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Conserved domains on  [gi|15833442|ref|NP_312215|]
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leader peptidase HopD [Escherichia coli O157:H7 str. Sakai]

Protein Classification

prepilin peptidase( domain architecture ID 11449472)

prepilin peptidase, A24 family peptidase, processes type 4 pilin precursor proteins (prepilins) to their mature forms by removal of leader peptides

CATH:  1.20.120.1220
EC:  3.4.23.43
Gene Ontology:  GO:0004190|GO:0016020
MEROPS:  A24
PubMed:  25793961|7961448

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PulO COG1989
Prepilin signal peptidase PulO (type II secretory pathway) or related peptidase [Cell motility, ...
4-146 2.43e-36

Prepilin signal peptidase PulO (type II secretory pathway) or related peptidase [Cell motility, Intracellular trafficking, secretion, and vesicular transport];


:

Pssm-ID: 441592 [Multi-domain]  Cd Length: 256  Bit Score: 125.67  E-value: 2.43e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833442   4 TLPFLILYACLSALLFFWDAKHGLLPDRFTCPLLWSGLLFYQVCHPDGLADALWGAIIGYGTFAVIYWGYRILRHKEGLG 83
Cdd:COG1989 100 QLLAALLLLSLLLALSFIDLDTQLLPDSLTLPLLWLGLLLSLLGGFVSLLDALLGALAGYLLLWLIYWLFKLLTGKEGMG 179
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15833442  84 YGDVKFLAALGAWHSWAFLPrLVFLAASFACGAVVIGLLMRGKESLKNPLPFGPFLAAAGFVI 146
Cdd:COG1989 180 GGDVKLLAALGAWLGWQALL-LILLLASLLGALVGLILLLLGRKGRKTPIPFGPFLALGGLIA 241
 
Name Accession Description Interval E-value
PulO COG1989
Prepilin signal peptidase PulO (type II secretory pathway) or related peptidase [Cell motility, ...
4-146 2.43e-36

Prepilin signal peptidase PulO (type II secretory pathway) or related peptidase [Cell motility, Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 441592 [Multi-domain]  Cd Length: 256  Bit Score: 125.67  E-value: 2.43e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833442   4 TLPFLILYACLSALLFFWDAKHGLLPDRFTCPLLWSGLLFYQVCHPDGLADALWGAIIGYGTFAVIYWGYRILRHKEGLG 83
Cdd:COG1989 100 QLLAALLLLSLLLALSFIDLDTQLLPDSLTLPLLWLGLLLSLLGGFVSLLDALLGALAGYLLLWLIYWLFKLLTGKEGMG 179
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15833442  84 YGDVKFLAALGAWHSWAFLPrLVFLAASFACGAVVIGLLMRGKESLKNPLPFGPFLAAAGFVI 146
Cdd:COG1989 180 GGDVKLLAALGAWLGWQALL-LILLLASLLGALVGLILLLLGRKGRKTPIPFGPFLALGGLIA 241
Peptidase_A24 pfam01478
Type IV leader peptidase family; Peptidase A24, or the prepilin peptidase as it is also known, ...
9-119 5.00e-12

Type IV leader peptidase family; Peptidase A24, or the prepilin peptidase as it is also known, processes the N-terminus of the prepilins. The processing is essential for the correct formation of the pseudopili of type IV bacterial protein secretion. The enzyme is found across eubacteria and archaea.


