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Conserved domains on  [gi|1277893522|gb|PIU99008.1|]
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PrsW family intramembrane metalloprotease, partial [Candidatus Wolfebacteria bacterium CG03_land_8_20_14_0_80_39_317]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PrsW-protease super family cl23838
PrsW family intramembrane metalloprotease; This family includes members such as the ...
 4-119 2.12e-16

PrsW family intramembrane metalloprotease; This family includes members such as the experimentally characterized PrsW protease from Bacillus subtilis. PrsW mediates site-1 cleavage of anti-sigma factor RsiW, and it senses antimicrobial peptides that damage the cell membrane and other agents that cause cell envelope stress. PrsW proteases, CPBP family (type II CAAX Proteases and Bacteriocin Processing enzymes), YhfC intramembrane metalloprotease, and APH-1 are distantly related. They share four predicted core transmembrane segments and possess similar, yet distinct sets of sequence motifs. The first N-terminal motif in PrsW bears the consensus signature of 'EExxK' the second motif 'FxxxE' and the third motif possess a conserved histidine. The fourth motif, 'HxxxB', is shared by the PrsW proteases and the CPBP, APH-1 and the YhfC families. Site-directed mutagenesis indicates that either double point mutation of the two conserved glutamates in the first motif (E75A/E76A), or a single mutation of the conserved histidine in the fourth motif (H175A), are of functional importance.


The actual alignment was detected with superfamily member COG2339:

Pssm-ID: 474075  Cd Length: 251  Bit Score: 72.24  E-value: 2.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893522   4 IFIFLGLLPSFAWLIFFLKEDVH-PEPKKMISRVFMAGALI-TFVAVGLQFLLRNILQSFQINEYHLVSFSFFGFIEETL 81
Cdd:COG2339    28 ILLLLALVPALALLAFFYWLDRYePEPLRLLLLAFLWGALVaVPAALLLNTLFGLLLPTEGDLGLFLGAFLVAGLVEEFA 107

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1277893522  82 KFLAAYLVVRKSPFFDEPIDAMIYMITAALGFAMVENI 119
Cdd:COG2339   108 KGLAVLLLLYRRREFDEPLDGIVYGAAVGLGFAFVENI 145
 
Name Accession Description Interval E-value
PrsW COG2339
Membrane proteinase PrsW, cleaves anti-sigma factor RsiW, M82 family [Signal transduction ...
 4-119 2.12e-16

Membrane proteinase PrsW, cleaves anti-sigma factor RsiW, M82 family [Signal transduction mechanisms];


Pssm-ID: 441909  Cd Length: 251  Bit Score: 72.24  E-value: 2.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893522   4 IFIFLGLLPSFAWLIFFLKEDVH-PEPKKMISRVFMAGALI-TFVAVGLQFLLRNILQSFQINEYHLVSFSFFGFIEETL 81
Cdd:COG2339    28 ILLLLALVPALALLAFFYWLDRYePEPLRLLLLAFLWGALVaVPAALLLNTLFGLLLPTEGDLGLFLGAFLVAGLVEEFA 107

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1277893522  82 KFLAAYLVVRKSPFFDEPIDAMIYMITAALGFAMVENI 119
Cdd:COG2339   108 KGLAVLLLLYRRREFDEPLDGIVYGAAVGLGFAFVENI 145
PrsW-protease pfam13367
PrsW family intramembrane metalloprotease; This family includes members such as the ...
 28-119 3.09e-11

PrsW family intramembrane metalloprotease; This family includes members such as the experimentally characterized PrsW protease from Bacillus subtilis. PrsW mediates site-1 cleavage of anti-sigma factor RsiW, and it senses antimicrobial peptides that damage the cell membrane and other agents that cause cell envelope stress. PrsW proteases, CPBP family (type II CAAX Proteases and Bacteriocin Processing enzymes), YhfC intramembrane metalloprotease, and APH-1 are distantly related. They share four predicted core transmembrane segments and possess similar, yet distinct sets of sequence motifs. The first N-terminal motif in PrsW bears the consensus signature of 'EExxK' the second motif 'FxxxE' and the third motif possess a conserved histidine. The fourth motif, 'HxxxB', is shared by the PrsW proteases and the CPBP, APH-1 and the YhfC families. Site-directed mutagenesis indicates that either double point mutation of the two conserved glutamates in the first motif (E75A/E76A), or a single mutation of the conserved histidine in the fourth motif (H175A), are of functional importance.


