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mreD mreD ftsW ftsW ftsI ftsI slt slt mrcA mrcA mreB mreB rpoA rpoA mreC mreC mtgA mtgA dacB dacB glnE glnE pbpC pbpC rodZ rodZ mrdA mrdA mrdB mrdB mrcB mrcB ftsZ ftsZ
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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
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
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Your Input:
mreDCell wall structural complex MreBCD transmembrane component MreD; Involved in formation of the rod shape of the cell. May also contribute to regulation of formation of penicillin-binding proteins; Belongs to the MreD family. (162 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)
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)
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)
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)
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)
rpoARNA polymerase, alpha subunit; DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. This subunit plays an important role in subunit assembly since its dimerization is the first step in the sequential assembly of subunits to form the holoenzyme. (329 aa)
mreCCell wall structural complex MreBCD transmembrane component MreC; Involved in formation and maintenance of cell shape. Responsible for formation of rod shape. May also contribute to regulation of formation of penicillin-binding proteins. Belongs to the MreC family. (367 aa)
mtgABiosynthetic peptidoglycan transglycosylase; Peptidoglycan polymerase that catalyzes glycan chain elongation from lipid-linked precursors. May play a role in peptidoglycan assembly during cell division in collaboration with other cell division proteins ; Belongs to the glycosyltransferase 51 family. (242 aa)
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)
glnEFused deadenylyltransferase/adenylyltransferase for glutamine synthetase; Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase inactivates GlnA by covalent transfer of an adenylyl group from ATP to 'Tyr-398' of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N- terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signa [...] (946 aa)
pbpCPenicillin-insensitive murein repair transglycosylase; Cell wall formation. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a transpeptidase C-terminal domain which may not be functional. (770 aa)
rodZMreB assembly cytoskeletal protein; Cytoskeletal protein that is involved in cell-shape control through regulation of the length of the long axis. Belongs to the RodZ family. (337 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)
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)
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)
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)
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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