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Conserved domains on  [gi|658548010|ref|WP_029740489|]
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prepilin peptidase-dependent protein [Enterobacter asburiae]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
T2SSJ super family cl42010
Type II secretion system (T2SS), protein J; The T2SJ proteins are pseudopilins, which are ...
 1-186 6.31e-91

Type II secretion system (T2SS), protein J; The T2SJ proteins are pseudopilins, which are targeted to the membrane in E. Coli. T2SJ forms a complex with T2SI (pfam02501) and T2SK (pfam03934) which is part of the Type II secretion apparatus involved in the translocation of proteins across the outer membrane in E.coli. The T2SK-I-J complex has quasihelical characteriztics.


The actual alignment was detected with superfamily member PRK10557:

Pssm-ID: 455355  Cd Length: 192  Bit Score: 263.76  E-value: 6.31e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548010   1 MSMKQRGFSLTEVLIATVISSLLLISASRFLPGLQRAVLVQSGQRQLEEEVWHHLFAMGKQLQRAGYCAGNCQGQALMTA 80
Cdd:PRK10557   2 MPVKQRGFSLLEVLLAMAIGSVLLLGAARFLPALQRQILTLTRQLRLEDEIWQRVFTVEKDLRRAGYCHGSCQGEGLEIA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548010  81 R----QGSCVIVRWDANSNGSWDNS-ASENDSTGFRLESGALETQRGATSCEGKGWEKLTDPDMLTIAHFVVRKVEHAGF 155
Cdd:PRK10557  82 NpgeaQGSCLIVAWDLNSNGRWEGApHKESEQFGYRLRNGVLETLRGATSCQGKGWEKLTDPDEITITTFSVERLDTSGF 161

                        170       180       190
                 ....*....|....*....|....*....|.
gi 658548010 156 APEVNIELAAIHKGEQGEPWQALYTVTGYNL 186
Cdd:PRK10557 162 SPVLTLNLRAASKAEPAIVVQATYSVTGFNL 192
 
Name Accession Description Interval E-value
PRK10557 PRK10557
prepilin peptidase-dependent protein;
1-186 6.31e-91

prepilin peptidase-dependent protein;


Pssm-ID: 236714  Cd Length: 192  Bit Score: 263.76  E-value: 6.31e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548010   1 MSMKQRGFSLTEVLIATVISSLLLISASRFLPGLQRAVLVQSGQRQLEEEVWHHLFAMGKQLQRAGYCAGNCQGQALMTA 80
Cdd:PRK10557   2 MPVKQRGFSLLEVLLAMAIGSVLLLGAARFLPALQRQILTLTRQLRLEDEIWQRVFTVEKDLRRAGYCHGSCQGEGLEIA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548010  81 R----QGSCVIVRWDANSNGSWDNS-ASENDSTGFRLESGALETQRGATSCEGKGWEKLTDPDMLTIAHFVVRKVEHAGF 155
Cdd:PRK10557  82 NpgeaQGSCLIVAWDLNSNGRWEGApHKESEQFGYRLRNGVLETLRGATSCQGKGWEKLTDPDEITITTFSVERLDTSGF 161

                        170       180       190
                 ....*....|....*....|....*....|.
gi 658548010 156 APEVNIELAAIHKGEQGEPWQALYTVTGYNL 186
Cdd:PRK10557 162 SPVLTLNLRAASKAEPAIVVQATYSVTGFNL 192
PulJ COG4795
Type II secretory pathway, PulJ/GspJ component [Intracellular trafficking, secretion, and ...
 1-118 3.24e-24

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


Pssm-ID: 443823 [Multi-domain]  Cd Length: 118  Bit Score: 91.61  E-value: 3.24e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548010   1 MSMKQRGFSLTEVLIATVISSLLLISASRFLPGLQRAVLVQSGQRQLEEEVWHHLFAMGKQLQRAGYCAGNCQGQALMTA 80
Cdd:COG4795    4 ARRRQRGFTLLELLVALAIFALLLLAAYRGLDSVLRSRERLEQQAERLQELQRALALLERDLRQAGPRPDEGGDPEPALS 83

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 658548010  81 RQGSCVIvrwDANSNGSWDNSASENDSTGFRLESGALE 118
Cdd:COG4795   84 GGGSCLI---DLNRNGWWNPLRSELQRVGYRLRDGALE 118
N_methyl pfam07963
Prokaryotic N-terminal methylation motif; This short motif directs methylation of the ...
 3-28 5.79e-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: 38.51  E-value: 5.79e-05
                          10        20
                  ....*....|....*....|....*.
gi 658548010    3 MKQRGFSLTEVLIATVISSLLLISAS 28
Cdd:pfam07963   2 RKQRGFTLIELLVALAILAILLAAAL 27
IV_pilin_GFxxxE TIGR02532
prepilin-type N-terminal cleavage/methylation domain; This model describes many but not all ...
 5-28 4.87e-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: 33.43  E-value: 4.87e-03
                          10        20
                  ....*....|....*....|....
gi 658548010    5 QRGFSLTEVLIATVISSLLLISAS 28
Cdd:TIGR02532   1 QRGFTLIELLVVLAILGILALIAL 24
 