Pssm-ID: 426281  Cd Length: 101  Bit Score: 58.71  E-value: 5.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833442     9 ILYACLSALLFFWDAKHGLLPDRFTCPLLWSGLLFyqVCHPDGLADALWGAIIGYGTFAVIYwgyrilrHKEGLGYGDVK 88
Cdd:pfam01478   1 LVLLSLLLLLSVIDLRTRLIPNRLTLPLLWLGLIF--ALGLLSLLDALLGAAAGFLLLFLLY-------LKGGMGGGDVK 71
                          90       100       110
                  ....*....|....*....|....*....|.
gi 15833442    89 FLAALGAWHSWAFLPrLVFLAASFACGAVVI 119
Cdd:pfam01478  72 LLAALGAWLGWQLLL-LFLLLASLLGAILGL 101
 
Name Accession Description Interval E-value
PulO COG1989
Prepilin signal peptidase PulO (type II secretory pathway) or related peptidase [Cell motility, ...
4-146 2.43e-36

Prepilin signal peptidase PulO (type II secretory pathway) or related peptidase [Cell motility, Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 441592 [Multi-domain]  Cd Length: 256  Bit Score: 125.67  E-value: 2.43e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833442   4 TLPFLILYACLSALLFFWDAKHGLLPDRFTCPLLWSGLLFYQVCHPDGLADALWGAIIGYGTFAVIYWGYRILRHKEGLG 83
Cdd:COG1989 100 QLLAALLLLSLLLALSFIDLDTQLLPDSLTLPLLWLGLLLSLLGGFVSLLDALLGALAGYLLLWLIYWLFKLLTGKEGMG 179
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15833442  84 YGDVKFLAALGAWHSWAFLPrLVFLAASFACGAVVIGLLMRGKESLKNPLPFGPFLAAAGFVI 146
Cdd:COG1989 180 GGDVKLLAALGAWLGWQALL-LILLLASLLGALVGLILLLLGRKGRKTPIPFGPFLALGGLIA 241
Peptidase_A24 pfam01478
Type IV leader peptidase family; Peptidase A24, or the prepilin peptidase as it is also known, ...
9-119 5.00e-12

Type IV leader peptidase family; Peptidase A24, or the prepilin peptidase as it is also known, processes the N-terminus of the prepilins. The processing is essential for the correct formation of the pseudopili of type IV bacterial protein secretion. The enzyme is found across eubacteria and archaea.


Pssm-ID: 426281  Cd Length: 101  Bit Score: 58.71  E-value: 5.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833442     9 ILYACLSALLFFWDAKHGLLPDRFTCPLLWSGLLFyqVCHPDGLADALWGAIIGYGTFAVIYwgyrilrHKEGLGYGDVK 88
Cdd:pfam01478   1 LVLLSLLLLLSVIDLRTRLIPNRLTLPLLWLGLIF--ALGLLSLLDALLGAAAGFLLLFLLY-------LKGGMGGGDVK 71
                          90       100       110
                  ....*....|....*....|....*....|.
gi 15833442    89 FLAALGAWHSWAFLPrLVFLAASFACGAVVI 119
Cdd:pfam01478  72 LLAALGAWLGWQLLL-LFLLLASLLGAILGL 101
CpaA COG4960
Flp pilus assembly protein, peptidase CpaA [Posttranslational modification, protein turnover, ...
3-153 2.09e-06

Flp pilus assembly protein, peptidase CpaA [Posttranslational modification, protein turnover, chaperones, Signal transduction mechanisms];


Pssm-ID: 443986  Cd Length: 161  Bit Score: 44.88  E-value: 2.09e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833442   3 TTLPFLILYACLSALLFFWDAKHGLLPDRFTCPLLWSGLLFYQVCHP-DGLADALWGAIIGYGTFAVIYWgyrilrhKEG 81
Cdd:COG4960   4 LLLLLLLLLLALLAFAAYTDLRTRRIPNRLVLALLLLGLLLALLSGLlAGLGLSLLGALIGLAVGFPLFA-------LGG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833442  82 LGYGDVKFLAALGAWHSWAFLPrLVFLAASFACGAVVIGLLM--------------RGKESLKNPLPFGPFLAAAGFVIG 147
Cdd:COG4960  77 MGGGDVKLLAALGLWLGPAALL-LFLLLTALAGGVLALILLLlrrlpaaagrppwlARLRDRKRGVPYGVAIAAGALLAL 155

                ....*.
gi 15833442 148 WDSLLI 153
Cdd:COG4960 156 PASLLL 161
 
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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