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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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13880. murJ.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 5CytoplasmicSequence analysis5
Transmembranei6 – 32HelicalSequence analysisAdd BLAST27
Topological domaini33 – 40PeriplasmicSequence analysis8
Transmembranei41 – 69HelicalSequence analysisAdd BLAST29
Topological domaini70 – 82CytoplasmicSequence analysisAdd BLAST13
Transmembranei83 – 109HelicalSequence analysisAdd BLAST27
Topological domaini110 – 123PeriplasmicSequence analysisAdd BLAST14
Transmembranei124 – 154HelicalSequence analysisAdd BLAST31
Topological domaini155 – 156CytoplasmicSequence analysis2
Transmembranei157 – 178HelicalSequence analysisAdd BLAST22
Topological domaini179 – 185PeriplasmicSequence analysis7
Transmembranei186 – 207HelicalSequence analysisAdd BLAST22
Topological domaini208 – 223CytoplasmicSequence analysisAdd BLAST16
Transmembranei224 – 253HelicalSequence analysisAdd BLAST30
Topological domaini254 – 263PeriplasmicSequence analysis10
Transmembranei264 – 292HelicalSequence analysisAdd BLAST29
Topological domaini293 – 302CytoplasmicSequence analysis10
Transmembranei303 – 337HelicalSequence analysisAdd BLAST35
Topological domaini338 – 346PeriplasmicSequence analysis9
Transmembranei347 – 374HelicalSequence analysisAdd BLAST28
Topological domaini375 – 379CytoplasmicSequence analysis5
Transmembranei380 – 402HelicalSequence analysisAdd BLAST23
Topological domaini403 – 409PeriplasmicSequence analysis7
Transmembranei410 – 429HelicalSequence analysisAdd BLAST20
Topological domaini430 – 443CytoplasmicSequence analysisAdd BLAST14
Transmembranei444 – 463HelicalSequence analysisAdd BLAST20
Topological domaini464 – 477PeriplasmicSequence analysisAdd BLAST14
Transmembranei478 – 499HelicalSequence analysisAdd BLAST22
Topological domaini500 – 511CytoplasmicSequence analysisAdd BLAST12

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)DescriptionActionsGraphical viewLength
Mutagenesisi18R → A or C: Lack of activity. 1 Publication1
Mutagenesisi24R → A or C: Lack of activity. 1 Publication1
Mutagenesisi39D → A or C: Lack of activity. 1 Publication1
Mutagenesisi52R → A: Decrease in activity. 1 Publication1
Mutagenesisi52R → C: Lack of activity. 1 Publication1
Mutagenesisi270R → A or C: Lack of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001820061 – 511Lipid II flippase MurJAdd BLAST511

Proteomic databases

PaxDbiP0AF16.
PRIDEiP0AF16.

Interactioni

Protein-protein interaction databases

BioGridi4260079. 316 interactors.
IntActiP0AF16. 1 interactor.
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.
PhylomeDBiP0AF16.

Family and domain databases

CDDicd13123. MATE_MurJ_like. 1 hit.
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 interactors.
IntActiP0AF16. 1 interactor.
STRINGi511145.b1069.

Protein family/group databases

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

Proteomic databases

PaxDbiP0AF16.
PRIDEiP0AF16.

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.
PhylomeDBiP0AF16.

Enzyme and pathway databases

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

Miscellaneous databases

PROiP0AF16.

Family and domain databases

CDDicd13123. MATE_MurJ_like. 1 hit.
InterProiIPR004268. MurJ.
[Graphical view]
PfamiPF03023. MVIN. 1 hit.
[Graphical view]
PIRSFiPIRSF002869. MviN. 1 hit.
PRINTSiPR01806. VIRFACTRMVIN.
TIGRFAMsiTIGR01695. murJ_mviN. 1 hit.
ProtoNetiSearch...

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: November 2, 2016
This is version 87 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.