count	source_label	source_id	relationship	target_label	target_id	entity_type	solr_id	publication_id	sentences
4		MESH:D014640	inhibits	MURG_ACICJ	UNIPROT:A5FUL0	Phenotype	597f2a06-3532-11e8-bf76-001a4a160175	24944023	Vancomycin inhibits MraY, MurG, the TG and also the TP[21].
4		MESH:D006851	activates	MURG_ACICJ	UNIPROT:A5FUL0	Phenotype	eb64c2c2-bc22-11e5-9b9d-001a4ae51247	PMC4109649	MurG activity is stimulated by CL, and its overexpression results in formation at the cell poles of membrane vesicles enriched in CL and MurG[139].
2	MURG_ACICJ	UNIPROT:A5FUL0	activates		CHEBI:27692	Chemical	a7f9de4a-c8da-11e5-a1fd-001a4ae51246	25544046	In addition, UDP-GlcNAc donates GlcNAc for MurG (Rv2153c)-catalyzed synthesis of lipid II (decaprenyl-P-P-MurNAc-[pentapeptide]-GlcNAc), which is the substrate for peptidoglycan polymerizing enzymes (Barry et al., 2007).
2	MURG_ACICJ	UNIPROT:A5FUL0	activates		CHEBI:27692	Chemical	7ae7614c-1bf1-11f0-a2ca-0050569a1f61	10.1016/j.bbamem.2024.184282	Then, anN-acetyl-D-glucosamine (GlcNAc) moiety of UDP-GlcNAc is transferred to Lipid I by MurG to produce Lipid II [5].
2	MURG_ACICJ	UNIPROT:A5FUL0	activates		PF:PF00805	ProteinFamily	a7f9de4a-c8da-11e5-a1fd-001a4ae51246	25544046	In addition, UDP-GlcNAc donates GlcNAc for MurG (Rv2153c)-catalyzed synthesis of lipid II (decaprenyl-P-P-MurNAc-[pentapeptide]-GlcNAc), which is the substrate for peptidoglycan polymerizing enzymes (Barry et al., 2007).
2	MURG_ACICJ	UNIPROT:A5FUL0	activates		PF:PF11397	ProteinFamily	c125db94-8770-11f0-8cae-0050569a1f61	PMC7387395	The final steps of the peptidoglycan pathway, the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide) GlcNAc (lipid intermediate II) is catalyzed by MurG protein [13].
2	MURG_ACICJ	UNIPROT:A5FUL0	activates		CHEBI:27692	Chemical	f5e2df5e-bc22-11e5-8abe-001a4ae51246	10.1016/j.bbamem.2007.06.007	Furthermore, MurG which synthesizes the lipid II precursor, localizes at mid-cell in an FtsZ-dependent way.|||These complexes contain enzymes for precursor (lipid II) synthesis (such as MraY and MurG), the cell elongation-specific murein synthesis complex (with RodA, MreD, MreC, PBP2 and, presumably, PBP1A), and the murein hydrolase sub-complex (with lytic transglycosylases, amidases and/or endopeptidases).
2	MURG_ACICJ	UNIPROT:A5FUL0	activates		CHEBI:27692	Chemical	c774ff64-f57b-11eb-9010-001a4a160176	32424210	MraY and MurG produce lipid II at the inner membrane and co-localize with both the division and elongation complexes inE.|||MraY and MurG produce lipid I and lipid II, respectively.
2		CHEBI:29670	inhibits	MURG_ACICJ	UNIPROT:A5FUL0	Chemical	bb17b14e-bc39-11e5-ac4e-001a4ae51246	10.1016/j.tips.2007.12.004	Ramoplanin functions by inhibiting MurG and transglycosylases.
2		MESH:D014640	inhibits	MURG_ACICJ	UNIPROT:A5FUL0	Phenotype	0ca8efd6-705e-11e6-a316-001a4ae51247	PMC5039524	However, neither vancomycin nor moenomycin inhibits MurG in vivo, as neither can penetrate the bacterial membranes and, therefore, do not encounter MurG [94].|||It was reported that a vancomycin derivative withN-chlorobiphenyl-N-methyl leucine was a potent inhibitor of MurG in vitro [94].
