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Conserved domains on  [gi|11559480|dbj|BAB18793|]
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GspH [Burkholderia cepacia]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
typeII_sec_gspH super family cl46935
type II secretion system protein H; This model represents GspH, protein H of the main terminal ...
 8-156 5.42e-20

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]


The actual alignment was detected with superfamily member TIGR01708:

Pssm-ID: 130769 [Multi-domain]  Cd Length: 143  Bit Score: 80.69  E-value: 5.42e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11559480     8 RRTRGFTLLEMLVVLVIAG-LLVSLASLSLTRNPRTDLREEAQRIALLFETAGDEAQVRARPIAWQPTAHGFQFdvsSPD 86
Cdd:TIGR01708   1 HRQSGFTLIELLVVLAIMGlVAAAAALSLVSHYGTKSLDQVAGRLAARLRLAQTSARATGRPVLLRLGSRGIRF---GER 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11559480    87 GWRTLRDDLLRPRDWDGGVTgaDIDYPGSDtraSRVVFGTESIDTPVRVTLHSAAGSATIVGTGNGRYEV 156
Cdd:TIGR01708  78 ASLALPVDEVKMTDWTGQET--VVADRQTV---LTVLFLPDGRASPMDMTLQRKGRSVTVAVNWLGGLRL 142
 
Name Accession Description Interval E-value
typeII_sec_gspH TIGR01708
type II secretion system protein H; This model represents GspH, protein H of the main terminal ...
 8-156 5.42e-20

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: 80.69  E-value: 5.42e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11559480     8 RRTRGFTLLEMLVVLVIAG-LLVSLASLSLTRNPRTDLREEAQRIALLFETAGDEAQVRARPIAWQPTAHGFQFdvsSPD 86
Cdd:TIGR01708   1 HRQSGFTLIELLVVLAIMGlVAAAAALSLVSHYGTKSLDQVAGRLAARLRLAQTSARATGRPVLLRLGSRGIRF---GER 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11559480    87 GWRTLRDDLLRPRDWDGGVTgaDIDYPGSDtraSRVVFGTESIDTPVRVTLHSAAGSATIVGTGNGRYEV 156
Cdd:TIGR01708  78 ASLALPVDEVKMTDWTGQET--VVADRQTV---LTVLFLPDGRASPMDMTLQRKGRSVTVAVNWLGGLRL 142
PulG COG2165
Type II secretory pathway, pseudopilin PulG [Cell motility, Intracellular trafficking, ...
 1-26 1.08e-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: 47.21  E-value: 1.08e-07
                        10        20
                ....*....|....*....|....*.
gi 11559480   1 MKHGAARRRTRGFTLLEMLVVLVIAG 26
Cdd:COG2165   1 MKLRRRRRRQRGFTLIELLVVIAIIG 26
N_methyl pfam07963
Prokaryotic N-terminal methylation motif; This short motif directs methylation of the ...
 7-26 2.12e-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: 39.28  E-value: 2.12e-05
                          10        20
                  ....*....|....*....|
gi 11559480     7 RRRTRGFTLLEMLVVLVIAG 26
Cdd:pfam07963   1 MRKQRGFTLIELLVALAILA 20
pilin_ComGC NF040999
competence type IV pilus major pilin ComGC; ComGC, encoded in the comG operon, is the major ...
 12-24 1.96e-03

competence type IV pilus major pilin ComGC; ComGC, encoded in the comG operon, is the major pilin of a type IV pilus involved in natural transformation of monoderm bacteria (those lacking an outer membrane) such as Bacillus subtilis and Streptococcus pneumoniae. In the seed alignment, Bacillus proteins have a pair of Cys residues likely to form a disulfide bond while Streptococcus proteins lack Cys residues.


Pssm-ID: 468929  Cd Length: 84  Bit Score: 35.57  E-value: 1.96e-03
                         10
                 ....*....|...
gi 11559480   12 GFTLLEMLVVLVI 24
Cdd:NF040999   3 GFTLIEMLIVLLI 15
 
Name Accession Description Interval E-value
typeII_sec_gspH TIGR01708
type II secretion system protein H; This model represents GspH, protein H of the main terminal ...
 8-156 5.42e-20

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: 80.69  E-value: 5.42e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11559480     8 RRTRGFTLLEMLVVLVIAG-LLVSLASLSLTRNPRTDLREEAQRIALLFETAGDEAQVRARPIAWQPTAHGFQFdvsSPD 86
Cdd:TIGR01708   1 HRQSGFTLIELLVVLAIMGlVAAAAALSLVSHYGTKSLDQVAGRLAARLRLAQTSARATGRPVLLRLGSRGIRF---GER 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11559480    87 GWRTLRDDLLRPRDWDGGVTgaDIDYPGSDtraSRVVFGTESIDTPVRVTLHSAAGSATIVGTGNGRYEV 156
Cdd:TIGR01708  78 ASLALPVDEVKMTDWTGQET--VVADRQTV---LTVLFLPDGRASPMDMTLQRKGRSVTVAVNWLGGLRL 142
PulG COG2165
Type II secretory pathway, pseudopilin PulG [Cell motility, Intracellular trafficking, ...
 1-26 1.08e-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: 47.21  E-value: 1.08e-07
                        10        20
                ....*....|....*....|....*.
gi 11559480   1 MKHGAARRRTRGFTLLEMLVVLVIAG 26
Cdd:COG2165   1 MKLRRRRRRQRGFTLIELLVVIAIIG 26
FimT COG4970
Type IV pilus assembly protein FimT [Cell motility, Extracellular structures];
1-74 1.37e-05

