D,L-endopeptidase, peptidoglycan hydrolase for cell separation
product
D,L-endopeptidase, peptidoglycan hydrolase
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
2,115,425 → 2,116,669
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]Protein family
Cu-Zn superoxide dismutase family (according to Swiss-Prot)Paralogous protein(s)
the C-terminal D,L-endopeptidase domains of [protein|321F248C22D7283C0F3323F1F4069E36F8D7FE6C|LytE], [protein|E8B88CBE4F9121DFEEF099D7947CD1E1AE656160|LytF], [protein|0FBE3F7ECACA7FCFAA4EE32E9B2BB35F0B793C0F|CwlS], and [protein|4F9D70C4BB4FCA809BEAC341C3F8122FB7FD8872|CwlO] exhibit strong sequence similarity[SW|Domains]
contains four N-acetylglucosamine-polymer-binding [SW|LysM domain]s [Pubmed|24355088,18430080]C-terminal D,L-endopeptidase domain [Pubmed|22139507][SW|Localization]
cell membrane (according to Swiss-Prot)localizes to cell septa and poles [Pubmed|22139507]Expression and Regulation
Operons
genes
[gene|0FBE3F7ECACA7FCFAA4EE32E9B2BB35F0B793C0F|cwlS]
description
[pubmed|22383849]
sigma factors
[protein|7024E4162A6D827069F882FDEACA696EBC05DD40|SigD]: sigma factor, [pubmed|22139507], in [regulon|7024E4162A6D827069F882FDEACA696EBC05DD40|SigD regulon][protein|DC3449D5F195E5C2E9E14FEC95396C8F1FDF73B4|SigH]: sigma factor, [pubmed|22139507], in [regulon|DC3449D5F195E5C2E9E14FEC95396C8F1FDF73B4|SigH regulon]regulatory mechanism
[protein|E39AFEB7B7F28969A35C4B51CC6E7819F71C79D9|CcpA]: repression, [pubmed|], in [regulon|E39AFEB7B7F28969A35C4B51CC6E7819F71C79D9|CcpA regulon][protein|5872812AB61E92E2944E926915EB7FEE71BFA6D5|Abh]: repression, synergistic transcription repression with [protein|E5110D9C36E8C55AFD1419987B14A53232165F20|AbrB] [Pubmed|20817675], in [regulon|5872812AB61E92E2944E926915EB7FEE71BFA6D5|Abh regulon][protein|E5110D9C36E8C55AFD1419987B14A53232165F20|AbrB]: repression, synergistic transcription repression with [protein|5872812AB61E92E2944E926915EB7FEE71BFA6D5|Abh] [Pubmed|20817675], in [regulon|E5110D9C36E8C55AFD1419987B14A53232165F20|AbrB regulon]regulation
repressed by glucose (3-fold) ([protein|E39AFEB7B7F28969A35C4B51CC6E7819F71C79D9|CcpA]) [Pubmed|12850135]view in new tabgenes
[gene|0FBE3F7ECACA7FCFAA4EE32E9B2BB35F0B793C0F|cwlS]-[gene|3B45734D18D01BAB6D244DE3547C84F9488075FB|yojM]
description
[Pubmed|22383849]
view in new tabBiological materials
Mutant
MGNA-B424 (yojL::erm), available at the [https://shigen.nig.ac.jp/bsub/resource/strainGeneDisrupted/detail/1423 NBRP B. subtilis, Japan]References
Reviews
Original publications
16855244,12850135,22139507,20817675,24355088