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Literature summary for 2.4.1.129 extracted from

  • Karinou, E.; Schuster, C.F.; Pazos, M.; Vollmer, W.; Gruendling, A.
    Inactivation of the monofunctional peptidoglycan glycosyltransferase SgtB allows Staphylococcus aureus to survive in the absence of lipoteichoic acid (2019), J. Bacteriol., 201, e00574-18 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.4.1.129

Protein Variants

Protein Variants Comment Organism
additional information introduction of wild-type and mutant SgtBs in a wild-type Staphylococcus aureus strain and in an ltaS mutant strain (ANG2135) deficient in lipoteichoic acid (LTA). Growth and cell morphology of wild-type and mutant strains. Introduction of SgtB or MazE in the respective suppressor strain results in growth arrest. Inactivation of MazE or SgtB is sufficient to allow Staphylococcus aureus to grow in the absence of LTA. Inactivation of SgtB leading to an increase in peptidoglycan cross-linking in an LTA-negative Staphylococcus aureus strain. Increased resistance of the sgtB mutant to oxacillin Staphylococcus aureus

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
 Staphylococcus aureus 16020
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol Staphylococcus aureus
-
 [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Staphylococcus aureus W8U4T4
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
-
 Staphylococcus aureus [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
-
 ?

Synonyms

Synonyms Comment Organism
MGT
-
 Staphylococcus aureus
PBP
-
 Staphylococcus aureus
penicillin binding protein
-
 Staphylococcus aureus
SgtB
-
 Staphylococcus aureus

General Information

General Information Comment Organism
malfunction an Staphylococcus aureus sgtB transposon mutant, with the monofunctional peptidoglycan glycosyltransferase SgtB inactivated, display a 4fold increase in the MIC of oxacillin, suggesting that alterations in the peptidoglycan structure can help bacteria compensate for the lack of lipoteichoic acid (LTA). Muropeptide analysis of peptidoglycans isolated from a wild-type strain and sgtB mutant strain does not reveal any sizable alterations in the peptidoglycan structure. In contrast, the peptidoglycan isolated from an LTA-negative ltaS mutant strain shows a significant reduction in the fraction of highly cross-linked peptidoglycan, which is partially rescued in the sgtB ltaS double mutant suppressor strain. Introduction of SgtB or MazE in the respective suppressor strain results in growth arrest. Increased resistance of the sgtB mutant to oxacillin. The increase in peptidoglycan cross-linking potentially strengthens the cell wall to better sustain the high internal turgor pressure and might be at least partly responsible for the observed growth improvement Staphylococcus aureus
physiological function Staphylococcus aureus has a typical Gram-positive cell envelope, which consists of a cytoplasmic membrane surrounded by a thick peptidoglycan layer. The peptidoglycan layer is a dynamic macromolecular structure that undergoes constant cycles of polymerization and hydrolysis to allow bacteria to grow and to divide. It is composed of glycan chains made of alternating N-acetylglucosamine and N-acetylmuramic acid residues connected by peptide bridges. This mesh-like sacculus is able to protect the cell from environmental threats while withstanding the high internal osmotic pressure. The final steps of peptidoglycan synthesis are catalyzed by enzymes termed penicillin binding proteins (PBPs) and coordinated actions of these enzymes are crucial for cell survival. PBPs with glycosyltransferase and transpeptidase activities polymerize the glycan chains and form peptide cross-bridges, while monofunctional transpeptidases, e.g. the monofunctional peptidoglycan glycosyltransferase SgtB in Staphylococcus aureus, have only the former activity. Important function of lipoteichoic acid (LTA) in cell wall integrity through its necessity for proper peptidoglycan assembly Staphylococcus aureus