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0  structures 2173  species 0  interactions 3146  sequences 34  architectures

Family: PrsW-protease (PF13367)

Summary: PrsW family intramembrane metalloprotease

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PrsW family intramembrane metalloprotease Provide feedback

This family includes members such as the experimentally characterized PrsW protease from Bacillus subtilis P50738. 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.

Literature references

  1. Ellermeier CD, Losick R;, Genes Dev. 2006;20:1911-1922.: Evidence for a novel protease governing regulated intramembrane proteolysis and resistance to antimicrobial peptides in Bacillus subtilis. PUBMED:16816000 EPMC:16816000

  2. Pei J, Mitchell DA, Dixon JE, Grishin NV;, J Mol Biol. 2011;410:18-26.: Expansion of type II CAAX proteases reveals evolutionary origin of gamma-secretase subunit APH-1. PUBMED:21570408 EPMC:21570408

Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR026898

PrsW, appears to be a member of a widespread family of membrane proteins that includes at least one previously known protease. PrsW appears to be responsible for Site-1 cleavage of the RsiW anti-sigma factor, the cognate anti-sigma factor, and it senses antimicrobial peptides that damage the cell membrane and other agents that cause cell envelope stress, the three acidic residues, E75, E76 and E95 in B7GHM8 appear to be crucial since their mutation to alanine renders the protein inactive. Based on predictions of the bioinformatics programme TMHMM it is likely that these residues are located on the extracytoplasmic face of PrsW placing them in a position to act as a sensor for cell envelope stress [ PUBMED:16816000 ].

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Pfam Clan

This family is a member of clan Peptidase_U (CL0472), which has the following description:

This superfamily includes proteins classed as clan U by the MEROPS database. The proteins are membrane bound peptidases. The clan also includes Pfam:PF10086 which is a related family of uncharacterised proteins.

The clan contains the following 4 members:

Aph-1 PrsW-protease Rce1-like YhfC


We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...

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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

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Representative proteomes UniProt

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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

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HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...


This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

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Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Jackhmmer:B0SDU2
Previous IDs: none
Type: Family
Sequence Ontology: SO:0100021
Author: Coggill P , El-Gebali S
Number in seed: 64
Number in full: 3146
Average length of the domain: 196.10 aa
Average identity of full alignment: 23 %
Average coverage of the sequence by the domain: 54.43 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 57096847 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 23.5 23.5
Trusted cut-off 23.8 23.6
Noise cut-off 23.4 23.4
Model length: 196
Family (HMM) version: 8
Download: download the raw HMM for this family

Species distribution

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Archea Archea Eukaryota Eukaryota
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Viroids Viroids Unclassified sequence Unclassified sequence


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AlphaFold Structure Predictions

The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.

Protein Predicted structure External Information
C0H4H7 View 3D Structure Click here
Q2G1C5 View 3D Structure Click here

trRosetta Structure

The structural model below was generated by the Baker group with the trRosetta software using the Pfam UniProt multiple sequence alignment.

The InterPro website shows the contact map for the Pfam SEED alignment. Hovering or clicking on a contact position will highlight its connection to other residues in the alignment, as well as on the 3D structure.

Improved protein structure prediction using predicted inter-residue orientations. Jianyi Yang, Ivan Anishchenko, Hahnbeom Park, Zhenling Peng, Sergey Ovchinnikov, David Baker Proceedings of the National Academy of Sciences Jan 2020, 117 (3) 1496-1503; DOI: 10.1073/pnas.1914677117;