NRGFTLIELLLTFVILGIIATITLNFSLAIIDERKMLQ 40
Cdd:COG2165   10 QRGFTLIELLVVIAIIGILAALALPALQGARERARRAE 47
FimT COG4970
Type IV pilus assembly protein FimT [Cell motility, Extracellular structures];
3-26 2.02e-06

Type IV pilus assembly protein FimT [Cell motility, Extracellular structures];


Pssm-ID: 443996 [Multi-domain]  Cd Length: 73  Bit Score: 43.30  E-value: 2.02e-06
                         10        20
                 ....*....|....*....|....
gi 501579058   3 NRGFTLIELLLTFVILGIIATITL 26
Cdd:COG4970    8 QRGFTLIELLVVLAILAILAAIAV 31
PilE COG4968
Type IV pilus assembly protein PilE [Cell motility, Extracellular structures];
3-26 1.29e-05

Type IV pilus assembly protein PilE [Cell motility, Extracellular structures];


Pssm-ID: 443994 [Multi-domain]  Cd Length: 124  Bit Score: 42.37  E-value: 1.29e-05
                         10        20
                 ....*....|....*....|....
gi 501579058   3 NRGFTLIELLLTFVILGIIATITL 26
Cdd:COG4968    9 QRGFTLIELMIVVAIIGILAAIAI 32
PulJ COG4795
Type II secretory pathway, PulJ/GspJ component [Intracellular trafficking, secretion, and ...
 3-47 1.08e-04

Type II secretory pathway, PulJ/GspJ component [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 443823 [Multi-domain]  Cd Length: 118  Bit Score: 39.61  E-value: 1.08e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 501579058   3 NRGFTLIELLLTFVILGIIATITLNFSLAIIDERKMLQKSYEIMQ 47
Cdd:COG4795    8 QRGFTLLELLVALAIFALLLLAAYRGLDSVLRSRERLEQQAERLQ 52
N_methyl pfam07963
Prokaryotic N-terminal methylation motif; This short motif directs methylation of the ...
 1-26 2.14e-04

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: 36.58  E-value: 2.14e-04
                          10        20
                  ....*....|....*....|....*.
gi 501579058    1 MYNRGFTLIELLLTFVILGIIATITL 26
Cdd:pfam07963   2 RKQRGFTLIELLVALAILAILLAAAL 27
IV_pilin_GFxxxE TIGR02532
prepilin-type N-terminal cleavage/methylation domain; This model describes many but not all ...
 3-26 2.42e-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: 36.51  E-value: 2.42e-04
                          10        20
                  ....*....|....*....|....
gi 501579058    3 NRGFTLIELLLTFVILGIIATITL 26
Cdd:TIGR02532   1 QRGFTLIELLVVLAILGILALIAL 24
PilA COG4969
Type IV pilus assembly protein, major pilin PilA [Cell motility, Extracellular structures];
4-26 2.94e-04

Type IV pilus assembly protein, major pilin PilA [Cell motility, Extracellular structures];


Pssm-ID: 443995 [Multi-domain]  Cd Length: 134  Bit Score: 38.54  E-value: 2.94e-04
                         10        20
                 ....*....|....*....|...
gi 501579058   4 RGFTLIELLLTFVILGIIATITL 26
Cdd:COG4969    6 KGFTLIELMIVVAIIGILAAIAI 28
PilV COG4967
Type IV pilus assembly protein PilV [Cell motility, Extracellular structures];
4-23 4.23e-03

Type IV pilus assembly protein PilV [Cell motility, Extracellular structures];


Pssm-ID: 443993 [Multi-domain]  Cd Length: 86  Bit Score: 34.57  E-value: 4.23e-03
                         10        20
                 ....*....|....*....|
gi 501579058   4 RGFTLIELLLTFVILGIIAT 23
Cdd:COG4967   11 RGFTLIEVLVALVILSIGLL 30
typeII_sec_gspG TIGR01710
type II secretion system protein G; This model represents GspG, protein G of the main terminal ...
 4-25 4.36e-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: 35.48  E-value: 4.36e-03
                          10        20
                  ....*....|....*....|..
gi 501579058    4 RGFTLIELLLTFVILGIIATIT 25
Cdd:TIGR01710   1 RGFTLLEIMVVLVILGLLAALV 22
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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