P0A724 (LPXA_SHIFL) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 64.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase Short name=UDP-N-acetylglucosamine acyltransferase EC=2.3.1.129 | ||||
| Gene names |
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| Organism | Shigella flexneri [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 623 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Shigella![]() |
Protein attributes
| Sequence length | 262 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell By similarity. HAMAP-Rule MF_00387 |
| Catalytic activity | (R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] + UDP-N-acetyl-alpha-D-glucosamine = [acyl-carrier-protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetyl-alpha-D-glucosamine. HAMAP-Rule MF_00387 |
| Pathway | Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 1/6. HAMAP-Rule MF_00387 |
| Subunit structure | Homotrimer By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the transferase hexapeptide repeat family. LpxA subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Lipid A biosynthesis Lipid biosynthesis Lipid metabolism |
| Cellular component | Cytoplasm |
| Domain | Repeat |
| Molecular function | Acyltransferase Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | lipid A biosynthetic process Inferred from electronic annotation. Source: HAMAP |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase activity Inferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||
Molecule processing | |||||||
|---|---|---|---|---|---|---|---|
| Chain | 1 – 262 | 262 | Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase HAMAP-Rule MF_00387 | PRO_0000188069 | |||
Sequences
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References
| [1] | "Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157." Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y. Yu J.Nucleic Acids Res. 30:4432-4441(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 301 / Serotype 2a. |
| [2] | "Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T." Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R. Infect. Immun. 71:2775-2786(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700930 / 2457T / Serotype 2a. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE005674 Genomic DNA. Translation: AAN41833.1. AE014073 Genomic DNA. Translation: AAP15714.1. |
| RefSeq | NP_706126.1. NC_004337.2. NP_835909.1. NC_004741.1. |
3D structure databases | |
| ProteinModelPortal | P0A724. |
| SMR | P0A724. Positions 1-262. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 198214.SF0171. |
Proteomic databases | |
| PaxDb | P0A724. |
| PRIDE | P0A724. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAN41833; AAN41833; SF0171. AAP15714; AAP15714; S0174. |
| GeneID | 1027519. 1080989. |
| KEGG | sfl:SF0171. sfx:S0174. |
| PATRIC | 18701300. VBIShiFle31049_0191. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG1043. |
| HOGENOM | HOG000294326. |
| KO | K00677. |
| OMA | REFCTFN. |
| ProtClustDB | PRK05289. |
Enzyme and pathway databases | |
| UniPathway | UPA00359; UER00477. |
Family and domain databases | |
| HAMAP | MF_00387. LpxA. |
| InterPro | IPR001451. Hexapep_transf. IPR018357. Hexapep_transf_CS. IPR010137. Lipid_A_LpxA. IPR011004. Trimer_LpxA-like. [Graphical view] |
| Pfam | PF00132. Hexapep. 5 hits. [Graphical view] |
| PIRSF | PIRSF000456. UDP-GlcNAc_acltr. 1 hit. |
| SUPFAM | SSF51161. Trimer_LpxA_like. 1 hit. |
| TIGRFAMs | TIGR01852. lipid_A_lpxA. 1 hit. |
| PROSITE | PS00101. HEXAPEP_TRANSFERASES. 2 hits. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | LPXA_SHIFL | ||||||||
| Accession | Primary (citable) accession number: P0A724 Secondary accession number(s): P10440, P78243 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
