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212  structures 8444  species 0  interactions 17660  sequences 128  architectures

Family: Lon_C (PF05362)

Summary: Lon protease (S16) C-terminal proteolytic domain

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

This is the Wikipedia entry entitled "Lon protease family". More...

Lon protease family Edit Wikipedia article

ATP-dependent protease La (LON) domain
PDB 2ane EBI.jpg
crystal structure of n-terminal domain of e.coli lon protease
Identifiers
SymbolLON
PfamPF02190
Pfam clanCL0178
InterProIPR003111
SMARTLON
MEROPSS16
SCOP21zbo / SCOPe / SUPFAM
Lon protease (S16) C-terminal proteolytic domain
Identifiers
SymbolLON
PfamPF05362
Pfam clanCL0329
InterProIPR008269
MEROPSS16
SCOP21rr9 / SCOPe / SUPFAM

In molecular biology, the Lon protease family is a family of proteases. They are found in archaea, bacteria and eukaryotes. Lon proteases are ATP-dependent serine peptidases belonging to the MEROPS peptidase family S16 (lon protease family, clan SF). In the eukaryotes the majority of the Lon proteases are located in the mitochondrial matrix.[1][2] In yeast, the Lon protease PIM1 is located in the mitochondrial matrix. It is required for mitochondrial function, it is constitutively expressed but is increased after thermal stress, suggesting that PIM1 may play a role in the heat shock response.[3]


References

  1. ^ Wang N, Gottesman S, Willingham MC, Gottesman MM, Maurizi MR (1993). "A human mitochondrial ATP-dependent protease that is highly homologous to bacterial Lon protease". Proc. Natl. Acad. Sci. U.S.A. 90 (23): 11247–51. PMC 47959. PMID 8248235. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
  2. ^ Barakat S, Pearce DA, Sherman F, Rapp WD (1998). "Maize contains a Lon protease gene that can partially complement a yeast pim1-deletion mutant". Plant Mol. Biol. 37 (1): 141–54. PMID 9620272. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
  3. ^ Van Dyck L, Pearce DA, Sherman F (1994). "PIM1 encodes a mitochondrial ATP-dependent protease that is required for mitochondrial function in the yeast Saccharomyces cerevisiae". J. Biol. Chem. 269 (1): 238–42. PMID 8276800. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)

External links

MEROPS family S16

This article incorporates text from the public domain Pfam and InterPro: IPR003111

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Lon protease (S16) C-terminal proteolytic domain Provide feedback

The Lon serine proteases must hydrolyse ATP to degrade protein substrates. In Escherichia coli, these proteases are involved in turnover of intracellular proteins, including abnormal proteins following heat-shock. The active site for protease activity resides in a C-terminal domain. The Lon proteases are classified as family S16 in Merops.

Literature references

  1. Vasilyeva OV, Kolygo KB, Leonova YF, Potapenko NA, Ovchinnikova TV; , FEBS Lett 2002;526:66-70.: Domain structure and ATP-induced conformational changes in Escherichia coli protease Lon revealed by limited proteolysis and autolysis. PUBMED:12208506 EPMC:12208506


Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR008269

Lon (also known as endopeptidase La) is a multi-domain ATP- dependent protease found throughout all kingdoms of life. It is involved in protein quality control and several regulatory processes. All Lon proteases contain an ATPase domain belonging to the AAA+ superfamily of molecular machines, and a proteolytic domain with a serine-lysine catalytic dyad in which a lysine assists the catalytic serine in proteolytic cleavage. Lon proteases can be divided into two subfamilies: A type (A-Lons), which have a large multi-lobed N-terminal domain together with the ATPase and protease domains, and B type (B-Lons), which lack an N domain, but have a membrane-anchoring region emerging from the ATPase domain. B-Lons are found in Archaea, in which they are the lone membrane-anchored ATP-dependent protease. The soluble A-Lons are found in all bacteria and in eukaryotic cell organelles, such as mitochondria and peroxisomes, and are needed for recovery from various stress conditions [ PUBMED:14665623 , PUBMED:15456757 , PUBMED:16002085 , PUBMED:20834233 , PUBMED:20222013 , PUBMED:24520911 ]. The Lon proteolytic domain forms peptidase family S16 of clan SJ [ PUBMED:16002085 ].