2		MESH:D002308	activates	MURG_ACICJ	UNIPROT:A5FUL0	Phenotype	f088dc5a-38ff-11e8-a51f-001a4a160176	26278972	Addition of cardiolipin to the cardiolipin-null strain rescues the main localization of MurG-YFP to the spore (Fig. 4C, S6).|||This interpretation is also consistent with data showing that cardiolipin-based recruitment enhances enzymatic activity of MurG (van den Brink-van der Laan et al., 2003) and other enzymes.
2		MESH:D001455	inhibits	MURG_ACICJ	UNIPROT:A5FUL0	Phenotype	0ca8efd6-705e-11e6-a316-001a4ae51247	PMC5039524	Moenomycin, a known antibiotic that interferes with the function of the transglycosylase domain of PBP1B [105], was also found to inhibit MurG.|||However, neither vancomycin nor moenomycin inhibits MurG in vivo, as neither can penetrate the bacterial membranes and, therefore, do not encounter MurG [94].
1	MURG_ACICJ	UNIPROT:A5FUL0	activates		CHEBI:27692	Chemical	0ca8efd6-705e-11e6-a316-001a4ae51247	PMC5039524	MurG attaches the GlcNAc from UDP-GlcNAc to Lipid I and produces Lipid II [88].
1	MURG_ACICJ	UNIPROT:A5FUL0	deglycosylatesProtein		CHEBI:27692	Chemical	a30154b8-d1f5-11ee-b346-0050569a791b	10.1007/s10719-018-9842-7	[44]7D-cycloserineD-alanine-D-alanine ligase (Ddl)Inhibits cell growth by reducing supply of substrates for the final peptide ligation[45]8Muramycin: Nucleoside-peptide antibioticsPhospho-N-acetylmuramoyl-pentapeptide-transferase (MurX/MraY)Inhibits the synthesis of Lipid I[46,47–48]9Substituted prolinesUDP-N-acetylglucosamine-N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol-N-acetylglucosamine transferase (MurG)Inhibits the synthesis of Lipid II[49]10Depsipeptide antibioticsLipid IIPrevents the transglycosylation of the translocated Lipid II by binding to it.
1	MURG_ACICJ	UNIPROT:A5FUL0	activates		CHEBI:27692	Chemical	10aff2b0-bbdb-11e5-8abe-001a4ae51246	PMC4440368	The final step of the peptidoglycan subunit biosynthesis is the addition of N-acetylglucosamine (GlcNAc) to lipid I catalyzed by MurG producing lipid II (Muchova et al.,2011).
1	MURG_ACICJ	UNIPROT:A5FUL0	activates		CHEBI:27692	Chemical	959c0f60-1b65-11e6-8d81-001a4ae51247	PMC4866016	MurG catalyzes glycosyl transfer from UDP-GlcNAc to MurNAc present in lipid I to produce lipid II [44].
1	MURG_ACICJ	UNIPROT:A5FUL0	activates		CHEBI:59640	Chemical	10aff2b0-bbdb-11e5-8abe-001a4ae51246	PMC4440368	The final step of the peptidoglycan subunit biosynthesis is the addition of N-acetylglucosamine (GlcNAc) to lipid I catalyzed by MurG producing lipid II (Muchova et al.,2011).
1	MURG_ACICJ	UNIPROT:A5FUL0	glycosylatesProtein		CHEBI:16264	Chemical	6d49859a-c8e7-11e5-9ad8-001a4ae51247	18077448	The phospho-N-acetylmuramyl pentapeptide is transferred from this species by MraY to a membrane-bound undecaprenyl-phosphate carrier to form lipid I (undecaprenyl-pyrophosphoryl-N-acetylmuramyl-l-alanyl-γ-d-glutamyl-l-lysyl-d-alanyl-d-alanine), which is then glycosylated with UDP-N-acetylglucosamine by MurG to form lipid II (undecaprenyl-pyrophosphoryl-N-acetylmuramyl (N-acetylglucosaminyl)-l-alanyl-γ-d-glutamyl-l-lysyl-d-alanyl-d-alanine) (1) (Fig. 1).
