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Conserved domains on  [gi|327549342|gb|EGF33913|]
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General secretion pathway protein I [Oxalobacteraceae bacterium IMCC9480]

Protein Classification

PulG and T2SSI domain-containing protein( domain architecture ID 11450570)

PulG and T2SSI domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
T2SSI pfam02501
Type II secretion system (T2SS), protein I; The Type II secretion system, also called ...
 44-123 8.64e-22

Type II secretion system (T2SS), protein I; The Type II secretion system, also called Secretion-dependent pathway (SDP), is responsible for the transport of proteins across the outer membrane first exported to the periplasm by the Sec or Tat translocon in Gram-negative (diderm) bacteria. As members of the T2SJ family, members of the T2SI family are pseudopilins containing prepilin signal sequences.


:

Pssm-ID: 426802  Cd Length: 80  Bit Score: 81.93  E-value: 8.64e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549342   44 LRAAMMATWSAENRLTEIRLAHSYPPLGKTAFECPQAEMRLVCEQEVLSTPNINFRRVEVSVYDARSPTRRIIKLNQLVS 123
Cdd:pfam02501   1 LEDRTLAQWVAENQLAELRLEPQWPAIGESSGECEQAGRRWYWRVEVVPTPDPGFRRVDVSVRADKDEARPLASLRTYVG 80
PulG COG2165
Type II secretory pathway, pseudopilin PulG [Cell motility, Intracellular trafficking, ...
 1-80 1.25e-10

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: 54.15  E-value: 1.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549342   1 MHPYRSRSTGFTLLEVLVALVIVGTALGASLRAVGSLTQNSNDLRAAMMAtWSAENRLTEIRLAHSYPPLGKTAFECPQA 80
Cdd:COG2165    3 LRRRRRRQRGFTLIELLVVIAIIGILAALALPALQGARERARRAELRSNL-RQIQQALERYRLDNGRYPSSLTGLLADVR 81
 
Name Accession Description Interval E-value
T2SSI pfam02501
Type II secretion system (T2SS), protein I; The Type II secretion system, also called ...
 44-123 8.64e-22

Type II secretion system (T2SS), protein I; The Type II secretion system, also called Secretion-dependent pathway (SDP), is responsible for the transport of proteins across the outer membrane first exported to the periplasm by the Sec or Tat translocon in Gram-negative (diderm) bacteria. As members of the T2SJ family, members of the T2SI family are pseudopilins containing prepilin signal sequences.


Pssm-ID: 426802  Cd Length: 80  Bit Score: 81.93  E-value: 8.64e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549342   44 LRAAMMATWSAENRLTEIRLAHSYPPLGKTAFECPQAEMRLVCEQEVLSTPNINFRRVEVSVYDARSPTRRIIKLNQLVS 123
Cdd:pfam02501   1 LEDRTLAQWVAENQLAELRLEPQWPAIGESSGECEQAGRRWYWRVEVVPTPDPGFRRVDVSVRADKDEARPLASLRTYVG 80
gspI TIGR01707
type II secretion system protein I; This model represents GspI, one of two proteins highly ...
 10-105 2.92e-18

type II secretion system protein I; This model represents GspI, one of two proteins highly conserved at their N-termini and described by pfam02501 but easily separable phylogenetically. The other is GspJ. Both GspI and GspJ are proteins of the type II secretion pathway, or main terminal branch of the general secretion pathway. This pathway carries proteins across the outer membrane. Note that proteins of type II secretion are cryptic in E. coli K-12 - present but not yet demonstrated to act on any target.


Pssm-ID: 273767 [Multi-domain]  Cd Length: 101  Bit Score: 73.71  E-value: 2.92e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549342   10 GFTLLEVLVALVIVGTALGASLRAVGSLTQNSNDLRAAMMATWSAENRLTEIRLAHSYPPLGKTA-FECPQAEMRLVCEQ 88
Cdd:TIGR01707   1 GFTLLEVLVALAIFAAAALALISSVGGQTNAIGRLRDKTLALWIADNRLAELSLGVGPPALGRNSgKELIAGREWLWRSQ 80

                          90
                  ....*....|....*..
gi 327549342   89 eVLSTPNINFRRVEVSV 105
Cdd:TIGR01707  81 -VHSTDDPTLLRVDITV 96
PulG COG2165
Type II secretory pathway, pseudopilin PulG [Cell motility, Intracellular trafficking, ...
 1-80 1.25e-10

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: 54.15  E-value: 1.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549342   1 MHPYRSRSTGFTLLEVLVALVIVGTALGASLRAVGSLTQNSNDLRAAMMAtWSAENRLTEIRLAHSYPPLGKTAFECPQA 80
Cdd:COG2165    3 LRRRRRRQRGFTLIELLVVIAIIGILAALALPALQGARERARRAELRSNL-RQIQQALERYRLDNGRYPSSLTGLLADVR 81
N_methyl pfam07963
Prokaryotic N-terminal methylation motif; This short motif directs methylation of the ...
 5-31 1.25e-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: 1.25e-04
                          10        20
                  ....*....|....*....|....*..
gi 327549342    5 RSRSTGFTLLEVLVALVIVGTALGASL 31
Cdd:pfam07963   1 MRKQRGFTLIELLVALAILAILLAAAL 27
IV_pilin_GFxxxE TIGR02532
prepilin-type N-terminal cleavage/methylation domain; This model describes many but not all ...
 10-31 4.16e-03

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: 32.66  E-value: 4.16e-03
                          10        20
                  ....*....|....*....|..
gi 327549342   10 GFTLLEVLVALVIVGTALGASL 31
Cdd:TIGR02532   3 GFTLIELLVVLAILGILALIAL 24
PRK08808 PRK08808
type II secretion system protein J;
3-41 9.77e-03

type II secretion system protein J;


Pssm-ID: 181557 [Multi-domain]  Cd Length: 211  Bit Score: 34.42  E-value: 9.77e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 327549342   3 PYRSRSTGFTLLEVLVALVIV--GTALG-ASLRAVGSLTQNS 41
Cdd:PRK08808   1 MMRRRAAGFTLIEVLLATVLLvgGLALAfATLRSASAVSQRG 42
 
Name Accession Description Interval E-value
T2SSI pfam02501
Type II secretion system (T2SS), protein I; The Type II secretion system, also called ...
 44-123 8.64e-22

Type II secretion system (T2SS), protein I; The Type II secretion system, also called Secretion-dependent pathway (SDP), is responsible for the transport of proteins across the outer membrane first exported to the periplasm by the Sec or Tat translocon in Gram-negative (diderm) bacteria. As members of the T2SJ family, members of the T2SI family are pseudopilins containing prepilin signal sequences.


Pssm-ID: 426802  Cd Length: 80  Bit Score: 81.93  E-value: 8.64e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549342   44 LRAAMMATWSAENRLTEIRLAHSYPPLGKTAFECPQAEMRLVCEQEVLSTPNINFRRVEVSVYDARSPTRRIIKLNQLVS 123
Cdd:pfam02501   1 LEDRTLAQWVAENQLAELRLEPQWPAIGESSGECEQAGRRWYWRVEVVPTPDPGFRRVDVSVRADKDEARPLASLRTYVG 80
gspI TIGR01707
type II secretion system protein I; This model represents GspI, one of two proteins highly ...
 10-105 2.92e-18

type II secretion system protein I; This model represents GspI, one of two proteins highly conserved at their N-termini and described by pfam02501 but easily separable phylogenetically. The other is GspJ. Both GspI and GspJ are proteins of the type II secretion pathway, or main terminal branch of the general secretion pathway. This pathway carries proteins across the outer membrane. Note that proteins of type II secretion are cryptic in E. coli K-12 - present but not yet demonstrated to act on any target.


Pssm-ID: 273767 [Multi-domain]  Cd Length: 101  Bit Score: 73.71  E-value: 2.92e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549342   10 GFTLLEVLVALVIVGTALGASLRAVGSLTQNSNDLRAAMMATWSAENRLTEIRLAHSYPPLGKTA-FECPQAEMRLVCEQ 88
Cdd:TIGR01707   1 GFTLLEVLVALAIFAAAALALISSVGGQTNAIGRLRDKTLALWIADNRLAELSLGVGPPALGRNSgKELIAGREWLWRSQ 80

                          90
                  ....*....|....*..
gi 327549342   89 eVLSTPNINFRRVEVSV 105
Cdd:TIGR01707  81 -VHSTDDPTLLRVDITV 96
PulG COG2165
Type II secretory pathway, pseudopilin PulG [Cell motility, Intracellular trafficking, ...
 1-80 1.25e-10

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: 54.15  E-value: 1.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549342   1 MHPYRSRSTGFTLLEVLVALVIVGTALGASLRAVGSLTQNSNDLRAAMMAtWSAENRLTEIRLAHSYPPLGKTAFECPQA 80
Cdd:COG2165    3 LRRRRRRQRGFTLIELLVVIAIIGILAALALPALQGARERARRAELRSNL-RQIQQALERYRLDNGRYPSSLTGLLADVR 81
PilV COG4967
Type IV pilus assembly protein PilV [Cell motility, Extracellular structures];
1-62 4.24e-09