Name Accession Description Interval E-value
PRK10557 PRK10557
prepilin peptidase-dependent protein;
1-186 6.31e-91

prepilin peptidase-dependent protein;


Pssm-ID: 236714  Cd Length: 192  Bit Score: 263.76  E-value: 6.31e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548010   1 MSMKQRGFSLTEVLIATVISSLLLISASRFLPGLQRAVLVQSGQRQLEEEVWHHLFAMGKQLQRAGYCAGNCQGQALMTA 80
Cdd:PRK10557   2 MPVKQRGFSLLEVLLAMAIGSVLLLGAARFLPALQRQILTLTRQLRLEDEIWQRVFTVEKDLRRAGYCHGSCQGEGLEIA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548010  81 R----QGSCVIVRWDANSNGSWDNS-ASENDSTGFRLESGALETQRGATSCEGKGWEKLTDPDMLTIAHFVVRKVEHAGF 155
Cdd:PRK10557  82 NpgeaQGSCLIVAWDLNSNGRWEGApHKESEQFGYRLRNGVLETLRGATSCQGKGWEKLTDPDEITITTFSVERLDTSGF 161

                        170       180       190
                 ....*....|....*....|....*....|.
gi 658548010 156 APEVNIELAAIHKGEQGEPWQALYTVTGYNL 186
Cdd:PRK10557 162 SPVLTLNLRAASKAEPAIVVQATYSVTGFNL 192
PulJ COG4795
Type II secretory pathway, PulJ/GspJ component [Intracellular trafficking, secretion, and ...
 1-118 3.24e-24

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


Pssm-ID: 443823 [Multi-domain]  Cd Length: 118  Bit Score: 91.61  E-value: 3.24e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548010   1 MSMKQRGFSLTEVLIATVISSLLLISASRFLPGLQRAVLVQSGQRQLEEEVWHHLFAMGKQLQRAGYCAGNCQGQALMTA 80
Cdd:COG4795    4 ARRRQRGFTLLELLVALAIFALLLLAAYRGLDSVLRSRERLEQQAERLQELQRALALLERDLRQAGPRPDEGGDPEPALS 83

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 658548010  81 RQGSCVIvrwDANSNGSWDNSASENDSTGFRLESGALE 118
Cdd:COG4795   84 GGGSCLI---DLNRNGWWNPLRSELQRVGYRLRDGALE 118
PilW COG4966
Type IV pilus assembly protein PilW [Cell motility, Extracellular structures];
4-67 5.58e-09

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


Pssm-ID: 443992 [Multi-domain]  Cd Length: 158  Bit Score: 52.87  E-value: 5.58e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658548010   4 KQRGFSLTEVLIATVISSLLLISASRFLPGLQRAVLVQSGQRQLEEEVWHHLFAMGKQLQRAGY 67
Cdd:COG4966    3 RQRGFTLVELMVALAIGLIVLAAVLQLFLSSRRSYRTQEALARLQENGRFALDLLSRDLRQAGY 66
PulG COG2165
Type II secretory pathway, pseudopilin PulG [Cell motility, Intracellular trafficking, ...
 1-49 4.94e-05

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: 40.67  E-value: 4.94e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 658548010   1 MSMKQRGFSLTEVLIATVISSLLLISASRFLPGLQRAVLVQSGQRQLEE 49
Cdd:COG2165    6 RRRRQRGFTLIELLVVIAIIGILAALALPALQGARERARRAELRSNLRQ 54
N_methyl pfam07963
Prokaryotic N-terminal methylation motif; This short motif directs methylation of the ...
 3-28 5.79e-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: 38.51  E-value: 5.79e-05
                          10        20
                  ....*....|....*....|....*.
gi 658548010    3 MKQRGFSLTEVLIATVISSLLLISAS 28
Cdd:pfam07963   2 RKQRGFTLIELLVALAILAILLAAAL 27
PilV COG4967
Type IV pilus assembly protein PilV [Cell motility, Extracellular structures];
4-46 4.19e-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: 4.19e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 658548010   4 KQRGFSLTEVLIATVISSLLLISASRFLPGLQRAVlVQSGQRQ 46
Cdd:COG4967    9 RQRGFTLIEVLVALVILSIGLLGLAGLQAASLRSS-QDARQRT 50
FimT COG4970
Type IV pilus assembly protein FimT [Cell motility, Extracellular structures];
1-47 2.90e-03

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


Pssm-ID: 443996 [Multi-domain]  Cd Length: 73  Bit Score: 35.21  E-value: 2.90e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 658548010   1 MSMKQRGFSLTEVLIATVISSLLL-ISASRFLPGLQRAVLvQSGQRQL 47
Cdd:COG4970    4 LRRRQRGFTLIELLVVLAILAILAaIAVPSFSSLIARQRL-RAAANEL 50
IV_pilin_GFxxxE TIGR02532
prepilin-type N-terminal cleavage/methylation domain; This model describes many but not all ...
 5-28 4.87e-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: 33.43  E-value: 4.87e-03
                          10        20
                  ....*....|....*....|....
gi 658548010    5 QRGFSLTEVLIATVISSLLLISAS 28
Cdd:TIGR02532   1 QRGFTLIELLVVLAILGILALIAL 24
 
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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