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Protein

Phospho-N-acetylmuramoyl-pentapeptide-transferase

Gene

mraY

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

First step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan.1 Publication

Catalytic activityi

UDP-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala) + undecaprenyl phosphate = UMP + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol.

Cofactori

Pathwayi: peptidoglycan biosynthesis

This protein is involved in the pathway peptidoglycan biosynthesis, which is part of Cell wall biogenesis.
View all proteins of this organism that are known to be involved in the pathway peptidoglycan biosynthesis and in Cell wall biogenesis.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Cell cycle, Cell division, Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis

Keywords - Ligandi

Magnesium, Manganese

Enzyme and pathway databases

BioCyciEcoCyc:PHOSNACMURPENTATRANS-MONOMER.
ECOL316407:JW0085-MONOMER.
MetaCyc:PHOSNACMURPENTATRANS-MONOMER.
UniPathwayiUPA00219.

Protein family/group databases

TCDBi9.B.146.1.6. the putative undecaprenyl-phosphate n-acetylglucosaminyl transferase (murg) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Phospho-N-acetylmuramoyl-pentapeptide-transferase (EC:2.7.8.13)
Alternative name(s):
UDP-MurNAc-pentapeptide phosphotransferase
Gene namesi
Name:mraY
Synonyms:murX
Ordered Locus Names:b0087, JW0085
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10604. mraY.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1818Periplasmic1 PublicationAdd
BLAST
Transmembranei19 – 4527HelicalAdd
BLAST
Topological domaini46 – 7631Cytoplasmic1 PublicationAdd
BLAST
Transmembranei77 – 9014HelicalAdd
BLAST
Topological domaini91 – 966Periplasmic1 Publication
Transmembranei97 – 11317HelicalAdd
BLAST
Topological domaini114 – 13320Cytoplasmic1 PublicationAdd
BLAST
Transmembranei134 – 15623HelicalAdd
BLAST
Topological domaini157 – 17317Periplasmic1 PublicationAdd
BLAST
Transmembranei174 – 18815HelicalAdd
BLAST
Topological domaini189 – 19911Cytoplasmic1 PublicationAdd
BLAST
Transmembranei200 – 22021HelicalAdd
BLAST
Topological domaini221 – 23818Periplasmic1 PublicationAdd
BLAST
Transmembranei239 – 25113HelicalAdd
BLAST
Topological domaini252 – 27019Cytoplasmic1 PublicationAdd
BLAST
Transmembranei271 – 28414HelicalAdd
BLAST
Topological domaini285 – 2873Periplasmic1 Publication
Transmembranei288 – 29912HelicalAdd
BLAST
Topological domaini300 – 34142Cytoplasmic1 PublicationAdd
BLAST
Transmembranei342 – 35716HelicalAdd
BLAST
Topological domaini358 – 3603Periplasmic1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL3957.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 360360Phospho-N-acetylmuramoyl-pentapeptide-transferasePRO_0000108820Add
BLAST

Proteomic databases

PaxDbiP0A6W3.

Interactioni

Protein-protein interaction databases

BioGridi4261478. 327 interactions.
STRINGi511145.b0087.

Chemistry

BindingDBiP0A6W3.

Structurei

3D structure databases

ProteinModelPortaliP0A6W3.
SMRiP0A6W3. Positions 15-358.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105CPY. Bacteria.
COG0472. LUCA.
HOGENOMiHOG000275122.
InParanoidiP0A6W3.
KOiK01000.
OMAiHQNKKDT.
OrthoDBiEOG69GZPZ.
PhylomeDBiP0A6W3.

Family and domain databases

HAMAPiMF_00038. MraY.
InterProiIPR000715. Glycosyl_transferase_4.
IPR003524. PNAcMuramoyl-5peptid_Trfase.
IPR018480. PNAcMuramoyl-5peptid_Trfase_CS.
[Graphical view]
PANTHERiPTHR22926. PTHR22926. 1 hit.
PfamiPF00953. Glycos_transf_4. 1 hit.
PF10555. MraY_sig1. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00445. mraY. 1 hit.
PROSITEiPS01347. MRAY_1. 1 hit.
PS01348. MRAY_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0A6W3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLVWLAEHLV KYYSGFNVFS YLTFRAIVSL LTALFISLWM GPRMIAHLQK
60 70 80 90 100
LSFGQVVRND GPESHFSKRG TPTMGGIMIL TAIVISVLLW AYPSNPYVWC
110 120 130 140 150
VLVVLVGYGV IGFVDDYRKV VRKDTKGLIA RWKYFWMSVI ALGVAFALYL
160 170 180 190 200
AGKDTPATQL VVPFFKDVMP QLGLFYILLA YFVIVGTGNA VNLTDGLDGL
210 220 230 240 250
AIMPTVFVAG GFALVAWATG NMNFASYLHI PYLRHAGELV IVCTAIVGAG
260 270 280 290 300
LGFLWFNTYP AQVFMGDVGS LALGGALGII AVLLRQEFLL VIMGGVFVVE
310 320 330 340 350
TLSVILQVGS FKLRGQRIFR MAPIHHHYEL KGWPEPRVIV RFWIISLMLV
360
LIGLATLKVR
Length:360
Mass (Da):39,875
Last modified:March 15, 2005 - v1
Checksum:iF3550AFA3CD636AE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51584 Genomic DNA. Translation: CAA35932.1.
X55034 Genomic DNA. Translation: CAA38864.1.
U00096 Genomic DNA. Translation: AAC73198.1.
AP009048 Genomic DNA. Translation: BAB96655.1.
PIRiS08395.
RefSeqiNP_414629.1. NC_000913.3.
WP_000964131.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73198; AAC73198; b0087.
BAB96655; BAB96655; BAB96655.
GeneIDi944814.
KEGGiecj:JW0085.
eco:b0087.
PATRICi32115279. VBIEscCol129921_0091.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51584 Genomic DNA. Translation: CAA35932.1.
X55034 Genomic DNA. Translation: CAA38864.1.
U00096 Genomic DNA. Translation: AAC73198.1.
AP009048 Genomic DNA. Translation: BAB96655.1.
PIRiS08395.
RefSeqiNP_414629.1. NC_000913.3.
WP_000964131.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP0A6W3.
SMRiP0A6W3. Positions 15-358.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261478. 327 interactions.
STRINGi511145.b0087.

Chemistry

BindingDBiP0A6W3.
ChEMBLiCHEMBL3957.

Protein family/group databases

TCDBi9.B.146.1.6. the putative undecaprenyl-phosphate n-acetylglucosaminyl transferase (murg) family.

Proteomic databases

PaxDbiP0A6W3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73198; AAC73198; b0087.
BAB96655; BAB96655; BAB96655.
GeneIDi944814.
KEGGiecj:JW0085.
eco:b0087.
PATRICi32115279. VBIEscCol129921_0091.

Organism-specific databases

EchoBASEiEB0599.
EcoGeneiEG10604. mraY.

Phylogenomic databases

eggNOGiENOG4105CPY. Bacteria.
COG0472. LUCA.
HOGENOMiHOG000275122.
InParanoidiP0A6W3.
KOiK01000.
OMAiHQNKKDT.
OrthoDBiEOG69GZPZ.
PhylomeDBiP0A6W3.

Enzyme and pathway databases

UniPathwayiUPA00219.
BioCyciEcoCyc:PHOSNACMURPENTATRANS-MONOMER.
ECOL316407:JW0085-MONOMER.
MetaCyc:PHOSNACMURPENTATRANS-MONOMER.

Miscellaneous databases

PROiP0A6W3.

Family and domain databases

HAMAPiMF_00038. MraY.
InterProiIPR000715. Glycosyl_transferase_4.
IPR003524. PNAcMuramoyl-5peptid_Trfase.
IPR018480. PNAcMuramoyl-5peptid_Trfase_CS.
[Graphical view]
PANTHERiPTHR22926. PTHR22926. 1 hit.
PfamiPF00953. Glycos_transf_4. 1 hit.
PF10555. MraY_sig1. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00445. mraY. 1 hit.
PROSITEiPS01347. MRAY_1. 1 hit.
PS01348. MRAY_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence involving murD and an open reading frame ORF-Y spacing murF and ftsW in Escherichia coli."
    Ikeda M., Wachi M., Ishino F., Matsuhashi M.
    Nucleic Acids Res. 18:1058-1058(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region."
    Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A.
    Nucleic Acids Res. 20:3305-3308(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "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.
  5. "Phospho-N-acetylmuramoyl-pentapeptide-transferase of Escherichia coli K12. Properties of the membrane-bound and the extracted and partially purified enzyme."
    Geis A., Plapp R.
    Biochim. Biophys. Acta 527:414-424(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
    Strain: K12.
  6. "The Escherichia coli mraY gene encoding UDP-N-acetylmuramoyl-pentapeptide: undecaprenyl-phosphate phospho-N-acetylmuramoyl-pentapeptide transferase."
    Ikeda M., Wachi M., Jung H.K., Ishino F., Matsuhashi M.
    J. Bacteriol. 173:1021-1026(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: K12.
  7. "Topological analysis of the mraY protein catalyzing the first membrane step of peptidoglycan synthesis."
    Bouhss A., Mengin-Lecreulx D., Le Beller D., Van Heijenoort J.
    Mol. Microbiol. 34:576-585(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY.
  8. "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.

Entry informationi

Entry nameiMRAY_ECOLI
AccessioniPrimary (citable) accession number: P0A6W3
Secondary accession number(s): P15876
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: April 13, 2016
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.