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Protein

Phospho-N-acetylmuramoyl-pentapeptide-transferase

Gene

mraY

Organism
Aquifex aeolicus (strain VF5)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.UniRule annotation3 Publications

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.UniRule annotation3 Publications

Cofactori

Mg2+3 Publications, Mn2+1 Publication

Activity regulationi

Inhibited by natural nucleoside antibiotics including tunicamycin, capuramycin and muraymycin. Usually the cofactor magnesium is not required for antibiotic binding.3 Publications

Kineticsi

  1. KM=190 µM for UDP-MurNAc-pentapeptide1 Publication

    Pathwayi: peptidoglycan biosynthesis

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

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei70InhibitorCombined sources1 Publication1
    Binding sitei75InhibitorCombined sources1 Publication1
    Binding sitei190InhibitorCombined sources1 Publication1
    Binding sitei193InhibitorCombined sources1 Publication1
    Binding sitei196InhibitorCombined sources1 Publication1
    Binding sitei264Inhibitor; via amide nitrogen and carbonyl oxygenCombined sources1 Publication1
    Binding sitei268InhibitorCombined sources1 Publication1
    Binding sitei305InhibitorCombined sources1 Publication1
    Binding sitei321Inhibitor; via carbonyl oxygenCombined sources1 Publication1

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

    Molecular functionTransferase
    Biological processCell cycle, Cell division, Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis
    LigandMagnesium, Manganese, Metal-binding

    Enzyme and pathway databases

    BioCyciAAEO224324:G1G15-40-MONOMER
    UniPathwayi
    UPA00219

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phospho-N-acetylmuramoyl-pentapeptide-transferaseUniRule annotation (EC:2.7.8.13UniRule annotation3 Publications)
    Alternative name(s):
    UDP-MurNAc-pentapeptide phosphotransferaseUniRule annotation
    Gene namesi
    Name:mraYUniRule annotation
    Ordered Locus Names:aq_053
    OrganismiAquifex aeolicus (strain VF5)
    Taxonomic identifieri224324 [NCBI]
    Taxonomic lineageiBacteriaAquificaeAquificalesAquificaceaeAquifex
    Proteomesi
    • UP000000798 Componenti: Chromosome

    Subcellular locationi

    Topology

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Topological domaini1 – 25Periplasmic1 PublicationAdd BLAST25
    Transmembranei26 – 48Helical; Name=Helix 11 PublicationAdd BLAST23
    Topological domaini49 – 74Cytoplasmic1 PublicationAdd BLAST26
    Transmembranei75 – 92Helical; Name=Helix 21 PublicationAdd BLAST18
    Topological domaini93 – 98Periplasmic1 Publication6
    Transmembranei99 – 120Helical; Name=Helix 31 PublicationAdd BLAST22
    Topological domaini121 – 130Cytoplasmic1 Publication10
    Transmembranei131 – 152Helical; Name=Helix 41 PublicationAdd BLAST22
    Topological domaini153 – 172Periplasmic1 PublicationAdd BLAST20
    Transmembranei173 – 194Helical; Name=Helix 51 PublicationAdd BLAST22
    Topological domaini195 – 197Cytoplasmic1 Publication3
    Transmembranei198 – 218Helical; Name=Helix 61 PublicationAdd BLAST21
    Topological domaini219 – 233Periplasmic1 PublicationAdd BLAST15
    Transmembranei234 – 255Helical; Name=Helix 71 PublicationAdd BLAST22
    Topological domaini256 – 264Cytoplasmic1 Publication9
    Transmembranei265 – 280Helical; Name=Helix 81 PublicationAdd BLAST16
    Topological domaini281 – 284Periplasmic1 Publication4
    Transmembranei285 – 310Helical; Name=Helix 91 PublicationAdd BLAST26
    Topological domaini311 – 332Cytoplasmic1 PublicationAdd BLAST22
    Transmembranei333 – 355Helical; Name=Helix 101 PublicationAdd BLAST23
    Topological domaini356 – 359Periplasmic1 Publication4

    GO - Cellular componenti

    Keywords - Cellular componenti

    Cell inner membrane, Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi70K → A: Reduces binding to inhibitor. 1 Publication1
    Mutagenesisi117D → A: Loss of catalytic activity. 1 Publication1
    Mutagenesisi118D → A: Loss of catalytic activity. 1 Publication1
    Mutagenesisi190N → A: Loss of catalytic activity. 1 Publication1
    Mutagenesisi193D → A: Loss of catalytic activity. 1 Publication1
    Mutagenesisi196D → A: Loss of catalytic activity. 1 Publication1
    Mutagenesisi196D → N: Loss of catalytic activity. 1 Publication1
    Mutagenesisi262F → A: Impairs binding to inhibitor. 1 Publication1
    Mutagenesisi262F → W: Reduces binding to inhibitor. 1 Publication1
    Mutagenesisi265D → A: Loss of catalytic activity. Reduces binding to inhibitor. 2 Publications1
    Mutagenesisi305Q → A: Impairs binding to inhibitor. 1 Publication1
    Mutagenesisi324H → A: Loss of catalytic activity. 1 Publication1
    Mutagenesisi325H → A: Reduces the catalytic activity. 1 Publication1
    Mutagenesisi326H → A: Reduces the catalytic activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001087721 – 359Phospho-N-acetylmuramoyl-pentapeptide-transferaseAdd BLAST359

    Proteomic databases

    PRIDEiO66465

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself5EBI-16071899,EBI-16071899

    GO - Molecular functioni

    Protein-protein interaction databases

    DIPiDIP-61734N
    STRINGi224324.aq_053

    Structurei

    Secondary structure

    1359
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    SMRiO66465
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyltransferase 4 family. MraY subfamily.UniRule annotation

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiENOG4105CPY Bacteria
    COG0472 LUCA
    HOGENOMiHOG000275122
    InParanoidiO66465
    KOiK01000
    OMAiLMSPLHH
    OrthoDBiPOG091H00VH

    Family and domain databases

    CDDicd06852 GT_MraY, 1 hit
    HAMAPiMF_00038 MraY, 1 hit
    InterProiView protein in InterPro
    IPR000715 Glycosyl_transferase_4
    IPR003524 PNAcMuramoyl-5peptid_Trfase
    IPR018480 PNAcMuramoyl-5peptid_Trfase_CS
    PANTHERiPTHR22926 PTHR22926, 1 hit
    PfamiView protein in Pfam
    PF00953 Glycos_transf_4, 1 hit
    PF10555 MraY_sig1, 1 hit
    TIGRFAMsiTIGR00445 mraY, 1 hit
    PROSITEiView protein in PROSITE
    PS01347 MRAY_1, 1 hit
    PS01348 MRAY_2, 1 hit

    Sequencei

    Sequence statusi: Complete.

    O66465-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MLYQLALLLK DYWFAFNVLK YITFRSFTAV LIAFFLTLVL SPSFINRLRK
    60 70 80 90 100
    IQRLFGGYVR EYTPESHEVK KYTPTMGGIV ILIVVTLSTL LLMRWDIKYT
    110 120 130 140 150
    WVVLLSFLSF GTIGFWDDYV KLKNKKGISI KTKFLLQVLS ASLISVLIYY
    160 170 180 190 200
    WADIDTILYF PFFKELYVDL GVLYLPFAVF VIVGSANAVN LTDGLDGLAI
    210 220 230 240 250
    GPAMTTATAL GVVAYAVGHS KIAQYLNIPY VPYAGELTVF CFALVGAGLG
    260 270 280 290 300
    FLWFNSFPAQ MFMGDVGSLS IGASLATVAL LTKSEFIFAV AAGVFVFETI
    310 320 330 340 350
    SVILQIIYFR WTGGKRLFKR APFHHHLELN GLPEPKIVVR MWIISILLAI

    IAISMLKLR
    Length:359
    Mass (Da):40,341
    Last modified:August 1, 1998 - v1
    Checksum:iB2D6292EA6EA16D4
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE000657 Genomic DNA Translation: AAC06418.1
    PIRiF70304
    RefSeqiNP_213025.1, NC_000918.1
    WP_010879963.1, NC_000918.1

    Genome annotation databases

    EnsemblBacteriaiAAC06418; AAC06418; aq_053
    GeneIDi1192662
    KEGGiaae:aq_053
    PATRICifig|224324.8.peg.41

    Similar proteinsi

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE000657 Genomic DNA Translation: AAC06418.1
    PIRiF70304
    RefSeqiNP_213025.1, NC_000918.1
    WP_010879963.1, NC_000918.1

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4J72X-ray3.30A/B1-359[»]
    5CKRX-ray2.95A1-359[»]
    SMRiO66465
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-61734N
    STRINGi224324.aq_053

    Proteomic databases

    PRIDEiO66465

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC06418; AAC06418; aq_053
    GeneIDi1192662
    KEGGiaae:aq_053
    PATRICifig|224324.8.peg.41

    Phylogenomic databases

    eggNOGiENOG4105CPY Bacteria
    COG0472 LUCA
    HOGENOMiHOG000275122
    InParanoidiO66465
    KOiK01000
    OMAiLMSPLHH
    OrthoDBiPOG091H00VH

    Enzyme and pathway databases

    UniPathwayi
    UPA00219

    BioCyciAAEO224324:G1G15-40-MONOMER

    Family and domain databases

    CDDicd06852 GT_MraY, 1 hit
    HAMAPiMF_00038 MraY, 1 hit
    InterProiView protein in InterPro
    IPR000715 Glycosyl_transferase_4
    IPR003524 PNAcMuramoyl-5peptid_Trfase
    IPR018480 PNAcMuramoyl-5peptid_Trfase_CS
    PANTHERiPTHR22926 PTHR22926, 1 hit
    PfamiView protein in Pfam
    PF00953 Glycos_transf_4, 1 hit
    PF10555 MraY_sig1, 1 hit
    TIGRFAMsiTIGR00445 mraY, 1 hit
    PROSITEiView protein in PROSITE
    PS01347 MRAY_1, 1 hit
    PS01348 MRAY_2, 1 hit
    ProtoNetiSearch...

    Entry informationi

    Entry nameiMRAY_AQUAE
    AccessioniPrimary (citable) accession number: O66465
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: August 1, 1998
    Last modified: October 10, 2018
    This is version 124 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

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