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Protein

Lipid II flippase MurJ

Gene

murJ

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in peptidoglycan biosynthesis. Transports lipid-linked peptidoglycan precursors from the inner to the outer leaflet of the cytoplasmic membrane.3 Publications

GO - Molecular functioni

  • lipid-linked peptidoglycan transporter activity Source: EcoCyc

GO - Biological processi

  • cell wall organization Source: UniProtKB-KW
  • glycolipid translocation Source: CACAO
  • lipid-linked peptidoglycan transport Source: EcoCyc
  • lipid translocation Source: EcoCyc
  • peptidoglycan biosynthetic process Source: EcoCyc
  • regulation of cell shape Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis, Transport

Enzyme and pathway databases

BioCyciEcoCyc:G6561-MONOMER.
ECOL316407:JW1056-MONOMER.
MetaCyc:G6561-MONOMER.

Protein family/group databases

TCDBi2.A.66.4.3. the multidrug/oligosaccharidyl-lipid/polysaccharide (mop) flippase superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipid II flippase MurJ
Alternative name(s):
Peptidoglycan biosynthesis protein MurJ
Gene namesi
Name:murJ
Synonyms:mviN, yceN
Ordered Locus Names:b1069, JW1056
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13880. murJ.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 55CytoplasmicSequence analysis
Transmembranei6 – 3227HelicalSequence analysisAdd
BLAST
Topological domaini33 – 408PeriplasmicSequence analysis
Transmembranei41 – 6929HelicalSequence analysisAdd
BLAST
Topological domaini70 – 8213CytoplasmicSequence analysisAdd
BLAST
Transmembranei83 – 10927HelicalSequence analysisAdd
BLAST
Topological domaini110 – 12314PeriplasmicSequence analysisAdd
BLAST
Transmembranei124 – 15431HelicalSequence analysisAdd
BLAST
Topological domaini155 – 1562CytoplasmicSequence analysis
Transmembranei157 – 17822HelicalSequence analysisAdd
BLAST
Topological domaini179 – 1857PeriplasmicSequence analysis
Transmembranei186 – 20722HelicalSequence analysisAdd
BLAST
Topological domaini208 – 22316CytoplasmicSequence analysisAdd
BLAST
Transmembranei224 – 25330HelicalSequence analysisAdd
BLAST
Topological domaini254 – 26310PeriplasmicSequence analysis
Transmembranei264 – 29229HelicalSequence analysisAdd
BLAST
Topological domaini293 – 30210CytoplasmicSequence analysis
Transmembranei303 – 33735HelicalSequence analysisAdd
BLAST
Topological domaini338 – 3469PeriplasmicSequence analysis
Transmembranei347 – 37428HelicalSequence analysisAdd
BLAST
Topological domaini375 – 3795CytoplasmicSequence analysis
Transmembranei380 – 40223HelicalSequence analysisAdd
BLAST
Topological domaini403 – 4097PeriplasmicSequence analysis
Transmembranei410 – 42920HelicalSequence analysisAdd
BLAST
Topological domaini430 – 44314CytoplasmicSequence analysisAdd
BLAST
Transmembranei444 – 46320HelicalSequence analysisAdd
BLAST
Topological domaini464 – 47714PeriplasmicSequence analysisAdd
BLAST
Transmembranei478 – 49922HelicalSequence analysisAdd
BLAST
Topological domaini500 – 51112CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of plasma membrane Source: EcoCyc
  • plasma membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi18 – 181R → A or C: Lack of activity. 1 Publication
Mutagenesisi24 – 241R → A or C: Lack of activity. 1 Publication
Mutagenesisi39 – 391D → A or C: Lack of activity. 1 Publication
Mutagenesisi52 – 521R → A: Decrease in activity. 1 Publication
Mutagenesisi52 – 521R → C: Lack of activity. 1 Publication
Mutagenesisi270 – 2701R → A or C: Lack of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 511511Lipid II flippase MurJPRO_0000182006Add
BLAST

Proteomic databases

PaxDbiP0AF16.

Interactioni

Protein-protein interaction databases

BioGridi4260079. 316 interactions.
IntActiP0AF16. 1 interaction.
STRINGi511145.b1069.

Structurei

3D structure databases

ProteinModelPortaliP0AF16.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the MurJ/MviN family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105CJR. Bacteria.
COG0728. LUCA.
HOGENOMiHOG000263812.
InParanoidiP0AF16.
KOiK03980.
OMAiIFAEGSF.
OrthoDBiEOG6C0131.
PhylomeDBiP0AF16.

Family and domain databases

InterProiIPR004268. MurJ.
[Graphical view]
PfamiPF03023. MVIN. 1 hit.
[Graphical view]
PIRSFiPIRSF002869. MviN. 1 hit.
PRINTSiPR01806. VIRFACTRMVIN.
TIGRFAMsiTIGR01695. murJ_mviN. 1 hit.

Sequencei

Sequence statusi: Complete.

