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dacB dacB mrcA mrcA gmk gmk slt slt mpl mpl ampC ampC ftsI ftsI murF murF ampE ampE ampD ampD mrcB mrcB mltD mltD dacA dacA rlpA rlpA mrdA mrdA dacC dacC yceG yceG nagZ nagZ pbpG pbpG mltF mltF mltB mltB mltA mltA
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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
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
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Your Input:
dacBD-alanyl-D-alanine carboxypeptidase; Not involved in transpeptidation but exclusively catalyzes a DD-carboxypeptidase and DD-endopeptidase reaction. Belongs to the peptidase S13 family. (477 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)
gmkGuanylate kinase; Essential for recycling GMP and indirectly, cGMP. Belongs to the guanylate kinase family. (207 aa)
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)
mplUDP-N-acetylmuramate:L-alanyl-gamma-D-glutamyl- meso-diaminopimelate ligase; Reutilizes the intact tripeptide L-alanyl-gamma-D-glutamyl- meso-diaminopimelate by linking it to UDP-N-acetylmuramate. The enzyme can also use the tetrapeptide L-alanyl-gamma-D-glutamyl-meso-2,6- diaminoheptanedioyl-D-alanine or the pentapeptide L-alanyl-gamma-D- glutamyl-meso-2,6-diaminoheptandioyl-D-alanyl-D-alanine in vivo and in vitro; Belongs to the MurCDEF family. Mpl subfamily. (457 aa)
ampCPenicillin-binding protein; This protein is a serine beta-lactamase with a substrate specificity for cephalosporins; Belongs to the class-C beta-lactamase family. (377 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)
murFUDP-N-acetylmuramoyl-tripeptide: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. (452 aa)
ampEAmpicillin resistance inner membrane protein; Putative signaling protein in beta-lactamase regulation. AmpE seems not to act as a direct sensor for beta-lactams. (284 aa)
ampD1,6-anhydro-N-acetylmuramyl-L-alanine amidase, Zn-dependent; Involved in cell wall peptidoglycan recycling. Specifically cleaves the amide bond between the lactyl group of N-acetylmuramic acid and the alpha-amino group of the L-alanine in degradation products containing an anhydro N-acetylmuramyl moiety. Is also involved in beta-lactamase induction ; Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family. (183 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)
mltDPutative membrane-bound lytic murein transglycosylase D; Murein-degrading enzyme. May play a role in recycling of muropeptides during cell elongation and/or cell division (By similarity); Belongs to the transglycosylase Slt family. (452 aa)
dacAD-alanyl-D-alanine carboxypeptidase (penicillin-binding protein 5); Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors. (403 aa)
rlpASeptal ring protein, suppressor of prc, minor lipoprotein; Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides; Belongs to the RlpA family. (362 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)
dacCD-alanyl-D-alanine carboxypeptidase; Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors. (400 aa)
yceGSeptation protein, ampicillin sensitivity; Functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation. Belongs to the transglycosylase MltG family. (340 aa)
nagZBeta N-acetyl-glucosaminidase; Plays a role in peptidoglycan recycling by cleaving the terminal beta-1,4-linked N-acetylglucosamine (GlcNAc) from peptide- linked peptidoglycan fragments, giving rise to free GlcNAc, anhydro-N- acetylmuramic acid and anhydro-N-acetylmuramic acid-linked peptides. Cleaves GlcNAc linked beta-1,4 to MurNAc tripeptides. (341 aa)
pbpGD-alanyl-D-alanine endopeptidase; Cell wall formation. May play a specialized role in remodeling the cell wall. Specifically hydrolyzes the DD- diaminopimelate-alanine bonds in high-molecular-mass murein sacculi; Belongs to the peptidase S11 family. (310 aa)
mltFMembrane-bound lytic transglycosylase F, murein hydrolase; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. (518 aa)
mltBMembrane-bound lytic murein transglycosylase B; 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. (361 aa)
mltAMembrane-bound lytic murein transglycosylase A; Murein-degrading enzyme. May play a role in recycling of muropeptides during cell elongation and/or cell division. Degrades murein glycan strands and insoluble, high-molecular weight murein sacculi. (365 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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