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dacA dacA amiE amiE ddl ddl murF murF pbpF pbpF pbpH pbpH pbpB pbpB spoVD spoVD murE murE mraY mraY murD murD murG murG murB murB uppS uppS dacC dacC yodJ yodJ ponA ponA dacB dacB dacF dacF pbpA pbpA dgkA dgkA murC murC uppP uppP pbpD pbpD bcrC bcrC murAA murAA murAB murAB pbpG pbpG
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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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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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dacAD-alanyl-D-alanine carboxypeptidase (penicillin-binding protein 5); Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors; Belongs to the peptidase S11 family. (443 aa)
amiEAmidase hydrolyzing N-acetylmuramyl-L-Ala bond of MurNAc peptides; Involved in muropeptide recycling. Hydrolyzes the amide bond between N-acetylmuramic acid (MurNAc) and the L-alanine residue of the stem peptide. Cannot hydrolyze muropeptides containing N- acetylglucosamine (GlcNAc) at the non-reducing end. (441 aa)
ddlD-alanyl-D-alanine ligase A; Cell wall formation. (354 aa)
murFUDP-N-acetylmuramoylalanyl-D-glutamyl-2, 6-diaminopimelate-D-alanyl-D-alanine ligase; Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein; Belongs to the MurCDEF family. MurF subfamily. (457 aa)
pbpFPenicillin-binding protein 2C required for spore germination; Cell wall formation. May be involved in outgrowth of the germinated spore or it could function in the synthesis of the germ cell wall; In the N-terminal section; belongs to the glycosyltransferase 51 family. (714 aa)
pbpHPenicillin-binding enzyme for formation of rod-shaped peptidoglycan cell wall; Involved in the polymerization of peptidoglycan. Plays a redundant role with PBP2a in determining the rod shape of the cell during vegetative growth and spore outgrowth. Belongs to the transpeptidase family. (704 aa)
pbpBPenicillin-binding protein 2B; Penicillin-binding proteins (PBPs) function in the late steps of murein biosynthesis. PBP-2B is required for vegetative cell division and sporulation septation. Beta-lactamase inactivates the PBPs by acylating an essential serine residue in the active site of these proteins, thereby interrupting normal cell wall synthesis; Belongs to the transpeptidase family. (716 aa)
spoVDPenicillin-binding protein; Penicillin-binding protein with an unknown catalytic activity. May have a specialized role in the morphogenesis of spore cortex, which is a modified form of peptidoglycan. Pore cortex formation is determined primarily by the mother cell. (646 aa)
murEUDP-N-acetylmuramoylalanyl-D-glutamate-2, 6-diaminopimelate ligase; Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. Belongs to the MurCDEF family. MurE subfamily. (494 aa)
mraYphospho-N-acetylmuramoyl-pentapeptide transferase; First step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan; Belongs to the glycosyltransferase 4 family. MraY subfamily. (324 aa)
murDUDP-N-acetylmuramoylalanyl-D-glutamate ligase; Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). Belongs to the MurCDEF family. (451 aa)
murGUndecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase; Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc- (pentapeptide)GlcNAc (lipid intermediate II); Belongs to the glycosyltransferase 28 family. MurG subfamily. (363 aa)
murBUDP-N-acetylenolpyruvoylglucosamine reductase; Cell wall formation. (303 aa)
uppSUndecaprenyl pyrophosphate synthase; Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids. (260 aa)
dacCD-alanyl-D-alanine carboxypeptidase; Catalyzes DD-carboxypeptidase and transpeptidation reactions. (491 aa)
yodJD-alanyl-D-alanine carboxypeptidase lipoprotein; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. (273 aa)
ponAPeptidoglycan glycosyltransferase (penicillin-binding proteins 1A and 1B); 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). (914 aa)
dacBD-alanyl-D-alanine carboxypeptidase (penicillin-binding protein 5*); Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors. Required specifically for the synthesis of the spore form of peptidoglycan (cortex). (382 aa)
dacFD-alanyl-D-alanine carboxypeptidase (penicilin binding protein); Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors. (389 aa)
pbpATranspeptidase (penicillin-binding protein 2A); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (716 aa)
dgkAUndecaprenol kinase; Catalyzes the phosphorylation of undecaprenol in vitro, which is probably the physiological substrate. Exhibits no detectable activity against other substrates such as monoacylglycerol, ceramide, or diacylglycerol (DAG). Appears indispensable for the maintenance of spore stability and viability in B.subtilis. (123 aa)
murCUDP-N-acetyl muramate-alanine ligase; Cell wall formation; Belongs to the MurCDEF family. (432 aa)
uppPUndecaprenyl-diphosphatase; Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin; Belongs to the UppP family. (276 aa)
pbpDPenicillin-binding protein 4; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; In the C-terminal section; belongs to the transpeptidase family. (624 aa)
bcrCUndecaprenyl pyrophosphate phosphatase; Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin; Belongs to the BcrC/YbjG family. (193 aa)
murAAUDP-N-acetylglucosamine 1-carboxyvinyltransferase; Cell wall formation. Adds enolpyruvyl to UDP-N- acetylglucosamine. Essential for cell growth; Belongs to the EPSP synthase family. MurA subfamily. (436 aa)
murABUDP-N-acetylglucosamine 1-carboxyvinyltransferase; Cell wall formation. Adds enolpyruvyl to UDP-N- acetylglucosamine; Belongs to the EPSP synthase family. MurA subfamily. (429 aa)
pbpGSporulation specific penicillin-binding protein; Involved in the polymerization and cross-linking of spore peptidoglycan. May be required for synthesis of the spore germ cell wall, the first layer of peptidoglycan synthesized on the surface of the inner forespore membrane; In the C-terminal section; belongs to the transpeptidase family. (691 aa)
Your Current Organism:
Bacillus subtilis 168
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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