1	MURG_ACICJ	UNIPROT:A5FUL0	activates		GO:0009252	Phenotype	0a217ddc-bc36-11e5-8abe-001a4ae51246	PMC4331358	These observations were consistent with those of a previous study [21], which revealed that the enhanced expression of MurA, MurG, and Ddl in a mutant at pH 3.5 contributed to peptidoglycan synthesis, maintaining cellular structural integrity inLactobacillus caseiZhang.
1	MURG_ACICJ	UNIPROT:A5FUL0	activates		GO:0009058	Phenotype	52da1db6-c471-11e5-91a7-001a4ae51247	PMC2663061	In testing the individual reactions, we found the MraY reaction to be inhibited (Fig.6C and D), whereas the downstream biosynthesis steps catalyzed by MurG, FemX, and PBP2 remained unaffected by friulimicin (Fig.7).
1	MURG_ACICJ	UNIPROT:A5FUL0	activates		MESH:D010457	Phenotype	c14496a8-f580-11eb-91b4-001a4a160176	33078277	A C55-polyisoprenoid carrier binds UDP-MurNAc-pentapeptide, which is converted to lipid-linked MurNAc-pentapeptide (lipid I) by MraY; subsequently, GlcNAc is added to lipid I by MurG, producing the peptidoglycan precursor GlcNAc-MurNAc(-pentapeptide)-pyrophosphoryl undecaprenol (lipid II).
1	MURG_ACICJ	UNIPROT:A5FUL0	inhibits		GO:0016049	Phenotype	7bd8d856-bc2e-11e5-ac4e-001a4ae51246	PMC3433793	Depletion of MurG by cell culture in the absence of IPTG leads to arrest of cell growth, cell bulging, and ultimately cell lysis (Fig. 3).
1	MURG_ACICJ	UNIPROT:A5FUL0	activates		PF:PF00805	ProteinFamily	d5ff427c-3797-11e6-9aa8-001a4ae51247	PMC4803751	The next steps in PG formation are the synthesis of the lipid precursor intermediates, undecaprenyl-diphospho-MurNAc-pentapeptide (lipid I) and undecaprenyl-diphospho-MurNAc-(pentapeptide)-GlcNAc (lipid II), by the enzymes MraY and MurG, respectively; these reactions occur at the level of the cytoplasmic membrane (Bouhss et al.,2008).
1	MURG_ACICJ	UNIPROT:A5FUL0	activates		PF:PF11397	ProteinFamily	10aff2b0-bbdb-11e5-8abe-001a4ae51246	PMC4440368	The final step of the peptidoglycan subunit biosynthesis is the addition of N-acetylglucosamine (GlcNAc) to lipid I catalyzed by MurG producing lipid II (Muchova et al.,2011).
1	MURG_ACICJ	UNIPROT:A5FUL0	activates		PF:PF11397	ProteinFamily	ce77be7c-bc49-11e5-ac4e-001a4ae51246	10.1016/j.tetlet.2006.05.129	Our synthetic strategy includes (1) a practical synthesis of the pentapeptide (building block 1) in solution phase (step i), (2) transfer the pentapeptide to the polymer-support (step ii), (3) conjugation of appropriately protected MurNAc (building block 2) to the polymer-supported pentapeptide (step iii), (4) introduction of lipid analogues (building block 3) (step iv), and (5) simultaneous deprotection to form lipid I analogues followed by MurG catalyzed GlcNAc addition to lipid I analogues leading to lipid II analogues3a(step v) as illustrated inScheme 1.
1		MESH:D014640	inhibits	MURG_ACICJ	UNIPROT:A5FUL0	Phenotype	e599a51e-c8df-11e5-9624-001a4ae51246	PMC1426922	"Vancomycin inhibits MraY, MurG, and the transglycosylase
                      and transpeptidase (13) by binding to the terminald-Ala-d-Ala residues of peptidoglycan, lipid I, lipid II, and the sugar precursor UDP-MurNAc(pp)."
1		MESH:D014640	inhibits	MURG_ACICJ	UNIPROT:A5FUL0	Phenotype	4dda21b6-ca03-11e5-ab20-001a4ae51246	PMC1068599	We have shown inhibition of MurG by vancomycin.
