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InterPro: IPR011096 Propeptide, peptidase M4/M36

Protein matchesHelp
UniProtKB
Matches:
1152 proteins
AccessionHelp IPR011096 Propeptide_peptidase_M4/M36
TypeHelp Domain
SignaturesHelp
GO Term annotationHelp
Function GO:0004222 metalloendopeptidase activity
GO:0008270 zinc ion binding
InterPro annotation
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AbstractHelp

The FTP domain is found in the propeptide region of bacterial and fungal metallopeptidases belonging to MEROPS peptidase families M4 and M36 respectively. In bacteria the FTP domain is N-terminal to this entry, the PepSY domain; in fungi the M36 peptidases do not contain the PepSY domain. Propeptide swapping experiments have shown that the propeptides of the M4 and M36 families are not functionally interchangeable [1].

The function of the propeptide in M36 peptidases has not been described, but it is likely, as in other related peptidases, to have targeting, chaperone activity and to inhibit peptidase activity, so as to prevent premature activation [1, 2].

Database linksHelp
Enzyme: EC:3.4.24
PANDIT: PF07504
Blocks: IPB011096
MEROPS: M36 , M4

Taxonomic coverageHelp

Example proteinsHelp
A5YCB9 Extracellular metalloproteinase 5

P00800 Thermolysin

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Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR001842 Peptidase M36, fungalysin
IPR001570 Peptidase M4, thermolysin C-terminal
IPR005075 Peptidase M4, propeptide, PepSY
IPR011096 Propeptide, peptidase M4/M36
IPR013856 Peptidase M4, thermolysin
PDB Chain
CATH Domain
SCOP Domain

PublicationsHelp
1. Tang B, Nirasawa S, Kitaoka M, Marie-Claire C, Hayashi K.
General function of N-terminal propeptide on assisting protein folding and inhibiting catalytic activity based on observations with a chimeric thermolysin-like protease.
Biochem. Biophys. Res. Commun. 301 1093-8 2003 [PubMed: 12589825]
http://dx.doi.org/10.1016/S0006-291X(03)00084-6
2. Markaryan A, Lee JD, Sirakova TD, Kolattukudy PE.
Specific inhibition of mature fungal serine proteinases and metalloproteinases by their propeptides.
J. Bacteriol. 178 2211-5 1996 [PubMed: 8636020]
http://jb.asm.org/cgi/content/abstract/178/8/2211

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