P0AF16-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNLLKSLAAV SSMTMFSRVL GFARDAIVAR IFGAGMATDA FFVAFKLPNL
60 70 80 90 100
LRRIFAEGAF SQAFVPILAE YKSKQGEDAT RVFVSYVSGL LTLALAVVTV
110 120 130 140 150
AGMLAAPWVI MVTAPGFADT ADKFALTSQL LKITFPYILL ISLASLVGAI
160 170 180 190 200
LNTWNRFSIP AFAPTLLNIS MIGFALFAAP YFNPPVLALA WAVTVGGVLQ
210 220 230 240 250
LVYQLPHLKK IGMLVLPRIN FHDAGAMRVV KQMGPAILGV SVSQISLIIN
260 270 280 290 300
TIFASFLASG SVSWMYYADR LMEFPSGVLG VALGTILLPS LSKSFASGNH
310 320 330 340 350
DEYNRLMDWG LRLCFLLALP SAVALGILSG PLTVSLFQYG KFTAFDALMT
360 370 380 390 400
QRALIAYSVG LIGLIVVKVL APGFYSRQDI KTPVKIAIVT LILTQLMNLA
410 420 430 440 450
FIGPLKHAGL SLSIGLAACL NASLLYWQLR KQKIFTPQPG WMAFLLRLVV
460 470 480 490 500
AVLVMSGVLL GMLHIMPEWS LGTMPWRLLR LMAVVLAGIA AYFAALAVLG
510
FKVKEFARRT V
Length:511
Mass (Da):55,267
Last modified:December 20, 2005 - v1
Checksum:iCB20FE3CFC9419C2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC74153.1.
AP009048 Genomic DNA. Translation: BAA35877.1.
PIRiB64850.
RefSeqiNP_415587.1. NC_000913.3.
WP_001050683.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74153; AAC74153; b1069.
BAA35877; BAA35877; BAA35877.
GeneIDi945487.
KEGGiecj:JW1056.
eco:b1069.
PATRICi32117377. VBIEscCol129921_1111.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC74153.1.
AP009048 Genomic DNA. Translation: BAA35877.1.
PIRiB64850.
RefSeqiNP_415587.1. NC_000913.3.
WP_001050683.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP0AF16.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260079. 316 interactions.
IntActiP0AF16. 1 interaction.
STRINGi511145.b1069.

Protein family/group databases

TCDBi2.A.66.4.3. the multidrug/oligosaccharidyl-lipid/polysaccharide (mop) flippase superfamily.

Proteomic databases

PaxDbiP0AF16.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74153; AAC74153; b1069.
BAA35877; BAA35877; BAA35877.
GeneIDi945487.
KEGGiecj:JW1056.
eco:b1069.
PATRICi32117377. VBIEscCol129921_1111.

Organism-specific databases

EchoBASEiEB3639.
EcoGeneiEG13880. murJ.

Phylogenomic databases

eggNOGiENOG4105CJR. Bacteria.
COG0728. LUCA.
HOGENOMiHOG000263812.
InParanoidiP0AF16.
KOiK03980.
OMAiIFAEGSF.
OrthoDBiEOG6C0131.
PhylomeDBiP0AF16.

Enzyme and pathway databases

BioCyciEcoCyc:G6561-MONOMER.
ECOL316407:JW1056-MONOMER.
MetaCyc:G6561-MONOMER.

Miscellaneous databases

PROiP0AF16.

Family and domain databases

InterProiIPR004268. MurJ.
[Graphical view]
PfamiPF03023. MVIN. 1 hit.
[Graphical view]
PIRSFiPIRSF002869. MviN. 1 hit.
PRINTSiPR01806. VIRFACTRMVIN.
TIGRFAMsiTIGR01695. murJ_mviN. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "Global topology analysis of the Escherichia coli inner membrane proteome."
    Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
    Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
    Strain: K12 / MG1655 / ATCC 47076.
  5. "Involvement of an essential gene, mviN, in murein synthesis in Escherichia coli."
    Inoue A., Murata Y., Takahashi H., Tsuji N., Fujisaki S., Kato J.
    J. Bacteriol. 190:7298-7301(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PEPTIDOGLYCAN BIOSYNTHESIS.
  6. "Bioinformatics identification of MurJ (MviN) as the peptidoglycan lipid II flippase in Escherichia coli."
    Ruiz N.
    Proc. Natl. Acad. Sci. U.S.A. 105:15553-15557(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PEPTIDOGLYCAN BIOSYNTHESIS, PROBABLE FUNCTION IN LIPID II TRANSLOCATION, GENE NAME.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  7. "Structure-function analysis of MurJ reveals a solvent-exposed cavity containing residues essential for peptidoglycan biogenesis in Escherichia coli."
    Butler E.K., Davis R.M., Bari V., Nicholson P.A., Ruiz N.
    J. Bacteriol. 195:4639-4649(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROBABLE FUNCTION AS A TRANSPORTER, SUBCELLULAR LOCATION, TOPOLOGY, MUTAGENESIS OF ARG-18; ARG-24; ASP-39; ARG-52 AND ARG-270.
  8. "Bacterial cell wall. MurJ is the flippase of lipid-linked precursors for peptidoglycan biogenesis."
    Sham L.T., Butler E.K., Lebar M.D., Kahne D., Bernhardt T.G., Ruiz N.
    Science 345:220-222(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A FLIPPASE.

Entry informationi

Entry nameiMURJ_ECOLI
AccessioniPrimary (citable) accession number: P0AF16
Secondary accession number(s): P75932
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: January 20, 2016
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

FtsW (AC P0ABG4) is also proposed to act as a lipid II flippase. The identity of the lipid II flippase is controversial with conflicting in vivo and in vitro results.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.