1		MESH:D002308	activates	MURG_ACICJ	UNIPROT:A5FUL0	Phenotype	0ca8efd6-705e-11e6-a316-001a4ae51247	PMC5039524	Later, it was reported that lipid vesicles enriched in the negatively-charged cardiolipin co-purified with EcMurG and the presence of cardiolipin also enhanced MurG activity [93].
1		MESH:D013395	activates	MURG_ACICJ	UNIPROT:A5FUL0	Phenotype	fcde63de-0c52-11f0-a2ca-0050569a1f61	10.1016/S0960-894X(00)00583-7	MurG (UDP-N-acetylglucosamine: undecaprenyl-pyrophosphoryl-N-acetylmuramoyl-pentapeptideN-acetyl glucosaminyl transferase) [GenBank P17443] is a cytoplasmatic membrane-associated GlcNAc transferase, responsible for the conversion of Lipid I (1) to Lipid II (2), the substrate for transglycosylases and transpeptidases.5Although the MurG enzyme was first described in 1965, studies of its mechanism have lagged because Lipid I, the sugar acceptor of MurG, could not be isolated in large amounts from natural sources.
1		CHEBI:15841	inhibits	MURG_ACICJ	UNIPROT:A5FUL0	Chemical	9eec1168-ea75-11ee-b346-0050569a791b	PMC9293667	Enramycin, a polypeptide antibiotic, inhibits MurG, which is involved in peptidoglycan synthesis in Gram-positive bacteria (Fang et al., 2006).
1		MESH:D014415	inhibits	MURG_ACICJ	UNIPROT:A5FUL0	Phenotype	4dda21b6-ca03-11e5-ab20-001a4ae51246	PMC1068599	"Thus, the inhibition of MurG by tunicamycin is an artifact of the effect of tunicamycin on the blank reaction and does not
                         reflect its effect on MurG."
1		MESH:D006096	decreases	MURG_ACICJ	UNIPROT:A5FUL0	Phenotype	16959862-c46c-11e5-a92e-001a4ae51246	PMC3986158	"When the localization of MurG was investigated by Western blot analysis
                                  (Fig. 5B), both MP196 and gramicidin S treatment caused almost complete loss of MurG from the membrane fraction of treatedB.subtiliswithin 5 min."
1		UNIPROT:A5FYN4	activates	MURG_ACICJ	UNIPROT:A5FUL0	Protein	1828f85c-5c43-11e7-86a3-001a4ae51246	PMC5146858	The biosynthesis of PG includes cytoplasmic steps mediated by MurA to F, and thereafter the transfer through the membrane via the transferases MarY and MurG, and finally the binding of new material to cell wall.
1		UNIPROT:Q01465	inhibits	MURG_ACICJ	UNIPROT:A5FUL0	Protein	12ed4f0a-f00b-11e5-9b35-001a4ae51246	20233306	MurG localization is dependent on intact helical cables of MreB as treatment with A22, an inhibitor of MreB polymerization, disrupts the positioning of MurG (Divakaruniet al., 2007).
1		CHEBI:38624	inhibits	MURG_ACICJ	UNIPROT:A5FUL0	Chemical	7bd8d856-bc2e-11e5-ac4e-001a4ae51246	PMC3433793	To deplete MurG, the relevant culture was grown in DSM with 1 mM IPTG for 2 h and diluted into a medium lacking IPTG to an OD600 nmof 0.05 and incubated for an additional 2 h. For membrane visualization, the fluorescent dye FM 4-64 (Molecular Probes) at concentrations of 0.2–1 μg mL−1and nonyl acridine orange (NAO; Molecular Probes) at concentrations of 0.05–0.1 μg mL−1were used.
1		UNIPROT:P75151	decreases	MURG_ACICJ	UNIPROT:A5FUL0	Protein	16959862-c46c-11e5-a92e-001a4ae51246	PMC3986158	"When the localization of MurG was investigated by Western blot analysis
                                  (Fig. 5B), both MP196 and gramicidin S treatment caused almost complete loss of MurG from the membrane fraction of treatedB.subtiliswithin 5 min."
