ponA
168
major Class A penicillin-binding protein 1A/1B, contributes to cell elongation and [wiki|cell division], required for the control of cell diameter (together with the [wiki|Rod complex])
locus
BSU_22320
Molecular weight
99.36 kDa
pI
4.75
function
bifunctional glucosyltransferase/ transpeptidase, polymerizes and cross-links peptidoglycan
product
penicillin-binding protein 1A/1B, member of the [wiki|divisome]
essential
no
synonyms
ponA
Outlinks
Genomic Context
Categories containing this gene/protein
List of homologs in different organisms, belongs to COG0744 (Galperin et al., 2021)
This gene is a member of the following regulons
Gene
Coordinates
2,341,444 2,344,188
Phenotypes of a mutant
the mutant tends to acquire suppressor mutations that result in improved growth [Pubmed|28189581]
prevents bulging of the cells when grown at low Mg2+ concentrations, suppresses the lethal effect of a [gene|A4C8719E06F774A6EB4D79757CC79CF89E453A54|mreB] mutation [Pubmed|19192185]
deletion of [gene|A8EEC896B279CFDDE9C3A6F146A04EC822E33A4F|ponA] restores growth and normal shape of a [gene|7150BABA5086D5E2EB8102E4901A216F43576282|glmR] mutant on gluconeogenic carbon sources [Pubmed|21320184]
a strain lacking all four class A [wiki|penicillin-binding proteins] ([gene|A8EEC896B279CFDDE9C3A6F146A04EC822E33A4F|ponA] [gene|E50D4B30C2A0987A356C988AF8A4951C0CDF6C06|pbpD] [gene|73275060537497E6A9859856C9F040763E36316B|pbpF] [gene|BDC2D775CCE7C06F5619BAC214F29CFC637FE804|pbpG]) is severely inhibited for L-form switching in the presence of D-cycloserine [pubmed|29456081]
a [gene|3DEAC421B4B173C6BBC700E57790751B7AFDF319|sigI] [gene|A8EEC896B279CFDDE9C3A6F146A04EC822E33A4F|ponA] double mutant is not viable due to its inability to repair gaps in the peptidoglycan mesh [Pubmed|36265902]
reduced survival after [category|SW.3.1.1|DNA replication] arrest imposed by inhibition of [protein|FB97DF0C147FB29944F60214CB9BC1803861DAA0|polC] activity [pubmed|36574412]
impaired growth on complex medium, this can be suppressed by the addition of Mg2+ or by deletion of [gene|4385EA135BDEB54B33C9A8E39150A60C83C0CEEA|mprF] [pubmed|36744964]
[gene|A8EEC896B279CFDDE9C3A6F146A04EC822E33A4F|ponA] [gene|59A7B26F810D7FEB07C176A8B2ECF6B83803DE49|ecsA], [gene|A8EEC896B279CFDDE9C3A6F146A04EC822E33A4F|ponA] [gene|3DEAC421B4B173C6BBC700E57790751B7AFDF319|sigI], and [gene|A8EEC896B279CFDDE9C3A6F146A04EC822E33A4F|ponA] [gene|CB50289535EA537F63BADD459BD11AA7759A6658|rasP] double mutants have a growth defect that can be suppressed by reduced fatty acid synthesis (mutations in [gene|22B3039DF4D106F121DBC765F49878C9B324FDB2|accA], [gene|ADD1CE87C1C5BA44FFF5499EA5E155C4C53A1C22|accB], [gene|1DFFEB155028A5C6B4B344769EF7DAAC14983322|accC], [gene|E4997526CC534E38413030E90F7A135ECF65DF40|accD] or downregulation of the [wiki|FapR regulon] due to specific mutations in [gene|FCDE900167AE36377979E0CF7BC33C7F351B95D3|fapR]) [pubmed|37017514]
The protein
Catalyzed reaction/ biological activity
[GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)](n)-diphospho-di-trans,octa-cis-undecaprenol + β-D-GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-di-trans,octa-cis-undecaprenol --> [GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-diphospho-di-trans-octa-cis-undecaprenol + di-trans,octa-cis-undecaprenyl diphosphate + H+ (according to UniProt)
Preferential cleavage: (Ac)(2)-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine (according to UniProt)
contributes to the control of cell diameter (cell diameter increases with PonA levels), acts antogonistically to the [wiki|Rod complex] [pubmed|31086310]
Protein family
N-terminal part: [wiki|glycosyltransferase 51 family] (according to UniProt)
C-terminal part: [wiki|transpeptidase family] (according to UniProt)
[wiki|Domains]
Fibronectin type-III (aa 708-795) (according to UniProt)
extracellular C-terminal intrinsically disordered region, directs synthase activity to sites of gaps in the peptidoglycan mesh to repair them [pubmed|36265902]
Structure
[PDB|3DWK] (from Staphylococcus aureus, aa 71 ... 656, 38% identity) [pubmed|18760285]
[AF|P39793]
Paralogous protein(s)
[protein|E50D4B30C2A0987A356C988AF8A4951C0CDF6C06|pbpD], [protein|73275060537497E6A9859856C9F040763E36316B|pbpF], [protein|BDC2D775CCE7C06F5619BAC214F29CFC637FE804|pbpG]
[wiki|Localization]
membrane associated [Pubmed|18763711]
anchored to the membrane, the major part is exposed to the outside (according to UniProt)
localizes to the spore septum during sporulation [Pubmed|15758244,15262952]
during vegetative growth: septal, low flourescence at periphery [pubmed|14731276]
localizes to the vegetative septum [Pubmed|15262952], this depends on [protein|7150BABA5086D5E2EB8102E4901A216F43576282|glmR] [Pubmed|21320184]
Additional information
the protein shifts from PBP1A to Pbp1B under alkaline conditions [pubmed|36993441]
Expression and Regulation
Operons
genes
[gene|ED1E2011C7E43A8B7E9FD9A471BC11B9DEA73177|recU]-[gene|A8EEC896B279CFDDE9C3A6F146A04EC822E33A4F|ponA]
description
[Pubmed|7814321]
regulation
constitutive during vegetative growth [Pubmed|15758244]
sigma factors
[protein|081DF3EE9FA56209D648C7677188C61CE3AA8E41|sigM]: sigma factor, [Pubmed|18179421], in [regulon|protein:081DF3EE9FA56209D648C7677188C61CE3AA8E41|sigM regulon]
[protein|360F48D576DE950DF79C1A2677B7A35A8D8CC30C|sigA]: sigma factor, [Pubmed|22211522], in [regulon|protein:360F48D576DE950DF79C1A2677B7A35A8D8CC30C|sigA regulon]
Biological materials
Mutant
BKE22320 ([gene|A8EEC896B279CFDDE9C3A6F146A04EC822E33A4F|ponA]::erm trpC2) available at [http://bgsc.org/getdetail.php?bgscid=BKE22320 BGSC], [Pubmed|28189581], upstream reverse: _UP1_CATAACATCTCAACCTTTCG, downstream forward: _UP4_TAAACAAAAAAGCCGTCACC
BKK22320 ([gene|A8EEC896B279CFDDE9C3A6F146A04EC822E33A4F|ponA]::kan trpC2) available at [http://bgsc.org/getdetail.php?bgscid=BKK22320 BGSC], [Pubmed|28189581], upstream reverse: _UP1_CATAACATCTCAACCTTTCG, downstream forward: _UP4_TAAACAAAAAAGCCGTCACC
two-hybrid system
''B. pertussis'' adenylate cyclase-based bacterial two hybrid system ([wiki|BACTH]), available in [wiki|Jeff Errington] lab
GFP fusion
2083 [gene|0467447B10EE7C1FDF86022AB6FBDBABFD32A9E5|trpC]2 [gene|A8EEC896B279CFDDE9C3A6F146A04EC822E33A4F|ponA]::pSG1492 (cat Pxyl-gfpa-[gene|A8EEC896B279CFDDE9C3A6F146A04EC822E33A4F|ponA]1-394) [pubmed|14731276], available in [wiki|Dirk Jan Scheffers]' lab and in the [http://bgsc.org BGSC]
labs
[wiki|Jeff Errington], Newcastle University, UK [http://www.ncl.ac.uk/camb/staff/profile/jeff.errington homepage]
References
Reviews
Original Publications
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Time of last update: 2024-12-19 21:32:13
Author of last update: Jstuelk