P27243 · WAAL_ECOLI
- ProteinO-antigen ligase
- GenewaaL
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids419 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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
Activity regulation
Activity does not require ATP and magnesium ions.
Pathway
Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Molecular Function | glycosyltransferase activity | |
Molecular Function | ligase activity | |
Biological Process | lipopolysaccharide core region biosynthetic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameO-antigen ligase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP27243
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell inner membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-19 | Cytoplasmic | ||||
Sequence: MLTSFKLHSLKPYTLKSSM | ||||||
Transmembrane | 20-38 | Helical; Name=1 | ||||
Sequence: ILEIITYILCFFSMIIAFV | ||||||
Topological domain | 39-43 | Periplasmic | ||||
Sequence: DNTFS | ||||||
Transmembrane | 44-61 | Helical; Name=2 | ||||
Sequence: IKIYNITAIVCLLSLILR | ||||||
Topological domain | 62-71 | Cytoplasmic | ||||
Sequence: GRQENYNIKN | ||||||
Transmembrane | 72-91 | Helical; Name=3 | ||||
Sequence: LILPLSIFLIGLLDLIWYSA | ||||||
Topological domain | 92-107 | Periplasmic | ||||
Sequence: FKVDNSPFRATYHSYL | ||||||
Transmembrane | 108-125 | Helical; Name=4 | ||||
Sequence: NTAKIFIFGSFIVFLTLT | ||||||
Topological domain | 126-134 | Cytoplasmic | ||||
Sequence: SQLKSKKES | ||||||
Transmembrane | 135-153 | Helical; Name=5 | ||||
Sequence: VLYTLYSLSFLIAGYAMYI | ||||||
Topological domain | 154-167 | Periplasmic | ||||
Sequence: NSIHENDRISFGVG | ||||||
Transmembrane | 168-187 | Helical; Name=6 | ||||
Sequence: TATGAAYSTMLIGIVSGVAI | ||||||
Topological domain | 188-194 | Cytoplasmic | ||||
Sequence: LYTKKNH | ||||||
Transmembrane | 195-211 | Helical; Name=7 | ||||
Sequence: PFLFLLNSCAVLYVLAL | ||||||
Topological domain | 212-216 | Periplasmic | ||||
Sequence: TQTRA | ||||||
Transmembrane | 217-234 | Helical; Name=8 | ||||
Sequence: TLLLFPIICVAALIAYYN | ||||||
Topological domain | 235-240 | Cytoplasmic | ||||
Sequence: KSPKKF | ||||||
Transmembrane | 241-259 | Helical; Name=9 | ||||
Sequence: TSSIVLLIAILASIVIIFN | ||||||
Topological domain | 260-348 | Periplasmic | ||||
Sequence: KPIQNRYNEALNDLNSYTNANSVTSLGARLAMYEIGLNIFIKSPFSFRSAESRAESMNLLVAEHNRLRGALEFSNVHLHNEIIEAGSLK | ||||||
Transmembrane | 349-367 | Helical; Name=10 | ||||
Sequence: GLMGIFSTLFLYFSLFYIA | ||||||
Topological domain | 368-372 | Cytoplasmic | ||||
Sequence: YKKRA | ||||||
Transmembrane | 373-391 | Helical; Name=11 | ||||
Sequence: LGLLILTLGIVGIGLSDVI | ||||||
Topological domain | 392-396 | Periplasmic | ||||
Sequence: IWARS | ||||||
Transmembrane | 397-412 | Helical; Name=12 | ||||
Sequence: IPIIIISAIVLLLVIN | ||||||
Topological domain | 413-419 | Cytoplasmic | ||||
Sequence: NRNNTIN |
Keywords
- Cellular component
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).
Deletion prevents formation of M(LPS) when colanic acid synthesis is induced (PubMed:17227761).
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 215 | Loss of activity. | ||||
Sequence: R → A | ||||||
Mutagenesis | 215 | No change in activity. | ||||
Sequence: R → K | ||||||
Mutagenesis | 265 | Leads to a reduced O-antigen surface expression. | ||||
Sequence: R → A | ||||||
Mutagenesis | 272 | Leads to a reduced O-antigen surface expression. | ||||
Sequence: D → A | ||||||
Mutagenesis | 286 | Leads to a reduced O-antigen surface expression. | ||||
Sequence: G → A | ||||||
Mutagenesis | 288 | Loss of activity. | ||||
Sequence: R → A | ||||||
Mutagenesis | 303 | No change in activity. | ||||
Sequence: P → A | ||||||
Mutagenesis | 338 | Loss of activity. | ||||
Sequence: H → A | ||||||
Mutagenesis | 389 | Loss of activity. | ||||
Sequence: D → A |
Miscellaneous
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000097284 | 1-419 | O-antigen ligase | |||
Sequence: MLTSFKLHSLKPYTLKSSMILEIITYILCFFSMIIAFVDNTFSIKIYNITAIVCLLSLILRGRQENYNIKNLILPLSIFLIGLLDLIWYSAFKVDNSPFRATYHSYLNTAKIFIFGSFIVFLTLTSQLKSKKESVLYTLYSLSFLIAGYAMYINSIHENDRISFGVGTATGAAYSTMLIGIVSGVAILYTKKNHPFLFLLNSCAVLYVLALTQTRATLLLFPIICVAALIAYYNKSPKKFTSSIVLLIAILASIVIIFNKPIQNRYNEALNDLNSYTNANSVTSLGARLAMYEIGLNIFIKSPFSFRSAESRAESMNLLVAEHNRLRGALEFSNVHLHNEIIEAGSLKGLMGIFSTLFLYFSLFYIAYKKRALGLLILTLGIVGIGLSDVIIWARSIPIIIISAIVLLLVINNRNNTIN |
Proteomic databases
Expression
Induction
Expressed in both exponential and stationary phase in rich medium (at protein level).
Structure
Sequence
- Sequence statusComplete
- Length419
- Mass (Da)46,878
- Last updated2003-08-29 v2
- ChecksumE15382BD2CC70533
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 205-224 | in Ref. 1; AAA24524 | ||||
Sequence: VLYVLALTQTRATLLLFPII → GTLCSGANTNQSNPTPVPYN | ||||||
Sequence conflict | 307 | in Ref. 1; AAA24524 | ||||
Sequence: R → T | ||||||
Sequence conflict | 344 | in Ref. 1; AAA24524 | ||||
Sequence: A → R |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |