STRINGSTRING
slt slt ftsI ftsI ftsW ftsW ftsZ ftsZ mrcB mrcB mrdB mrdB mrdA mrdA ybgC ybgC tolQ tolQ tolR tolR tolB tolB pal pal ybgF ybgF lpoB lpoB mepS mepS zapA zapA lpoA lpoA mreB mreB mrcA mrcA
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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sltLytic murein transglycosylase, soluble; Murein-degrading enzyme. Catalyzes the cleavage of the glycosidic bonds between N-acetylmuramic acid and N-acetylglucosamine residues in peptidoglycan. May play a role in recycling of muropeptides during cell elongation and/or cell division. (645 aa)
ftsITranspeptidase involved in septal peptidoglycan synthesis; Essential cell division protein that catalyzes cross-linking of the peptidoglycan cell wall at the division septum. Required for localization of FtsN. Belongs to the transpeptidase family. FtsI subfamily. (588 aa)
ftsWPutative lipid II flippase; Peptidoglycan polymerase that is essential for cell division (Probable). Functions probably in conjunction with the penicillin- binding protein 3 (ftsI). Required for localization of FtsI. (414 aa)
ftsZGTP-binding tubulin-like cell division protein; Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity. Polymerization and bundle formation is enhanced by CbeA. (383 aa)
mrcBFused glycosyl transferase and transpeptidase; Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross- linking of the peptide subunits); In the N-terminal section; belongs to the glycosyltransferase 51 family. (844 aa)
mrdBCell wall shape-determining protein; Peptidoglycan polymerase that is essential for cell wall elongation. Also required for the maintenance of the rod cell shape. Functions probably in conjunction with the penicillin-binding protein 2 (mrdA). (370 aa)
mrdAPenicillin-binding protein 2, transpeptidase involved in peptidoglycan synthesis; Catalyzes cross-linking of the peptidoglycan cell wall. Responsible for the determination of the rod shape of the cell. Is probably required for lateral peptidoglycan synthesis and maintenance of the correct diameter during lateral and centripetal growth. Belongs to the transpeptidase family. MrdA subfamily. (633 aa)
ybgCacyl-CoA thioester hydrolase; Thioesterase that appears to be involved in phospholipid metabolism. Some specific acyl-ACPs could be physiological substrates. Displays acyl-CoA thioesterase activity on malonyl-CoA in vitro, catalyzing the hydrolysis of the thioester bond. (134 aa)
tolQMembrane spanning protein in TolA-TolQ-TolR complex; Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. Required, with TolR, for the proton motive force-dependent activation of TolA and for TolA-Pal interaction. Is also involved in the uptake of group A colicins (colicins A, E1, E2, E3, and K) and in the uptake of filamentous phage DNA. The Tol-Pal system is also required for polar localization of chemoreceptors clusters. Belongs to the ExbB/TolQ family. (230 aa)
tolRMembrane spanning protein in TolA-TolQ-TolR complex; Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. Required, with TolQ, for the proton motive force-dependent activation of TolA and for TolA-Pal interaction .The Tol-Pal system is also required for polar localization of chemoreceptors clusters (Probable). There are about 900 TolR molecules per cell. Modeling suggests that non-covalent binding of OmpA (from the outer membrane) and TolR (from the inner membrane) to peptidoglycan [...] (142 aa)
tolBPeriplasmic protein; Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. TolB occupies a key intermediary position in the Tol-Pal system because it communicates directly with both membrane-embedded components, Pal in the outer membrane and TolA in the inner membrane. Is also involved in the uptake of some colicins A. The Tol-Pal system is also required for polar localization of chemoreceptors clusters. (430 aa)
palPeptidoglycan-associated outer membrane lipoprotein; Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. The Tol-Pal system is also required for polar localization of chemoreceptors clusters. (173 aa)
ybgFPeriplasmic TolA-binding protein; Mediates coordination of peptidoglycan synthesis and outer membrane constriction during cell division. Promotes physical and functional coordination of the PBP1B-LpoB and Tol machines, and regulates PBP1B activity in response to Tol energy state. (263 aa)
lpoBOM lipoprotein stimulator of MrcB transpeptidase; Regulator of peptidoglycan synthesis that is essential for the function of penicillin-binding protein 1B (PBP1b). Stimulates transpeptidase and transglycosylase activities of PBP1b in vitro. May also contribute to outer membrane constriction during cell division, in complex with PBP1b. (213 aa)
mepSMurein DD-endopeptidase MepS/Murein LD-carboxypeptidase; A murein DD-endopeptidase with specificity for D-Ala-meso- diaminopimelic acid (mDAP) cross-links. Its role is probably to cleave D-Ala-mDAP cross-links to allow insertion of new glycans and thus cell wall expansion. Functionally redundant with MepM and MepH. Also has weak LD-carboxypeptidase activity on L-mDAP-D-Ala peptide bonds. Partially suppresses a prc disruption mutant. Belongs to the peptidase C40 family. (188 aa)
zapAFtsZ stabilizer; Activator of cell division through the inhibition of FtsZ GTPase activity, therefore promoting FtsZ assembly into bundles of protofilaments necessary for the formation of the division Z ring. It is recruited early at mid-cell but it is not essential for cell division; Belongs to the ZapA family. Type 1 subfamily. (109 aa)
lpoAOM lipoprotein stimulator of MrcA transpeptidase; Regulator of peptidoglycan synthesis that is essential for the function of penicillin-binding protein 1A (PBP1a). Stimulates transpeptidase activity of PBP1a in vitro. (678 aa)
mreBCell wall structural complex MreBCD, actin-like component MreB; Forms membrane-associated dynamic filaments that are essential for cell shape determination. Acts by regulating cell wall synthesis and cell elongation, and thus cell shape. A feedback loop between cell geometry and MreB localization maintains elongated cell shape by targeting cell wall growth to regions of negative cell wall curvature. Filaments rotate around the cell circumference in concert with the cell wall synthesis enzymes. The process is driven by the cell wall synthesis machinery and does not depend on MreB polyme [...] (347 aa)
mrcAPenicillin-binding protein 1a, murein transglycosylase and transpeptidase; Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross- linking of the peptide subunits); In the N-terminal section; belongs to the glycosyltransferase 51 family. (850 aa)
Your Current Organism:
Escherichia coli K12
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 substr. MG1655, Escherichia coli MG1655, Escherichia coli str. K-12 substr. MG1655, Escherichia coli str. K12 substr. MG1655, Escherichia coli str. MG1655, Escherichia coli strain MG1655
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