ECOLI:MURJ

Species (Taxon ID)	Escherichia coli (strain K12). (83333)
Gene Name(s)	murJ (synonyms: mviN, yceN)
Protein Name(s)	Lipid II flippase MurJ Peptidoglycan biosynthesis protein MurJ
External Links
UniProt	P0AF16
EMBL	U00096 AP009048
PIR	B64850
RefSeq	NP_415587.1 YP_489337.1
ProteinModelPortal	P0AF16
IntAct	P0AF16
STRING	511145.b1069
TCDB	2.A.66.4.3
EnsemblBacteria	AAC74153 BAA35877
GeneID	12931085 945487
KEGG	ecj:Y75_p1039 eco:b1069
PATRIC	32117377
EchoBASE	EB3639
EcoGene	EG13880
eggNOG	COG0728
HOGENOM	HOG000263812
InParanoid	P0AF16
KO	K03980
OMA	LMMANIL
OrthoDB	EOG6C0131
PhylomeDB	P0AF16
BioCyc	EcoCyc:G6561-MONOMER ECOL316407:JW1056-MONOMER MetaCyc:G6561-MONOMER
PRO	PR:P0AF16
Proteomes	UP000000318 UP000000625
Genevestigator	P0AF16
GO	GO:0005887 GO:0005319 GO:0015648 GO:0071555 GO:0034204 GO:0015836 GO:0009252 GO:0008360
InterPro	IPR004268
Pfam	PF03023
PIRSF	PIRSF002869
PRINTS	PR01806
TIGRFAMs	TIGR01695

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
	GO:0034203	glycolipid translocation	PMID:25013077^[1]	ECO:0000315			P	Fig3 shows that MurJ activity is required for ColM dependent cleavage of lipidII in spheroplasts. When mutant MurJ(A29C) was inactivated with MTSES, flippase activity was reduced to a barely detectable level.	complete CACAO 10204
	GO:0031224	intrinsic component of membrane	PMID:28894177^[2]	ECO:0006005	fractionation evidence used in manual assertion		C	Supplementary Figure 3 shows MurJ (Lipid II flippase MurJ) is found in membrane fractions of Escherichia coli. UniProtKB - P0AF16 (MURJ_ECOLI) Organism: Escherichia coli (strain K12)	complete CACAO 13811
	GO:0015648	lipid-linked peptidoglycan transporter activity	PMID:28894177^[2]	ECO:0005801	enzymatic activity assay evidence used in manual assertion		F	Notes: Figure 4 - represent MurJ - membrane compartment using lipid flippase activity with ColM Uniport - Lipid II flippase MurJ , organism - Escherichia Coli	complete
involved_in	GO:0034203	glycolipid translocation	PMID:25013077^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0034204	lipid translocation	PMID:21873635^[3]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG13880 PANTHER:PTN001341949	P	Seeded From UniProt	complete
involved_in	GO:0015836	lipid-linked peptidoglycan transport	PMID:21873635^[3]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG13880 PANTHER:PTN001341949	P	Seeded From UniProt	complete
enables	GO:0015648	lipid-linked peptidoglycan transporter activity	PMID:21873635^[3]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG13880 PANTHER:PTN001341949	F	Seeded From UniProt	complete
involved_in	GO:0009252	peptidoglycan biosynthetic process	PMID:21873635^[3]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG13880 PANTHER:PTN001341949	P	Seeded From UniProt	complete
part_of	GO:0005887	integral component of plasma membrane	PMID:21873635^[3]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG13880 PANTHER:PTN001341949 UniProtKB:P9WJK3	C	Seeded From UniProt	complete
involved_in	GO:0034204	lipid translocation	PMID:18832143^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0034204	lipid translocation	PMID:25013077^[1]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0015836	lipid-linked peptidoglycan transport	PMID:18832143^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0015836	lipid-linked peptidoglycan transport	PMID:25013077^[1]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0015648	lipid-linked peptidoglycan transporter activity	PMID:18832143^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0015648	lipid-linked peptidoglycan transporter activity	PMID:25013077^[1]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0009252	peptidoglycan biosynthetic process	PMID:18708495^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005887	integral component of plasma membrane	PMID:23935042^[6]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005887	integral component of plasma membrane	PMID:18708495^[5]	ECO:0000245	automatically integrated combinatorial evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:15919996^[7]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005887	integral component of plasma membrane	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000432258	C	Seeded From UniProt	complete
enables	GO:0015648	lipid-linked peptidoglycan transporter activity	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000432258	F	Seeded From UniProt	complete
involved_in	GO:0015836	lipid-linked peptidoglycan transport	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000432258	P	Seeded From UniProt	complete
involved_in	GO:0009252	peptidoglycan biosynthetic process	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000432258	P	Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C	Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000037 GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0997 UniProtKB-KW:KW-1003 UniProtKB-SubCell:SL-0037	C	Seeded From UniProt	complete
involved_in	GO:0071555	cell wall organization	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0961	P	Seeded From UniProt	complete
part_of	GO:0016021	integral component of membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0812	C	Seeded From UniProt	complete
involved_in	GO:0008360	regulation of cell shape	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0133	P	Seeded From UniProt	complete
involved_in	GO:0009252	peptidoglycan biosynthetic process	GO_REF:0000037 GO_REF:0000041	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0573 UniPathway:UPA00219	P	Seeded From UniProt	complete
edit table

Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 ^1.3 ^1.4 Sham, LT et al. (2014) Bacterial cell wall. MurJ is the flippase of lipid-linked precursors for peptidoglycan biogenesis. Science 345 220-2 PubMed GONUTS page
↑ ^2.0 ^2.1 Chamakura, KR et al. (2017) A viral protein antibiotic inhibits lipid II flippase activity. Nat Microbiol 2 1480-1484 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 ^3.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 Ruiz, N (2008) Bioinformatics identification of MurJ (MviN) as the peptidoglycan lipid II flippase in Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 105 15553-7 PubMed GONUTS page
↑ ^5.0 ^5.1 Inoue, A et al. (2008) Involvement of an essential gene, mviN, in murein synthesis in Escherichia coli. J. Bacteriol. 190 7298-301 PubMed GONUTS page
↑ Butler, EK et al. (2013) Structure-function analysis of MurJ reveals a solvent-exposed cavity containing residues essential for peptidoglycan biogenesis in Escherichia coli. J. Bacteriol. 195 4639-49 PubMed GONUTS page
↑ Daley, DO et al. (2005) Global topology analysis of the Escherichia coli inner membrane proteome. Science 308 1321-3 PubMed GONUTS page

[PMID:25013077-1] 1.0 ^1.1 ^1.2 ^1.3 ^1.4 Sham, LT et al. (2014) Bacterial cell wall. MurJ is the flippase of lipid-linked precursors for peptidoglycan biogenesis. Science 345 220-2 PubMed GONUTS page

[PMID:28894177-2] 2.0 ^2.1 Chamakura, KR et al. (2017) A viral protein antibiotic inhibits lipid II flippase activity. Nat Microbiol 2 1480-1484 PubMed GONUTS page

[PMID:21873635-3] 3.0 ^3.1 ^3.2 ^3.3 ^3.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:18832143-4] 4.0 ^4.1 ^4.2 Ruiz, N (2008) Bioinformatics identification of MurJ (MviN) as the peptidoglycan lipid II flippase in Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 105 15553-7 PubMed GONUTS page

[PMID:18708495-5] 5.0 ^5.1 Inoue, A et al. (2008) Involvement of an essential gene, mviN, in murein synthesis in Escherichia coli. J. Bacteriol. 190 7298-301 PubMed GONUTS page

[PMID:23935042-6] Butler, EK et al. (2013) Structure-function analysis of MurJ reveals a solvent-exposed cavity containing residues essential for peptidoglycan biogenesis in Escherichia coli. J. Bacteriol. 195 4639-49 PubMed GONUTS page

[PMID:15919996-7] Daley, DO et al. (2005) Global topology analysis of the Escherichia coli inner membrane proteome. Science 308 1321-3 PubMed GONUTS page

[1]

[2]

[3]

[4]

[5]

[6]

[7]

ECOLI:MURJ

Contents

Annotations

Notes

References

b

c

e

g

i

l

m

o

p

r

Navigation menu

Personal tools

Namespaces

Variants

Views

More

Search

Navigation

Cacao

Links

Tools