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


Pssm-ID: 443993 [Multi-domain]  Cd Length: 86  Bit Score: 49.60  E-value: 4.24e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 327549342   1 MHPYRSRSTGFTLLEVLVALVIVGTALGASLRAVGSLTQNSNDLRAAMMATWSAENRLTEIR 62
Cdd:COG4967    3 RRRRRRRQRGFTLIEVLVALVILSIGLLGLAGLQAASLRSSQDARQRTQAALLAQDLLERLR 64
PulJ COG4795
Type II secretory pathway, PulJ/GspJ component [Intracellular trafficking, secretion, and ...
 1-64 2.16e-07

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


Pssm-ID: 443823 [Multi-domain]  Cd Length: 118  Bit Score: 46.16  E-value: 2.16e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 327549342   1 MHPYRSRSTGFTLLEVLVALVIVGTALGASLRAVGSLTQNSNDLRAAMMatwsaenRLTEIRLA 64
Cdd:COG4795    1 MKRARRRQRGFTLLELLVALAIFALLLLAAYRGLDSVLRSRERLEQQAE-------RLQELQRA 57
FimT COG4970
Type IV pilus assembly protein FimT [Cell motility, Extracellular structures];
1-51 5.96e-06

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


Pssm-ID: 443996 [Multi-domain]  Cd Length: 73  Bit Score: 40.99  E-value: 5.96e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 327549342   1 MHPYRSRSTGFTLLEVLVALVIVGTALGASLRAVGSLTQNS------NDLRAAMMAT 51
Cdd:COG4970    1 MKRLRRRQRGFTLIELLVVLAILAILAAIAVPSFSSLIARQrlraaaNELAAALRLA 57
N_methyl pfam07963
Prokaryotic N-terminal methylation motif; This short motif directs methylation of the ...
 5-31 1.25e-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: 1.25e-04
                          10        20
                  ....*....|....*....|....*..
gi 327549342    5 RSRSTGFTLLEVLVALVIVGTALGASL 31
Cdd:pfam07963   1 MRKQRGFTLIELLVALAILAILLAAAL 27
PilE COG4968
Type IV pilus assembly protein PilE [Cell motility, Extracellular structures];
1-57 2.35e-03

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


Pssm-ID: 443994 [Multi-domain]  Cd Length: 124  Bit Score: 35.44  E-value: 2.35e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 327549342   1 MHPYRSRSTGFTLLEVLVALVIVGTALGASLRAVGSLTQNSN--DLRAAMMATWSAENR 57
Cdd:COG4968    2 KKRMRRRQRGFTLIELMIVVAIIGILAAIAIPSYQDYVERARraEAKAALLELAQAQER 60
IV_pilin_GFxxxE TIGR02532
prepilin-type N-terminal cleavage/methylation domain; This model describes many but not all ...
 10-31 4.16e-03

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: 32.66  E-value: 4.16e-03
                          10        20
                  ....*....|....*....|..
gi 327549342   10 GFTLLEVLVALVIVGTALGASL 31
Cdd:TIGR02532   3 GFTLIELLVVLAILGILALIAL 24
type_IV_pilV TIGR02523
type IV pilus modification protein PilV; Pilus systems categorized as type IV pilins differ ...
 10-50 4.33e-03

type IV pilus modification protein PilV; Pilus systems categorized as type IV pilins differ greatly from one another, with some showing greater similarty to type II or type III secretion systems than to each other. Members of this protein family represent the PilV protein of type IV pilus systems as found in Pseudomonas aeruginosa PAO1, Pseudomonas syringae DC3000, Neisseria meningitidis MC58, Xylella fastidiosa 9a5c, etc. [Cell envelope, Surface structures, Protein fate, Protein modification and repair]


Pssm-ID: 131575  Cd Length: 139  Bit Score: 34.74  E-value: 4.33e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 327549342   10 GFTLLEVLVALVIVG----TALGASLRAVGSLTQNSNDLRAAMMA 50
Cdd:TIGR02523   3 GFSMIEVLVALLVLAigvlGMAALQLKAVRYTRSASTRTIASMLA 47
PRK08808 PRK08808
type II secretion system protein J;
3-41 9.77e-03

type II secretion system protein J;


Pssm-ID: 181557 [Multi-domain]  Cd Length: 211  Bit Score: 34.42  E-value: 9.77e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 327549342   3 PYRSRSTGFTLLEVLVALVIV--GTALG-ASLRAVGSLTQNS 41
Cdd:PRK08808   1 MMRRRAAGFTLIEVLLATVLLvgGLALAfATLRSASAVSQRG 42
 
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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