Family C58

Family

Summary Holotypes Alignment Tree Genomes Structure Literature

C58A

Summary Holotypes Alignment Tree Genomes Literature

C58B

Summary Holotypes Alignment Tree Genomes Literature

Summary for family C58

Family type peptidaseC58.001 - YopT peptidase (Yersinia pestis), MEROPS Accession MER0019811 (peptidase unit: 102-322)
Content of familyFamily C58 contains endopeptidases that also act as transamidases, attaching a lipid moiety to the newly exposed N-terminus of the substrate.
History Identifier created: MEROPS 6.0 (30 August 2002)
It was shown by Shao et al. (2002) that two homologous proteins that are involved in bacterial pathogenesis, YopT (C58.001) and AvrPphB (C58.002 ) are cysteine peptidases.
Catalytic typeCysteine
Active siteThe catalytic residues Cys98, His212 and Asp227 form an active site triad similar to that of papain, and Asn93 is the residue important for formation of the oxyanion hole (Zhu et al., 2004) (see the Alignment).
Activities and specificitiesAvrPphB activates itself by cleaving the Lys62Gly bond, and the newly exposed N-terminal Gly is then lipid-modified. Amongst other proteins, only those with a prenylated cysteine are substrates. Substrates include RhoA, the Rac and Cdc42 GTPases and host serine/threonine kinase PBS1 (which is cleaved at a single bond: Zhu, M. et al., 2004).
Molecular structureThe tertiary structure of AvrPphB has been determined (Zhu et al., 2004) and is similar to that of papain (C01.001). Family C58 is therefore included in clan CA.
ClanCA
Distribution of family Bacteria details  
Archaea -  
Protozoa -  
Fungi -  
Plants -  
Animals -  
Viruses -  
Biological functionsThe plague organism Yersinia pestis is able to disarm the host immune response by interfering with cell-signalling pathways. The outer membrane protein YopT switches off macrophage phagocytosis by inactivating the host GTPase RhoA. RhoA is cleaved near its C-terminus, N-terminal to a prenylated cysteine by which RhoA is attached to the membrane. Solubilized RhoA is no longer able to function in its cell-signalling pathway.
The plant pathogen Pseudomonas syringae causes halo blight disease in beans. The bacterium secretes an avirulence protein, AvrPphB, which induces onset of the disease. However, in plants harbouring the resistance genes PBS1 and RPS5, AvrPphB induces localized cell death at the infection site, thus diminishing pathogen growth.
ReviewsShao & Dixon (2004); Viboud & Bliska (2004)
Statistics for family C58Sequences:51
Identifiers:6
Identifiers with PDB entries:2
Downloadable files Sequence library (FastA format)
Sequence alignment (FastA format)
Phylogenetic tree (Newick format)
Subfamily C58A
Name Peptidase subfamily C58A
Subfamily type peptidase C58.001 - YopT peptidase (Yersinia pestis), MEROPS Accession MER0019811 (peptidase unit: 102-322)
Active site residues C139 H258 D274 
Statistics Sequences: 35
Identifiers: 1
Identifiers with PDB entries: 1
Other databases INTERPRO IPR003951
PFAM PF03543
SCOP 102723
Downloadable files Sequence library [FastA format]
Sequence alignment [FastA format]
Phylogenetic tree [Newick format]
Peptidases and Homologues MEROPS ID Structure
YopT peptidaseC58.001-
subfamily C58A unassigned peptidasesunassignedYes
Subfamily C58B
Name Peptidase subfamily C58B
Subfamily type peptidase C58.003 - HopN1 peptidase ({Pseudomonas} sp.) (Pseudomonas syringae), MEROPS Accession MER0029084 (peptidase unit: 119-321)
Active site residues C172 H283 D299 
Statistics Sequences: 16
Identifiers: 5
Identifiers with PDB entries: 1
Other databases PFAM PF03543
Downloadable files Sequence library [FastA format]
Sequence alignment [FastA format]
Phylogenetic tree [Newick format]
Peptidases and Homologues MEROPS ID Structure
AvrPphB peptidaseC58.002Yes
HopN1 peptidase (Pseudomonas sp.)C58.003-
NopT g.p. (Rhizobium sp. NGR234)C58.004-
RipT g.p. (Ralstonia solanacearum GMI1000)C58.005-
ORF4 g.p. (Pseudomonas syringae)C58.007-
subfamily C58B unassigned peptidasesunassigned-
Peptidases not assigned to subfamily
Peptidases and Homologues MEROPS ID Structure
family C58 non-peptidase homologuesnon-peptidase homologue-
family C58 unassigned peptidasesunassigned-