Pssm-ID: 433150  Cd Length: 195  Bit Score: 57.68  E-value: 3.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893522  28 EPKKMISRVFMAGALI-TFVAVGLQFLLRNILQSFQINEYHLVSFSFF--GFIEETLKFLAAYLVVRKSPFFDEPIDAMI 104
Cdd:pfam13367   1 EPWRLLLAAFLWGALVaVPLALLLNTLLQALLRLLSGGFGATFVAAFLvaPVVEETAKALGVLLLLYRRREFDEPLDGIV 80

                          90
                  ....*....|....*
gi 1277893522 105 YMITAALGFAMVENI 119
Cdd:pfam13367  81 YGAAVGLGFAVTENL 95
 
Name Accession Description Interval E-value
PrsW COG2339
Membrane proteinase PrsW, cleaves anti-sigma factor RsiW, M82 family [Signal transduction ...
 4-119 2.12e-16

Membrane proteinase PrsW, cleaves anti-sigma factor RsiW, M82 family [Signal transduction mechanisms];


Pssm-ID: 441909  Cd Length: 251  Bit Score: 72.24  E-value: 2.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893522   4 IFIFLGLLPSFAWLIFFLKEDVH-PEPKKMISRVFMAGALI-TFVAVGLQFLLRNILQSFQINEYHLVSFSFFGFIEETL 81
Cdd:COG2339    28 ILLLLALVPALALLAFFYWLDRYePEPLRLLLLAFLWGALVaVPAALLLNTLFGLLLPTEGDLGLFLGAFLVAGLVEEFA 107

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1277893522  82 KFLAAYLVVRKSPFFDEPIDAMIYMITAALGFAMVENI 119
Cdd:COG2339   108 KGLAVLLLLYRRREFDEPLDGIVYGAAVGLGFAFVENI 145
PrsW-protease pfam13367
PrsW family intramembrane metalloprotease; This family includes members such as the ...
 28-119 3.09e-11

PrsW family intramembrane metalloprotease; This family includes members such as the experimentally characterized PrsW protease from Bacillus subtilis. PrsW mediates site-1 cleavage of anti-sigma factor RsiW, and it senses antimicrobial peptides that damage the cell membrane and other agents that cause cell envelope stress. PrsW proteases, CPBP family (type II CAAX Proteases and Bacteriocin Processing enzymes), YhfC intramembrane metalloprotease, and APH-1 are distantly related. They share four predicted core transmembrane segments and possess similar, yet distinct sets of sequence motifs. The first N-terminal motif in PrsW bears the consensus signature of 'EExxK' the second motif 'FxxxE' and the third motif possess a conserved histidine. The fourth motif, 'HxxxB', is shared by the PrsW proteases and the CPBP, APH-1 and the YhfC families. Site-directed mutagenesis indicates that either double point mutation of the two conserved glutamates in the first motif (E75A/E76A), or a single mutation of the conserved histidine in the fourth motif (H175A), are of functional importance.


Pssm-ID: 433150  Cd Length: 195  Bit Score: 57.68  E-value: 3.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893522  28 EPKKMISRVFMAGALI-TFVAVGLQFLLRNILQSFQINEYHLVSFSFF--GFIEETLKFLAAYLVVRKSPFFDEPIDAMI 104
Cdd:pfam13367   1 EPWRLLLAAFLWGALVaVPLALLLNTLLQALLRLLSGGFGATFVAAFLvaPVVEETAKALGVLLLLYRRREFDEPLDGIV 80

                          90
                  ....*....|....*
gi 1277893522 105 YMITAALGFAMVENI 119
Cdd:pfam13367  81 YGAAVGLGFAVTENL 95
 
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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