[SW|cell shape]-determining protein, forms filaments, the polymers control/restrict the mobility of the cell wall elongation enzyme complex, required for [[protein|LytE ]]activity

[SW|cell shape]-determining protein, forms filaments, the polymers control/restrict the mobility of the cell wall elongation enzyme complex, required for [[protein|LytE ]]activity, part of the [[protein|Rod complex]] for lateral [SW|cell wall synthesis] and control of cell diameter

BSU28030

BSU_28030

1011

1014

BSU28030

BSU_28030

2,860,735 → 2,861,748

2,860,735 2,861,748

forms straight filaments in a heterologous system [Pubmed|21091501]

polymerizes in the presence of millimolar divalent cations, binds and hydrolyzes GTP and ATP [Pubmed|19117023]

involved in the organization of ϕ29 DNA replication machinery in peripheral helix-like structures [Pubmed|22420858]

required for [[protein|LytE]] activity [Pubmed|23869552]

forms straight filaments in a heterologous system [Pubmed|21091501]

polymerizes in the presence of millimolar divalent cations, binds and hydrolyzes GTP and ATP [Pubmed|19117023]

involved in the organization of 29 DNA replication machinery in peripheral helix-like structures [Pubmed|22420858]

required for [[protein|LytE]] activity [Pubmed|23869552]

ftsA/mreB family (according to Swiss-Prot)

[SW|FtsA/MreB family] (according to UniProt)

[[protein|Mbl]], [[protein|MreBH]]

[[this]]

during logarithmic growth, [[protein|MreB]] forms discrete patches that move processively along peripheral tracks perpendicular to the cell axis [Pubmed|21636744]

forms transverse bands as cells enter the stationary phase [Pubmed|21636744]

forms antiparallel double filaments [Pubmed|24843005]

close to the inner surface of the cytoplasmic membrane [Pubmed|16950129]

reports on helical structures formed by MreB [Pubmed|16950129,20566861] seem to be misinterpretation of data [Pubmed|21636744]

normal localization depends on the presence of glucolipids, [[protein|MreB]] forms irregular clusters in an ''[[gene|ugtP]]'' mutant [Pubmed|22362028]

during stationary phase: delocalized in the cytoplasm [Pubmed|26091431]

during development of [SW|genetic competence]: co-localizes with polar clusters of the late competence protein [[protein|ComGA]] ([[protein|ComGA]] sequesters [[protein|MreB]]) [Pubmed|26091431]

during logarithmic growth, [[protein|MreB]] forms discrete patches that move processively along peripheral tracks perpendicular to the cell axis [Pubmed|21636744]

forms transverse bands as cells enter the stationary phase [Pubmed|21636744]

forms antiparallel double filaments [Pubmed|24843005]

close to the inner surface of the cytoplasmic membrane [Pubmed|16950129]

reports on helical structures formed by MreB [Pubmed|16950129,20566861] seem to be misinterpretation of data [Pubmed|21636744]

normal localization depends on the presence of glucolipids, [[protein|MreB]] forms irregular clusters in an ''[[gene|ugtP]]'' mutant [Pubmed|22362028]

during stationary phase: delocalized in the cytoplasm [Pubmed|26091431]

during development of [SW|genetic competence]: co-localizes with polar clusters of the late competence protein [[protein|ComGA]] ([[protein|ComGA]] sequesters [[protein|MreB]]) [Pubmed|26091431]

MreB patch speed depends on the growth rate, the faster growth, the higher the patch speed [pubmed|28589952]

[SW|Jeff Errington], Newcastle University, UK [http://www.ncl.ac.uk/camb/staff/profile/jeff.errington homepage]

[SW|Peter Graumann], Freiburg University, Germany [http://www.biologie.uni-freiburg.de/data/bio2/graumann/index.htm homepage]

17506674, 17158703, 15037301, 21725336, 20825347, 21047262, 22166997, 22154164, 22652894, 21371139, 25578957, 25957405, 28500523

17506674, 17158703, 15037301, 21725336, 20825347, 21047262, 22166997, 22154164, 22652894, 21371139, 25578957, 25957405, 28500523, 28975672, 29355854, 29560261, 29522747, 33048060

17064365, 20566861, 21636744, 21636745, 22069484, 23783036, 24010660, 24843005, 25402772, 25676310

17064365, 20566861, 21636744, 21636745, 22069484, 23783036, 24010660, 24843005, 25402772, 25676310, 30696741, 30775967, 32973704

15752190, 11290328, 12809607, 1400224, 7836311, 16950129, 19192185, 19117023, 19643765, 19654094, 19659933, 8459776, 11544518, 20133608, 21091501, 21320184, 18179421, 21964069, 22343529, 22362028, 22420858, 21926231, 23879732, 23869552, 24261876, 24603761, 26091431, 17880425, 20233306, 27215790, 27376153, 28589952

15752190, 11290328, 12809607, 1400224, 7836311, 16950129, 19192185, 19117023, 19643765, 19654094, 19659933, 8459776, 11544518, 20133608, 21091501, 21320184, 18179421, 21964069, 22343529, 22362028, 22420858, 21926231, 23879732, 23869552, 24261876, 24603761, 26091431, 17880425, 20233306, 27215790, 27376153, 28589952, 30597729, 31086310, 32662773, 32686735

[SW|Jeff Errington], Newcastle University, UK [http://www.ncl.ac.uk/camb/staff/profile/jeff.errington homepage]

[SW|Peter Graumann], Freiburg University, Germany [http://www.biologie.uni-freiburg.de/data/bio2/graumann/index.htm homepage]