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Conserved domains on  [gi|736077200|ref|WP_034210775|]
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GspH/FimT family protein [Arenimonas metalli]

Protein Classification

GspH/FimT family protein( domain architecture ID 10572244)

GspH/FimT family protein similar to Escherichia coli General secretion pathway protein H (GspH) which is a minor pseudopilin and may function as an initiator or regulator of pilus biogenesis and dynamics, and/or as an adaptor between various pseudopilin component and other members of the type II secretion system (T2SS)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GspH pfam12019
Type II transport protein GspH; GspH is involved in bacterial type II export systems. Like all ...
42-134 6.82e-07

Type II transport protein GspH; GspH is involved in bacterial type II export systems. Like all pilins, GspH has an N terminus alpha helix. This helix is followed by nine beta strands forming two beta sheets, one of five antiparallel strands and one of four antiparallel strands. GspH is a minor pseudopilin; it is expressed much less than other pseudopilins in the type II secretion pilus (major pilins). The function and localization of minor pseudo-pilins are still to be fully unraveled. It has been suggested that some minor pseudopilins may assemble either into the base or the tip of pili, or both. They function as initiators or regulators of pilus biogenesis and dynamics, and/or as adaptors between various pseudopilin component and other members of the T2SS.


:

Pssm-ID: 463433  Cd Length: 108  Bit Score: 45.27  E-value: 6.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736077200   42 AAKELAAELRFTRAQAIATGREQVFRIDVGEKRWQGAGERSGELPADIALEVTGAREELE--------TPQVVAIRFFPE 113
Cdd:pfam12019   1 AANRLAAALQLARSEAIKRGRPVTVCPSDWSGGWIVFVDANANGDLDGGEDLLRVGAALAggdvlvtaSSASPQITFNPD 80
                          90       100
                  ....*....|....*....|..
gi 736077200  114 G-AATGGRLVLRNGEAAWRVDV 134
Cdd:pfam12019  81 GrAATPGTLTLCSGGSGRSRRV 102
 
Name Accession Description Interval E-value
GspH pfam12019
Type II transport protein GspH; GspH is involved in bacterial type II export systems. Like all ...
42-134 6.82e-07

Type II transport protein GspH; GspH is involved in bacterial type II export systems. Like all pilins, GspH has an N terminus alpha helix. This helix is followed by nine beta strands forming two beta sheets, one of five antiparallel strands and one of four antiparallel strands. GspH is a minor pseudopilin; it is expressed much less than other pseudopilins in the type II secretion pilus (major pilins). The function and localization of minor pseudo-pilins are still to be fully unraveled. It has been suggested that some minor pseudopilins may assemble either into the base or the tip of pili, or both. They function as initiators or regulators of pilus biogenesis and dynamics, and/or as adaptors between various pseudopilin component and other members of the T2SS.


Pssm-ID: 463433  Cd Length: 108  Bit Score: 45.27  E-value: 6.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736077200   42 AAKELAAELRFTRAQAIATGREQVFRIDVGEKRWQGAGERSGELPADIALEVTGAREELE--------TPQVVAIRFFPE 113
Cdd:pfam12019   1 AANRLAAALQLARSEAIKRGRPVTVCPSDWSGGWIVFVDANANGDLDGGEDLLRVGAALAggdvlvtaSSASPQITFNPD 80
                          90       100
                  ....*....|....*....|..
gi 736077200  114 G-AATGGRLVLRNGEAAWRVDV 134
Cdd:pfam12019  81 GrAATPGTLTLCSGGSGRSRRV 102
typeII_sec_gspH TIGR01708
type II secretion system protein H; This model represents GspH, protein H of the main terminal ...
3-139 1.22e-03

type II secretion system protein H; This model represents GspH, protein H 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: 130769 [Multi-domain]  Cd Length: 143  Bit Score: 36.77  E-value: 1.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736077200    3 RPRGFSLVELVVVMVLIAALAALGLGAIGSGLPGQQLRGAAKELAAELRFTRAQAIATGREQVFRIdvGEKRWQgAGERS 82
Cdd:TIGR01708   2 RQSGFTLIELLVVLAIMGLVAAAAALSLVSHYGTKSLDQVAGRLAARLRLAQTSARATGRPVLLRL--GSRGIR-FGERA 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 736077200   83 GELPADIALEVT----GAREELETPQVVAIRFFPEGAATGGRLVLRNGEAAWRVDVAWLTG 139
Cdd:TIGR01708  79 SLALPVDEVKMTdwtgQETVVADRQTVLTVLFLPDGRASPMDMTLQRKGRSVTVAVNWLGG 139
 
Name Accession Description Interval E-value
GspH pfam12019
Type II transport protein GspH; GspH is involved in bacterial type II export systems. Like all ...
42-134 6.82e-07

Type II transport protein GspH; GspH is involved in bacterial type II export systems. Like all pilins, GspH has an N terminus alpha helix. This helix is followed by nine beta strands forming two beta sheets, one of five antiparallel strands and one of four antiparallel strands. GspH is a minor pseudopilin; it is expressed much less than other pseudopilins in the type II secretion pilus (major pilins). The function and localization of minor pseudo-pilins are still to be fully unraveled. It has been suggested that some minor pseudopilins may assemble either into the base or the tip of pili, or both. They function as initiators or regulators of pilus biogenesis and dynamics, and/or as adaptors between various pseudopilin component and other members of the T2SS.


Pssm-ID: 463433  Cd Length: 108  Bit Score: 45.27  E-value: 6.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736077200   42 AAKELAAELRFTRAQAIATGREQVFRIDVGEKRWQGAGERSGELPADIALEVTGAREELE--------TPQVVAIRFFPE 113
Cdd:pfam12019   1 AANRLAAALQLARSEAIKRGRPVTVCPSDWSGGWIVFVDANANGDLDGGEDLLRVGAALAggdvlvtaSSASPQITFNPD 80
                          90       100
                  ....*....|....*....|..
gi 736077200  114 G-AATGGRLVLRNGEAAWRVDV 134
Cdd:pfam12019  81 GrAATPGTLTLCSGGSGRSRRV 102
typeII_sec_gspH TIGR01708
type II secretion system protein H; This model represents GspH, protein H of the main terminal ...
3-139 1.22e-03

type II secretion system protein H; This model represents GspH, protein H 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: 130769 [Multi-domain]  Cd Length: 143  Bit Score: 36.77  E-value: 1.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736077200    3 RPRGFSLVELVVVMVLIAALAALGLGAIGSGLPGQQLRGAAKELAAELRFTRAQAIATGREQVFRIdvGEKRWQgAGERS 82
Cdd:TIGR01708   2 RQSGFTLIELLVVLAIMGLVAAAAALSLVSHYGTKSLDQVAGRLAARLRLAQTSARATGRPVLLRL--GSRGIR-FGERA 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 736077200   83 GELPADIALEVT----GAREELETPQVVAIRFFPEGAATGGRLVLRNGEAAWRVDVAWLTG 139
Cdd:TIGR01708  79 SLALPVDEVKMTdwtgQETVVADRQTVLTVLFLPDGRASPMDMTLQRKGRSVTVAVNWLGG 139
 
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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