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


Pssm-ID: 443996 [Multi-domain]  Cd Length: 73  Bit Score: 40.99  E-value: 1.37e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 11559480   1 MKHGaaRRRTRGFTLLEMLVVLVIAGLLVSLASLSLTR-NPRTDLREEAQRIALLFETAGDEAQVRARPIAWQPT 74
Cdd:COG4970   1 MKRL--RRRQRGFTLIELLVVLAILAILAAIAVPSFSSlIARQRLRAAANELAAALRLARSEAIRRGQPVTLSPS 73
N_methyl pfam07963
Prokaryotic N-terminal methylation motif; This short motif directs methylation of the ...
 7-26 2.12e-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: 39.28  E-value: 2.12e-05
                          10        20
                  ....*....|....*....|
gi 11559480     7 RRRTRGFTLLEMLVVLVIAG 26
Cdd:pfam07963   1 MRKQRGFTLIELLVALAILA 20
PilE COG4968
Type IV pilus assembly protein PilE [Cell motility, Extracellular structures];
1-26 1.39e-04

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


Pssm-ID: 443994 [Multi-domain]  Cd Length: 124  Bit Score: 39.29  E-value: 1.39e-04
                        10        20
                ....*....|....*....|....*.
gi 11559480   1 MKHGAaRRRTRGFTLLEMLVVLVIAG 26
Cdd:COG4968   1 MKKRM-RRRQRGFTLIELMIVVAIIG 25
PilV COG4967
Type IV pilus assembly protein PilV [Cell motility, Extracellular structures];
1-24 2.75e-04

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


Pssm-ID: 443993 [Multi-domain]  Cd Length: 86  Bit Score: 37.66  E-value: 2.75e-04
                        10        20
                ....*....|....*....|....
gi 11559480   1 MKHGAARRRTRGFTLLEMLVVLVI 24
Cdd:COG4967   1 MSRRRRRRRQRGFTLIEVLVALVI 24
IV_pilin_GFxxxE TIGR02532
prepilin-type N-terminal cleavage/methylation domain; This model describes many but not all ...
 10-26 3.30e-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: 3.30e-04
                          10
                  ....*....|....*..
gi 11559480    10 TRGFTLLEMLVVLVIAG 26
Cdd:TIGR02532   1 QRGFTLIELLVVLAILG 17
ComGC COG4537
Competence protein ComGC [Mobilome: prophages, transposons];
1-26 4.21e-04

Competence protein ComGC [Mobilome: prophages, transposons];


Pssm-ID: 443603 [Multi-domain]  Cd Length: 108  Bit Score: 37.60  E-value: 4.21e-04
                        10        20
                ....*....|....*....|....*.
gi 11559480   1 MKHGAARRRTRGFTLLEMLVVLVIAG 26
Cdd:COG4537   2 KKKKRKLKKEKGFTLIEMLIVLLIIS 27
pilin_ComGC NF040999
competence type IV pilus major pilin ComGC; ComGC, encoded in the comG operon, is the major ...
 12-24 1.96e-03

competence type IV pilus major pilin ComGC; ComGC, encoded in the comG operon, is the major pilin of a type IV pilus involved in natural transformation of monoderm bacteria (those lacking an outer membrane) such as Bacillus subtilis and Streptococcus pneumoniae. In the seed alignment, Bacillus proteins have a pair of Cys residues likely to form a disulfide bond while Streptococcus proteins lack Cys residues.


Pssm-ID: 468929  Cd Length: 84  Bit Score: 35.57  E-value: 1.96e-03
                         10
                 ....*....|...
gi 11559480   12 GFTLLEMLVVLVI 24
Cdd:NF040999   3 GFTLIEMLIVLLI 15
PulJ COG4795
Type II secretory pathway, PulJ/GspJ component [Intracellular trafficking, secretion, and ...
 1-24 2.31e-03

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


Pssm-ID: 443823 [Multi-domain]  Cd Length: 118  Bit Score: 35.76  E-value: 2.31e-03
                        10        20
                ....*....|....*....|....
gi 11559480   1 MKHgaARRRTRGFTLLEMLVVLVI 24
Cdd:COG4795   1 MKR--ARRRQRGFTLLELLVALAI 22
typeII_sec_gspG TIGR01710
type II secretion system protein G; This model represents GspG, protein G of the main terminal ...
 11-26 4.07e-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: 4.07e-03
                          10
                  ....*....|....*.
gi 11559480    11 RGFTLLEMLVVLVIAG 26
Cdd:TIGR01710   1 RGFTLLEIMVVLVILG 16
GspH pfam12019
Type II transport protein GspH; GspH is involved in bacterial type II export systems. Like all ...
 47-152 6.43e-03

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: 34.48  E-value: 6.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11559480    47 EAQRIALLFETAGDEAQVRARPIAWQPTA--HGFQ-FDVSSPDGWRTLRDDLLR-PRDWDGGVTGadidyPGSDTRASRV 122
Cdd:pfam12019   1 AANRLAAALQLARSEAIKRGRPVTVCPSDwsGGWIvFVDANANGDLDGGEDLLRvGAALAGGDVL-----VTASSASPQI 75

                          90       100       110
                  ....*....|....*....|....*....|...
gi 11559480   123 VF---GTESIDTPVRVTLHSAAGSATIVGTGNG 152
Cdd:pfam12019  76 TFnpdGRAATPGTLTLCSGGSGRSRRVVVSASG 108
 
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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