The PepSY domain: a regulator of peptidase activity in the microbial environment?
The M4 family proteins are common eubacterial metallopeptidases that are involved in a range of functions from nutrient production to pathogenicity. Typically, they consist of a propeptide with inhibitory and chaperone functions and a peptidase unit. The propeptide is cleaved but remains attached un...
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| Veröffentlicht in: | Trends in biochemical sciences (Amsterdam. Regular ed.) 2004-04, Vol.29 (4), p.169-172 |
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| container_title | Trends in biochemical sciences (Amsterdam. Regular ed.) |
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| creator | Yeats, Corin Rawlings, Neil D. Bateman, Alex |
| description | The M4 family proteins are common eubacterial metallopeptidases that are involved in a range of functions from nutrient production to pathogenicity. Typically, they consist of a propeptide with inhibitory and chaperone functions and a peptidase unit. The propeptide is cleaved but remains attached until the peptidase is secreted and can be safely activated. Here, we describe a domain in the propeptide that is likely to contain the inhibitory activity, but not the chaperone activity. It is also in many non-peptidase proteins, including
Bacillus subtilis YpeB protein – a regulator of SleB spore cortex lytic enzyme – and a large number of eubacterial and archaeal cell-wall-associated and secreted proteins. We propose that it acts as a regulator of peptidase activity in the local environment and also protects the cell from lysis. |
| doi_str_mv | 10.1016/j.tibs.2004.02.004 |
| format | Article |
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Bacillus subtilis YpeB protein – a regulator of SleB spore cortex lytic enzyme – and a large number of eubacterial and archaeal cell-wall-associated and secreted proteins. We propose that it acts as a regulator of peptidase activity in the local environment and also protects the cell from lysis.</description><identifier>ISSN: 0968-0004</identifier><identifier>EISSN: 1362-4326</identifier><identifier>DOI: 10.1016/j.tibs.2004.02.004</identifier><identifier>PMID: 15124630</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Amino Acid Sequence ; Bacillus subtilis ; Bacteria - enzymology ; Bacteria - genetics ; Bacteria - metabolism ; Binding Sites - genetics ; Enzyme Activation ; Enzyme Precursors - genetics ; Enzyme Precursors - metabolism ; Metalloendopeptidases - chemistry ; Metalloendopeptidases - genetics ; Metalloendopeptidases - metabolism ; Molecular Sequence Data ; Protein Structure, Tertiary ; Regulatory Sequences, Nucleic Acid - genetics ; Sequence Homology, Amino Acid</subject><ispartof>Trends in biochemical sciences (Amsterdam. Regular ed.), 2004-04, Vol.29 (4), p.169-172</ispartof><rights>2004 Elsevier Ltd</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c449t-ecae9768875d6bf933ea02e54a8ecf0debe91b23884304730ea86c66049a72a53</citedby><cites>FETCH-LOGICAL-c449t-ecae9768875d6bf933ea02e54a8ecf0debe91b23884304730ea86c66049a72a53</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.tibs.2004.02.004$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,778,782,3539,27911,27912,45982</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15124630$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yeats, Corin</creatorcontrib><creatorcontrib>Rawlings, Neil D.</creatorcontrib><creatorcontrib>Bateman, Alex</creatorcontrib><title>The PepSY domain: a regulator of peptidase activity in the microbial environment?</title><title>Trends in biochemical sciences (Amsterdam. Regular ed.)</title><addtitle>Trends Biochem Sci</addtitle><description>The M4 family proteins are common eubacterial metallopeptidases that are involved in a range of functions from nutrient production to pathogenicity. Typically, they consist of a propeptide with inhibitory and chaperone functions and a peptidase unit. The propeptide is cleaved but remains attached until the peptidase is secreted and can be safely activated. Here, we describe a domain in the propeptide that is likely to contain the inhibitory activity, but not the chaperone activity. It is also in many non-peptidase proteins, including
Bacillus subtilis YpeB protein – a regulator of SleB spore cortex lytic enzyme – and a large number of eubacterial and archaeal cell-wall-associated and secreted proteins. 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Bacillus subtilis YpeB protein – a regulator of SleB spore cortex lytic enzyme – and a large number of eubacterial and archaeal cell-wall-associated and secreted proteins. We propose that it acts as a regulator of peptidase activity in the local environment and also protects the cell from lysis.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>15124630</pmid><doi>10.1016/j.tibs.2004.02.004</doi><tpages>4</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0968-0004 |
| ispartof | Trends in biochemical sciences (Amsterdam. Regular ed.), 2004-04, Vol.29 (4), p.169-172 |
| issn | 0968-0004 1362-4326 |
| language | eng |
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| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | Amino Acid Sequence Bacillus subtilis Bacteria - enzymology Bacteria - genetics Bacteria - metabolism Binding Sites - genetics Enzyme Activation Enzyme Precursors - genetics Enzyme Precursors - metabolism Metalloendopeptidases - chemistry Metalloendopeptidases - genetics Metalloendopeptidases - metabolism Molecular Sequence Data Protein Structure, Tertiary Regulatory Sequences, Nucleic Acid - genetics Sequence Homology, Amino Acid |
| title | The PepSY domain: a regulator of peptidase activity in the microbial environment? |
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