The structure of the Lon proteolytic domain consists of six alpha helices and ten beta strands [ PUBMED:14665623 , PUBMED:15456757 , PUBMED:16002085 , PUBMED:20834233 , PUBMED:20222013 ].

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 S5 (CL0329), which has the following description:

This superfamily contains a wide range of families that possess a structure similar to the second domain of ribosomal S5 protein.

The clan contains the following 18 members:

ChlI DNA_gyraseB DNA_mis_repair EFG_IV Fae GalKase_gal_bdg GHMP_kinases_N IGPD Lon_C LpxC Morc6_S5 Ribonuclease_P Ribosomal_S5_C Ribosomal_S9 RNase_PH Topo-VIb_trans UPF0029 Xol-1_N

Alignments

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.

  Seed
(23)
Full
(17660)
Representative proteomes UniProt
(79301)
RP15
(2917)
RP35
(8949)
RP55
(17547)
RP75
(28489)
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HTML View             
PP/heatmap 1            

1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(23)
Full
(17660)
Representative proteomes UniProt
(79301)
RP15
(2917)
RP35
(8949)
RP55
(17547)
RP75
(28489)
Alignment:
Format:
Order:
Sequence:
Gaps:
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(23)
Full
(17660)
Representative proteomes UniProt
(79301)
RP15
(2917)
RP35
(8949)
RP55
(17547)
RP75
(28489)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download  

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

HMM logo

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...

Trees

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.

Note: You can also download the data file for the tree.

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: Merops
Previous IDs: none
Type: Domain
Sequence Ontology: SO:0000417
Author: Studholme DJ
Number in seed: 23
Number in full: 17660
Average length of the domain: 179.4 aa
Average identity of full alignment: 33 %
Average coverage of the sequence by the domain: 25.31 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 21.1 21.1
Trusted cut-off 21.1 21.1
Noise cut-off 21.0 21.0
Model length: 205
Family (HMM) version: 16
Download: download the raw HMM for this family

Species distribution

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Colour assignments

Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence

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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...

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Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Lon_C domain has been found. There are 212 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein 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
A0A077ZGW8 View 3D Structure Click here
A0A077ZIH0 View 3D Structure Click here
A0A077ZMC3 View 3D Structure Click here
A0A077ZMG7 View 3D Structure Click here
A0A0D2GQM6 View 3D Structure Click here
A0A0D2GZD3 View 3D Structure Click here
A0A0H3GJ60 View 3D Structure Click here
A0A0H3GR39 View 3D Structure Click here
A0A0K0EES4 View 3D Structure Click here
A0A0K0IZJ4 View 3D Structure Click here
A0A0N4U770 View 3D Structure Click here
A0A0R4IH79 View 3D Structure Click here
A0A175W1N7 View 3D Structure Click here
A0A175W2U6 View 3D Structure Click here
A0A1C1C9V4 View 3D Structure Click here
A0A1C1CR16 View 3D Structure Click here
A0A1D6ETU0 View 3D Structure Click here
A0A1D6F4Q7 View 3D Structure Click here
A0A1D6IP30 View 3D Structure Click here
A0A1D6K094 View 3D Structure Click here
A0A1D6NGE9 View 3D Structure Click here
A0A2K6VQS2 View 3D Structure Click here
A0A3P7ECT6 View 3D Structure Click here
A0A3Q0KL23 View 3D Structure Click here
A0A486WX02 View 3D Structure Click here
A0A5K4ELM8 View 3D Structure Click here
A0A5S9MRR3 View 3D Structure Click here
A0L516 View 3D Structure Click here
A0LEE9 View 3D Structure Click here
A0LG61 View 3D Structure Click here
A2QCJ2 View 3D Structure Click here
A2RAF6 View 3D Structure Click here
A2YQ56 View 3D Structure Click here
A3LUF7 View 3D Structure Click here
A3M072 View 3D Structure Click here
A4J7L6 View 3D Structure Click here
A4S6Y4 View 3D Structure Click here
A5EWF3 View 3D Structure Click here
A5IYF2 View 3D Structure Click here
A6LD45 View 3D Structure Click here