P0AC78 · WECA_ECOLI
- ProteinUndecaprenyl-phosphate alpha-N-acetylglucosaminyl 1-phosphate transferase
- GenewecA
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids367 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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
- di-trans,octa-cis-undecaprenyl phosphate + UDP-N-acetyl-alpha-D-glucosamine = N-acetyl-alpha-D-glucosaminyl-di-trans,octa-cis-undecaprenyl diphosphate + UMP
Cofactor
Protein has several cofactor binding sites:
Activity regulation
Inhibited by tunicamycin.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
5.6 μM | UDP-GlcNAc | |||||
0.12 μM | UDP-GlcNAc | in the presence of Mg2+ | ||||
0.19 μM | UDP-GlcNAc | in the presence of Mn2+ | ||||
1.7 mM | Mg2+ | |||||
0.3 mM | Mn2+ |
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 90 | Important in orienting the substrate | ||||
Sequence: D | ||||||
Site | 91 | Important in orienting the substrate; probably interacts with magnesium or manganese | ||||
Sequence: D | ||||||
Site | 156 | Could be required for catalysis | ||||
Sequence: D | ||||||
Site | 159 | Could be required for catalysis | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | Gram-negative-bacterium-type cell wall | |
Cellular Component | membrane | |
Cellular Component | plasma membrane | |
Molecular Function | glycosyltransferase activity | |
Molecular Function | identical protein binding | |
Molecular Function | magnesium ion binding | |
Molecular Function | manganese ion binding | |
Molecular Function | phospho-N-acetylmuramoyl-pentapeptide-transferase activity | |
Molecular Function | phosphotransferase activity, for other substituted phosphate groups | |
Molecular Function | UDP-N-acetylglucosamine-undecaprenyl-phosphate N-acetylglucosaminephosphotransferase activity | |
Biological Process | cell wall macromolecule biosynthetic process | |
Biological Process | cell wall organization | |
Biological Process | enterobacterial common antigen biosynthetic process | |
Biological Process | lipopolysaccharide biosynthetic process | |
Biological Process | O antigen biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameUndecaprenyl-phosphate alpha-N-acetylglucosaminyl 1-phosphate transferase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP0AC78
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell inner membrane ; Multi-pass membrane protein
Note: Localizes to discrete regions in the plasma membrane.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-2 | Periplasmic | ||||
Sequence: MN | ||||||
Transmembrane | 3-23 | Helical | ||||
Sequence: LLTVSTDLISIFLFTTLFLFF | ||||||
Topological domain | 24-45 | Cytoplasmic | ||||
Sequence: ARKVAKKVGLVDKPNFRKRHQG | ||||||
Transmembrane | 46-66 | Helical | ||||
Sequence: LIPLVGGISVYAGICFTFGIV | ||||||
Topological domain | 67-68 | Periplasmic | ||||
Sequence: DY | ||||||
Transmembrane | 69-89 | Helical | ||||
Sequence: YIPHASLYLACAGVLVFIGAL | ||||||
Topological domain | 90-105 | Cytoplasmic | ||||
Sequence: DDRFDISVKIRATIQA | ||||||
Transmembrane | 106-126 | Helical | ||||
Sequence: AVGIVMMVFGKLYLSSLGYIF | ||||||
Topological domain | 127-131 | Periplasmic | ||||
Sequence: GSWEM | ||||||
Transmembrane | 132-152 | Helical | ||||
Sequence: VLGPFGYFLTLFAVWAAINAF | ||||||
Topological domain | 153-157 | Cytoplasmic | ||||
Sequence: NMVDG | ||||||
Transmembrane | 158-178 | Helical | ||||
Sequence: IDGLLGGLSCVSFAAIGMILW | ||||||
Topological domain | 179-186 | Periplasmic | ||||
Sequence: FDGQTSLA | ||||||
Transmembrane | 187-207 | Helical | ||||
Sequence: IWCFAMIAAILPYIMLNLGIL | ||||||
Topological domain | 208-212 | Cytoplasmic | ||||
