P27243 · WAAL_ECOLI

Function

function

Transferase involved in the biosynthesis of the lipopolysaccharide (LPS) (PubMed:21983211).
In vitro, catalyzes the transfer of a polymerized O-antigen molecule from its polyprenyl diphosphate membrane anchor to a terminal sugar of the lipid A-core oligosaccharide, finalizing the biosynthesis of the lipopolysaccharide (PubMed:21983211, PubMed:30047569).
The enzyme is functional and can be used to give diverse hybrid O-antigens in vitro, but K12 strains do not produce the O-antigen in vivo due to mutations in the rfb gene cluster (Probable). K12 strains are phenotypically rough, their lipopolysaccharide having a complete core structure, but no O-antigen (Probable). In highly mucoid K12 strains, WaaL can ligate colanic acid (CA or M-antigen) repeats to a significant proportion of lipopolysaccharide (LPS) core acceptor molecules, forming the LPS glycoform M(LPS) (PubMed:17227761).
The attachment point was identified as O-7 of the L-glycero-D-manno-heptose of the outer LPS core, the same position used for O-antigen ligation (PubMed:17227761).
Cannot catalyze ATP hydrolysis in vitro (PubMed:21983211).

Catalytic activity

  • a lipid-linked O antigen + a lipid A-core oligosaccharide = a lipopolysaccharide + a polyisoprenyl diphosphate.
    EC:2.4.99.26 (UniProtKB | ENZYME | Rhea)

Activity regulation

Activity does not require ATP and magnesium ions.

Pathway

Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis.

GO annotations

AspectTerm
Cellular Componentplasma membrane
Molecular Functionglycosyltransferase activity
Molecular Functionligase activity
Biological Processlipopolysaccharide core region biosynthetic process

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    O-antigen ligase
  • EC number
  • Alternative names
    • Surface polymer:lipid A-core ligase

Gene names

    • Name
      waaL
    • Synonyms
      rfaL
    • Ordered locus names
      b3622, JW3597

Organism names

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

Accessions

  • Primary accession
    P27243
  • Secondary accessions
    • Q2M7T6

Proteomes

Subcellular Location

Cell inner membrane
; Multi-pass membrane protein

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-19Cytoplasmic
Transmembrane20-38Helical; Name=1
Topological domain39-43Periplasmic
Transmembrane44-61Helical; Name=2
Topological domain62-71Cytoplasmic
Transmembrane72-91Helical; Name=3
Topological domain92-107Periplasmic
Transmembrane108-125Helical; Name=4
Topological domain126-134Cytoplasmic
Transmembrane135-153Helical; Name=5
Topological domain154-167Periplasmic
Transmembrane168-187Helical; Name=6
Topological domain188-194Cytoplasmic
Transmembrane195-211Helical; Name=7
Topological domain212-216Periplasmic
Transmembrane217-234Helical; Name=8
Topological domain235-240Cytoplasmic
Transmembrane241-259Helical; Name=9
Topological domain260-348Periplasmic
Transmembrane349-367Helical; Name=10
Topological domain368-372Cytoplasmic
Transmembrane373-391Helical; Name=11
Topological domain392-396Periplasmic
Transmembrane397-412Helical; Name=12
Topological domain413-419Cytoplasmic

Keywords

Phenotypes & Variants

Disruption phenotype

Deletion of the gene has no appreciable effect on the LPS profiles (PubMed:17227761).
Deletion prevents formation of M(LPS) when colanic acid synthesis is induced (PubMed:17227761).

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis215Loss of activity.
Mutagenesis215No change in activity.
Mutagenesis265Leads to a reduced O-antigen surface expression.
Mutagenesis272Leads to a reduced O-antigen surface expression.
Mutagenesis286Leads to a reduced O-antigen surface expression.
Mutagenesis288Loss of activity.
Mutagenesis303No change in activity.
Mutagenesis338Loss of activity.
Mutagenesis389Loss of activity.

Miscellaneous

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000972841-419O-antigen ligase

Proteomic databases

Expression

Induction

Expressed in both exponential and stationary phase in rich medium (at protein level).

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Structure

Family & Domains

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    419
  • Mass (Da)
    46,878
  • Last updated
    2003-08-29 v2
  • Checksum
    E15382BD2CC70533
MLTSFKLHSLKPYTLKSSMILEIITYILCFFSMIIAFVDNTFSIKIYNITAIVCLLSLILRGRQENYNIKNLILPLSIFLIGLLDLIWYSAFKVDNSPFRATYHSYLNTAKIFIFGSFIVFLTLTSQLKSKKESVLYTLYSLSFLIAGYAMYINSIHENDRISFGVGTATGAAYSTMLIGIVSGVAILYTKKNHPFLFLLNSCAVLYVLALTQTRATLLLFPIICVAALIAYYNKSPKKFTSSIVLLIAILASIVIIFNKPIQNRYNEALNDLNSYTNANSVTSLGARLAMYEIGLNIFIKSPFSFRSAESRAESMNLLVAEHNRLRGALEFSNVHLHNEIIEAGSLKGLMGIFSTLFLYFSLFYIAYKKRALGLLILTLGIVGIGLSDVIIWARSIPIIIISAIVLLLVINNRNNTIN

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict205-224in Ref. 1; AAA24524
Sequence conflict307in Ref. 1; AAA24524
Sequence conflict344in Ref. 1; AAA24524

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M95398
EMBL· GenBank· DDBJ
AAA24524.1
EMBL· GenBank· DDBJ
Genomic DNA
U00039
EMBL· GenBank· DDBJ
AAB18599.1
EMBL· GenBank· DDBJ
Genomic DNA
U00096
EMBL· GenBank· DDBJ
AAC76646.1
EMBL· GenBank· DDBJ
Genomic DNA
AP009048
EMBL· GenBank· DDBJ
BAE77670.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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