P0AC78 · WECA_ECOLI

  • Protein
    Undecaprenyl-phosphate alpha-N-acetylglucosaminyl 1-phosphate transferase
  • Gene
    wecA
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Catalyzes the transfer of the GlcNAc-1-phosphate moiety from UDP-GlcNAc onto the carrier lipid undecaprenyl phosphate (C55-P), yielding GlcNAc-pyrophosphoryl-undecaprenyl (GlcNAc-PP-C55). It is the first lipid-linked intermediate involved in enterobacterial common antigen (ECA) synthesis, and an acceptor for the addition of subsequent sugars to complete the biosynthesis of O-antigen lipopolysaccharide (LPS) in many E.coli O types. The apparent affinity of WecA for the polyisoprenyl phosphate substrates increases with the polyisoprenyl chain length. WecA is unable to utilize dolichyl phosphate (Dol-P).

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Activity regulation

Inhibited by tunicamycin.

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
5.6 μMUDP-GlcNAc
0.12 μMUDP-GlcNAcin the presence of Mg2+
0.19 μMUDP-GlcNAcin the presence of Mn2+
1.7 mMMg2+
0.3 mMMn2+
Vmax pH TEMPERATURE[C] NOTES EVIDENCE
57 pmol/min/mg(in the presence of Mg2+)
56 pmol/min/mg(in the presence of Mn2+)

Pathway

Bacterial outer membrane biogenesis; LPS O-antigen biosynthesis.
Bacterial outer membrane biogenesis; enterobacterial common antigen biosynthesis.

Features

Showing features for site.

TypeIDPosition(s)Description
Site90Important in orienting the substrate
Site91Important in orienting the substrate; probably interacts with magnesium or manganese
Site156Could be required for catalysis
Site159Could be required for catalysis

GO annotations

AspectTerm
Cellular ComponentGram-negative-bacterium-type cell wall
Cellular Componentmembrane
Cellular Componentplasma membrane
Molecular Functionglycosyltransferase activity
Molecular Functionidentical protein binding
Molecular Functionmagnesium ion binding
Molecular Functionmanganese ion binding
Molecular Functionphospho-N-acetylmuramoyl-pentapeptide-transferase activity
Molecular Functionphosphotransferase activity, for other substituted phosphate groups
Molecular FunctionUDP-N-acetylglucosamine-undecaprenyl-phosphate N-acetylglucosaminephosphotransferase activity
Biological Processcell wall macromolecule biosynthetic process
Biological Processcell wall organization
Biological Processenterobacterial common antigen biosynthetic process
Biological Processlipopolysaccharide biosynthetic process
Biological ProcessO antigen biosynthetic process

Keywords

Enzyme and pathway databases

Protein family/group databases

    • 9.B.146.1.7the putative undecaprenyl-phosphate n-acetylglucosaminyl transferase (murg) family

Names & Taxonomy

Protein names

  • Recommended name
    Undecaprenyl-phosphate alpha-N-acetylglucosaminyl 1-phosphate transferase
  • EC number
  • Alternative names
    • UDP-GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase
    • Undecaprenyl-phosphate GlcNAc-1-phosphate transferase

Gene names

    • Name
      wecA
    • Synonyms
      rfe
    • Ordered locus names
      b3784, JW3758

Organism names

  • Taxonomic identifier
  • Strains
    • K12
    • O8:K27
    • K12 / MB2884
    • K12 / MG1655 / ATCC 47076
    • K12 / W3110 / ATCC 27325 / DSM 5911
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia

Accessions

  • Primary accession
    P0AC78
  • Secondary accessions
    • P24235
    • P76751
    • Q2M892
    • Q9F8C8

Proteomes

Subcellular Location

Cell inner membrane
; Multi-pass membrane protein
Note: Localizes to discrete regions in the plasma membrane.

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-2Periplasmic
Transmembrane3-23Helical
Topological domain24-45Cytoplasmic
Transmembrane46-66Helical
Topological domain67-68Periplasmic
Transmembrane69-89Helical
Topological domain90-105Cytoplasmic
Transmembrane106-126Helical
Topological domain127-131Periplasmic
Transmembrane132-152Helical
Topological domain153-157Cytoplasmic
Transmembrane158-178Helical
Topological domain179-186Periplasmic
Transmembrane187-207Helical
Topological domain208-212Cytoplasmic
Transmembrane213-233Helical
Topological domain234-241Periplasmic
Transmembrane242-262Helical
Topological domain263-293Cytoplasmic
Transmembrane294-314Helical
Topological domain315-317Periplasmic
Transmembrane318-338Helical
Topological domain339-367Cytoplasmic

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis35Decrease in activity; both in vivo and in vitro.
Mutagenesis90Reduces slightly the velocity and shows a small increase of the affinity for the transferase.
Mutagenesis90-91Loss of activity in vivo. Decrease in activity in vitro. No change in binding to tunicamycin.
Mutagenesis91Reduces slightly the velocity and shows a small increase of the affinity for the transferase.
Mutagenesis94No loss in activity; both in vivo and in vitro.
Mutagenesis156Loss of activity.
Mutagenesis156Loss of activity; both in vivo and in vitro; when associated with E-159.
Mutagenesis156Loss of activity; both in vivo and in vitro. No binding to tunicamycin; when associated with G-159.
Mutagenesis159The activity is detectable but drastically reduced.
Mutagenesis159Loss of activity; both in vivo and in vitro; when associated with E-156.
Mutagenesis159Loss of activity; both in vivo and in vitro. No binding to tunicamycin; when associated with G-156.
Mutagenesis265Decrease in activity. Reduces binding to tunicamycin.
Mutagenesis276No loss of activity; both in vivo and in vitro.
Mutagenesis279Loss of activity. No binding to tunicamycin.
Mutagenesis279-282Loss of activity. No binding to tunicamycin.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001089411-367Undecaprenyl-phosphate alpha-N-acetylglucosaminyl 1-phosphate transferase

Proteomic databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the glycosyltransferase 4 family. WecA subfamily.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    367
  • Mass (Da)
    40,957
  • Last updated
    2005-11-08 v1
  • Checksum
    6EB11CC80C6B9CC8
MNLLTVSTDLISIFLFTTLFLFFARKVAKKVGLVDKPNFRKRHQGLIPLVGGISVYAGICFTFGIVDYYIPHASLYLACAGVLVFIGALDDRFDISVKIRATIQAAVGIVMMVFGKLYLSSLGYIFGSWEMVLGPFGYFLTLFAVWAAINAFNMVDGIDGLLGGLSCVSFAAIGMILWFDGQTSLAIWCFAMIAAILPYIMLNLGILGRRYKVFMGDAGSTLIGFTVIWILLETTQGKTHPISPVTALWIIAIPLMDMVAIMYRRLRKGMSPFSPDRQHIHHLIMRAGFTSRQAFVLITLAAALLASIGVLAEYSHFVPEWVMLVLFLLAFFLYGYCIKRAWKVARFIKRVKRRLRRNRGGSPNLTK

Sequence caution

The sequence AAA24526.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.
The sequence AAB20842.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict8in Ref. 1; AAB20842
Sequence conflict73in Ref. 1; AAB20842
Sequence conflict116in Ref. 3; AAG26342

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
S75640
EMBL· GenBank· DDBJ
AAB20842.1
EMBL· GenBank· DDBJ
Genomic DNA Different initiation
M76129
EMBL· GenBank· DDBJ
AAA24526.1
EMBL· GenBank· DDBJ
Genomic DNA Different initiation
AF248031
EMBL· GenBank· DDBJ
AAG26342.1
EMBL· GenBank· DDBJ
Genomic DNA
M87049
EMBL· GenBank· DDBJ
AAA67584.1
EMBL· GenBank· DDBJ
Genomic DNA
U00096
EMBL· GenBank· DDBJ
AAC76789.1
EMBL· GenBank· DDBJ
Genomic DNA
AP009048
EMBL· GenBank· DDBJ
BAE77514.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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