gamma-D-glutamate-meso-diaminopimelate muropeptidase, cell separase (major autolysin)
product
gamma-D-glutamate-meso-diaminopimelate muropeptidase (major autolysin)
Genomic Context
categories
[category|SW 1|Cellular processes] → [category|SW 1.1|Cell envelope and cell division] → [category|SW 1.1.3|Cell wall degradation/ turnover] → [category|SW 1.1.3.1|Autolysis][category|SW 1|Cellular processes] → [category|SW 1.1|Cell envelope and cell division] → [category|SW 1.1.3|Cell wall degradation/ turnover] → [category|SW 1.1.3.4|Endopeptidases]Gene
Coordinates
1,011,792 → 1,013,258
Phenotypes of a mutant
cell separation defect, this is increased by a ''[gene|321F248C22D7283C0F3323F1F4069E36F8D7FE6C|lytE]'' mutation [Pubmed|23855774]The protein
Catalyzed reaction/ biological activity
cleaves the peptide bond between D-Glu (position 2 in the peptioglycan peptide) and m-diamino pimelic acid (position 3) [Pubmed|18266855]degradation of gamma-polyglutamic acid [pubmed|29458655]Protein family
[SW|Peptidase C40 family] (according to UniProt)[SW|Domains]
contains five N-acetylglucosamine-polymer-binding [SW|LysM domain]s [Pubmed|18430080]C-terminal D,L-endopeptidase domain ([SW|NlpC/P60 domain]) [pubmed|29458655,22139507]5 [SW|LysM domain]s (aa 27-70, aa 92-135, aa 174-217, aa 240-283, aa 307-350) (according to UniProt)Effectors of protein activity
both enzymatic activities are inhibited by interaction with [protein|0CA55371306D4BD768CFA82027DCB4D581BCCB87|IseA] [pubmed|29458655]Structure
[PDB|4XCM] (from Thermus thermophilus, 31% identity) [pubmed|25760608][SW|Localization]
secreted (according to Swiss-Prot)localizes to cell septa and poles on the vegetative cell surface, this depends on the presence of lipoteichoic acids ([protein|418900B6DBDF3EF300C930B0C75E31B939F3CE00|LtaS]) [Pubmed|25288647,22139507]Expression and Regulation
Operons
genes
[gene|E8B88CBE4F9121DFEEF099D7947CD1E1AE656160|lytF]
description
[Pubmed|10322020]
sigma factors
[protein|7024E4162A6D827069F882FDEACA696EBC05DD40|SigD]: sigma factor, [Pubmed|10322020], in [regulon|7024E4162A6D827069F882FDEACA696EBC05DD40|SigD regulon]regulatory mechanism
[protein|920F91E748EE079FF864011D9052B073567C41E4|SlrR]: repression, in [regulon|920F91E748EE079FF864011D9052B073567C41E4|SlrR regulon][protein|5A6FBAE6553343092862CB79E150F934978C32A9|SinR]: repression, in [regulon|5A6FBAE6553343092862CB79E150F934978C32A9|SinR regulon]view in new tabBiological materials
Mutant
1A791 ( ''lytF''::''spec''), [Pubmed|10206711], available at [http://pasture.asc.ohio-state.edu/BGSC/getdetail.cfm?bgscid=1A791&Search=1A791 BGSC]1A792 ( ''lytF''::''spec''), [Pubmed|1588906], available at [http://pasture.asc.ohio-state.edu/BGSC/getdetail.cfm?bgscid=1A792&Search=1A792 BGSC]BKE09370 (Δ[gene|E8B88CBE4F9121DFEEF099D7947CD1E1AE656160|lytF]::erm trpC2) available at [http://www.bgsc.org/getdetail.php?bgscid=BKE09370 BGSC], [Pubmed|28189581], upstream reverse: _UP1_CATCTTAGCTCTCCTTTTTC, downstream forward: _UP4_TAAAAACAGAAACTGTGCGGBKK09370 (Δ[gene|E8B88CBE4F9121DFEEF099D7947CD1E1AE656160|lytF]::kan trpC2) available at [http://www.bgsc.org/getdetail.php?bgscid=BKK09370 BGSC], [Pubmed|28189581], upstream reverse: _UP1_CATCTTAGCTCTCCTTTTTC, downstream forward: _UP4_TAAAAACAGAAACTGTGCGGReferences
Reviews
Original publications
20351052,10322020,10206711,14594841,18761696,19542270,22139507,23855774,23091053,25288647,29458655,29458657,25760608