1		CHEBI:26020	inhibits	MURG_ACICJ	UNIPROT:A5FUL0	Chemical	fcde63de-0c52-11f0-a2ca-0050569a1f61	10.1016/S0960-894X(00)00583-7	Walker et al. evaluated the ability of phosphorylated Lipid I analogues incorporating changes in the lipid and peptide portions to act as alternative substrates or dead-end inhibitors for MurG.7In these studies the anomeric phosphate (4) inhibited MurG with an IC50of (50±25μg mL−1), but had no acceptor ability, suggesting that the anomeric group in Lipid I played a key role in acceptor recognition.
1		MESH:D000432	inhibits	MURG_ACICJ	UNIPROT:A5FUL0	Phenotype	6a67a0ce-bbe9-11e5-8abe-001a4ae51246	10.1016/S0378-1097(02)01203-X	However, methanol (15–40%, with or without Triton X-100) almost totally inhibited MurG when replacing DMSO.
1		CHEBI:61695	activates	MURG_ACICJ	UNIPROT:A5FUL0	Chemical	98ba8b86-bc01-11e5-9b9d-001a4ae51247	10.1016/j.tim.2011.11.004	The role of MreB coordinating PG synthesis in the cytosol and at the inner membrane Evidence suggests that PG precursor synthesizing proteins (MurA–MurG and MraY) might also form direct or indirect cytosolic complexes with MreB as many of these proteins quickly lose their MreB-like distribution pattern when cells are treated with A22, a small molecule inhibitor of MreB[25].
1		UNIPROT:Q13315	inhibits	MURG_ACICJ	UNIPROT:A5FUL0	Protein	826d149a-c46f-11e5-8491-001a4ae51247	PMC4128124	"Inducible depletion of MurG, GlfT2, and Pks13 via the addition of anhydrotetracycline (ATc) inhibited growth and induced
                                  morphological changes, consistent with the inhibition of cell wall synthesis (Fig. S1D)."
1		MESH:D001430	inhibits	MURG_ACICJ	UNIPROT:A5FUL0	Phenotype	ed7cdb16-c6ba-11ee-b346-0050569a791b	10.1016/j.ijfoodmicro.2023.110370	Additionally, one report found that the bacteriocin BM1157 inhibited murA, murD, murE, murG, and femB during peptidoglycan biosynthesis (Luo et al., 2021).
1		MESH:D001430	inhibits	MURG_ACICJ	UNIPROT:A5FUL0	Phenotype	f3a5ba4e-c94e-11ee-ae05-0050569a1f61	10.1016/j.foodcont.2022.109374	Bacteriocin BM1157 inhibited MurA, MurD, MurE, MurG, and FemB in the peptidoglycan biosynthesis pathway (Luo, Yi, Chen, Liu, & Lü, 2021).
1		MESH:D006851	activates	MURG_ACICJ	UNIPROT:A5FUL0	Phenotype	22ab6cce-ca5e-11e5-8050-001a4ae51246	PMC161595	"Activity
                   measurements with lipid I-containing vesicles showed that MurG activity is enhanced by the presence of CL."
1		CHEBI:29670	inhibits	MURG_ACICJ	UNIPROT:A5FUL0	Chemical	241a9914-cb2a-11e5-b419-001a4ae51246	PMC124240	"Inhibition of MurG activity might be explained simply if the ramoplanin–Lipid II complex was an inhibitor of MurG, because
                                  the enzyme is peripherally associated with the inner face of the cytoplasmic membrane (23)."
1		MESH:D007544	inhibits	MURG_ACICJ	UNIPROT:A5FUL0	Phenotype	7bd8d856-bc2e-11e5-ac4e-001a4ae51246	PMC3433793	To deplete MurG, the relevant culture was grown in DSM with 1 mM IPTG for 2 h and diluted into a medium lacking IPTG to an OD600 nmof 0.05 and incubated for an additional 2 h. For membrane visualization, the fluorescent dye FM 4-64 (Molecular Probes) at concentrations of 0.2–1 μg mL−1and nonyl acridine orange (NAO; Molecular Probes) at concentrations of 0.05–0.1 μg mL−1were used.
1		CHEBI:15776	inhibits	MURG_ACICJ	UNIPROT:A5FUL0	Chemical	4dda21b6-ca03-11e5-ab20-001a4ae51246	PMC1068599	"The β-lactams are accepted as inhibitors of transpeptidase that act by covalently binding to the penicillin binding proteins,
                         so it was surprising that cephalosporin C inhibited MurG."