ATP-dependent metalloprotease
function
cell division, sporulation initiation
product
ATP-dependent metalloprotease
Genomic Context
categories
[category|SW 1|Cellular processes] → [category|SW 1.1|Cell envelope and cell division] → [category|SW 1.1.8|Cell division] → [category|SW 1.1.8.2|Other genes][category|SW 3|Information processing] → [category|SW 3.3|Protein synthesis, modification and degradation] → [category|SW 3.3.7|Proteolysis] → [category|SW 3.3.7.4|Additional proteins involved in proteolysis][category|SW 4|Lifestyles] → [category|SW 4.1|Exponential and early post-exponential lifestyles] → [category|SW 4.1.2|Biofilm formation][category|SW 4|Lifestyles] → [category|SW 4.1|Exponential and early post-exponential lifestyles] → [category|SW 4.1.2|Biofilm formation] → [category|SW 4.1.2.4|Regulation][category|SW 4|Lifestyles] → [category|SW 4.3|Coping with stress] → [category|SW 4.3.2|Cell envelope stress proteins (controlled by SigM, V, W, X, Y)][category|SW 4|Lifestyles] → [category|SW 4.3|Coping with stress] → [category|SW 4.3.4|Heat shock proteins][category|SW 6|Groups of genes] → [category|SW 6.2|Membrane proteins][SW|Categories] containing this gene/protein
[SW|cell division], [SW|proteolysis], [SW|cell envelope stress proteins (controlled by SigM, V, W, X, Y)], [SW|heat shock proteins], [SW|biofilm formation], [SW|membrane proteins], [SW|sporulation/ other]This gene is a member of the following [SW|regulons]
[SW|SigM regulon], [SW|TilS-HprT regulon]Gene
Coordinates on the chromosome (coding sequence)
76,984 -> 78,897
Phenotypes of a mutant
defective in biofilm formation [Pubmed|22882210]strongly reduced sporulation frequency [Pubmed|22142536], [Pubmed|26735940]The protein
Catalyzed reaction/ biological activity
degrades [SW|Spo0E] and [SW|Spo0M], resulting in reduced sporulation frequency in a ''ftsH'' mutant [Pubmed|22142536][protein|search|FtsH] is involved in the degradation of [protein|search|EzrA] [Pubmed|24222488]degrades [SW|SpoIIE] [Pubmed|26465112]Paralogous protein(s)
[protein|search|YjoB]Effectors of protein activity
protease activity is controlled by the interaction with the flottilins [protein|search|FloA] and [protein|search|FloT] [Pubmed|24222488]Structure
[PDB|1LV7] (from ''E. coli'', 64% identity) [Pubmed|12176385][SW|Localization]
cell membrane [Pubmed|18763711]preferentially at the division septum [Pubmed|22882210]forms some foci in the membrane [Pubmed|22882210][SW|Interactions]
forms hexamers [Pubmed|26639779][SW|SpoVM]-[protein|search|FtsH] [Pubmed|10913836][protein|search|FloT]-[protein|search|FtsH] [Pubmed|26297017,22882210][protein|search|FloA]-[protein|search|FtsH] [Pubmed|22882210][protein|search|FtsH]-[SW|Spo0E] [Pubmed|22142536][protein|search|FtsH]-[SW|Spo0M] [Pubmed|22142536][SW|SpoIIE]-[SW|FtsH] [Pubmed|26465112]Expression and Regulation
Operon
''[protein|search|ftsH]'' [Pubmed|7608085]''[protein|search|tilS]-[protein|search|hprT]-[protein|search|ftsH]'' [Pubmed|18179421][SW|Sigma factor]
[protein|search|SigA] [Pubmed|7608085], [protein|search|SigM] [Pubmed|18179421]Regulation
induced by heat shock (class III)Regulatory mechanism
[protein|search|TilS]-[protein|search|HprT]: transcription activation [Pubmed|24001521]Additional information
the mRNA is very stable (half-life > 15 min) [http://www.ncbi.nlm.nih.gov/sites/entrez/12884008 PubMed]the [protein|search|FtsH] levels are reduced in a '[protein|search|floT] [protein|search|floA]' double mutant [PubMed|22882210]Biological materials
Mutant
1A1061 ( ''ftsH''::''cat''), [Pubmed|9076729], available at [http://pasture.asc.ohio-state.edu/BGSC/getdetail.cfm?bgscid=1A1061&Search=1A1061 BGSC]1A1060 ( ''ftsH''::''erm''), [Pubmed|10851010], available at [http://pasture.asc.ohio-state.edu/BGSC/getdetail.cfm?bgscid=1A1060&Search=1A1060 BGSC]References
Reviews
Original publications
10913836,12533473,9076729,10851010,9084181,15386101,10077851,19332814,12884008,7608085,9352926,19332814,18763711,12176385,18179421,24001521,22882210,22142536,24222488,26297017,26465112,26735940 