Sequence: GRRYK | ||||||
Transmembrane | 213-233 | Helical | ||||
Sequence: VFMGDAGSTLIGFTVIWILLE | ||||||
Topological domain | 234-241 | Periplasmic | ||||
Sequence: TTQGKTHP | ||||||
Transmembrane | 242-262 | Helical | ||||
Sequence: ISPVTALWIIAIPLMDMVAIM | ||||||
Topological domain | 263-293 | Cytoplasmic | ||||
Sequence: YRRLRKGMSPFSPDRQHIHHLIMRAGFTSRQ | ||||||
Transmembrane | 294-314 | Helical | ||||
Sequence: AFVLITLAAALLASIGVLAEY | ||||||
Topological domain | 315-317 | Periplasmic | ||||
Sequence: SHF | ||||||
Transmembrane | 318-338 | Helical | ||||
Sequence: VPEWVMLVLFLLAFFLYGYCI | ||||||
Topological domain | 339-367 | Cytoplasmic | ||||
Sequence: KRAWKVARFIKRVKRRLRRNRGGSPNLTK |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 35 | Decrease in activity; both in vivo and in vitro. | ||||
Sequence: D → G | ||||||
Mutagenesis | 90 | Reduces slightly the velocity and shows a small increase of the affinity for the transferase. | ||||
Sequence: D → E or N | ||||||
Mutagenesis | 90-91 | Loss of activity in vivo. Decrease in activity in vitro. No change in binding to tunicamycin. | ||||
Sequence: DD → EE or GG | ||||||
Mutagenesis | 91 | Reduces slightly the velocity and shows a small increase of the affinity for the transferase. | ||||
Sequence: D → N | ||||||
Mutagenesis | 94 | No loss in activity; both in vivo and in vitro. | ||||
Sequence: D → G | ||||||
Mutagenesis | 156 | Loss of activity. | ||||
Sequence: D → E or N | ||||||
Mutagenesis | 156 | Loss of activity; both in vivo and in vitro; when associated with E-159. | ||||
Sequence: D → E | ||||||
Mutagenesis | 156 | Loss of activity; both in vivo and in vitro. No binding to tunicamycin; when associated with G-159. | ||||
Sequence: D → G | ||||||
Mutagenesis | 159 | The activity is detectable but drastically reduced. | ||||
Sequence: D → E or N | ||||||
Mutagenesis | 159 | Loss of activity; both in vivo and in vitro; when associated with E-156. | ||||
Sequence: D → E | ||||||
Mutagenesis | 159 | Loss of activity; both in vivo and in vitro. No binding to tunicamycin; when associated with G-156. | ||||
Sequence: D → G | ||||||
Mutagenesis | 265 | Decrease in activity. Reduces binding to tunicamycin. | ||||
Sequence: R → K | ||||||
Mutagenesis | 276 | No loss of activity; both in vivo and in vitro. | ||||
Sequence: D → G | ||||||
Mutagenesis | 279 | Loss of activity. No binding to tunicamycin. | ||||
Sequence: H → S | ||||||
Mutagenesis | 279-282 | Loss of activity. No binding to tunicamycin. | ||||
Sequence: HIHH → GGGG |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000108941 | 1-367 | Undecaprenyl-phosphate alpha-N-acetylglucosaminyl 1-phosphate transferase | |||
Sequence: MNLLTVSTDLISIFLFTTLFLFFARKVAKKVGLVDKPNFRKRHQGLIPLVGGISVYAGICFTFGIVDYYIPHASLYLACAGVLVFIGALDDRFDISVKIRATIQAAVGIVMMVFGKLYLSSLGYIFGSWEMVLGPFGYFLTLFAVWAAINAFNMVDGIDGLLGGLSCVSFAAIGMILWFDGQTSLAIWCFAMIAAILPYIMLNLGILGRRYKVFMGDAGSTLIGFTVIWILLETTQGKTHPISPVTALWIIAIPLMDMVAIMYRRLRKGMSPFSPDRQHIHHLIMRAGFTSRQAFVLITLAAALLASIGVLAEYSHFVPEWVMLVLFLLAFFLYGYCIKRAWKVARFIKRVKRRLRRNRGGSPNLTK |
Proteomic databases
Structure
Family & Domains
Sequence similarities
Belongs to the glycosyltransferase 4 family. WecA subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length367
- Mass (Da)40,957
- Last updated2005-11-08 v1
- Checksum6EB11CC80C6B9CC8
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 8 | in Ref. 1; AAB20842 | ||||
Sequence: T → I | ||||||
Sequence conflict | 73 | in Ref. 1; AAB20842 | ||||
Sequence: A → V | ||||||
Sequence conflict | 116 | in Ref. 3; AAG26342 | ||||
Sequence: K → N |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |