Q9PIM1 (LPXA_CAMJE) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 71.
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 |
| ||||
| Organism | Campylobacter jejuni | ||||
| Taxonomic identifier | 197 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter |
Protein attributes
| Sequence length | 263 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
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 MF_00387 |
| Catalytic activity | (R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] + UDP-N-acetylglucosamine = [acyl-carrier-protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine. HAMAP 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 MF_00387 |
| Subunit structure | Homotrimer By similarity. HAMAP MF_00387 |
| Subcellular location | Cytoplasm By similarity HAMAP MF_00387. |
| Sequence similarities | Belongs to the transferase hexapeptide repeat family. LpxA subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Lipid A biosynthesis Lipid synthesis |
| Cellular component | Cytoplasm |
| Domain | Repeat |
| Molecular function | Acyltransferase Transferase |
| Technical term | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | lipid A biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| 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: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||
Molecule processing | |||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 263 | 263 | Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase HAMAP MF_00387 | PRO_0000188038 | |||||||||||||||||
Secondary structure | |||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||
| Beta strand | 182 – 185 | 4 | |||||||||||||||||||
| Beta strand | 190 – 194 | 5 | |||||||||||||||||||
| Turn | 200 – 202 | 3 | |||||||||||||||||||
| Helix | 205 – 219 | 15 | |||||||||||||||||||
| Helix | 224 – 232 | 9 | |||||||||||||||||||
| Helix | 238 – 249 | 12 | |||||||||||||||||||
Sequences
| ||||||||||||||||||
References
| [1] | "The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences." Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. Barrell B.G.Nature 403:665-668(2000) [PubMed: 10688204] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCTC 11168 / Serotype O:2. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | AL111168 Genomic DNA. Translation: CAL34428.1. | ||||||||||||
| PIR | A81446. | ||||||||||||
| RefSeq | YP_002343716.1. NC_002163.1. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | Q9PIM1. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| IntAct | Q9PIM1. 31 interactions. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| GeneID | 904599. | ||||||||||||
| GenomeReviews | Gene locus Cj0274 in contig AL111168_GR. | ||||||||||||
| KEGG | cje:Cj0274. | ||||||||||||
| PATRIC | 20057469. VBICamJej33762_0268. | ||||||||||||
Phylogenomic databases | |||||||||||||
| HOGENOM | HBG659295. | ||||||||||||
| OMA | REFCTFN. | ||||||||||||
| ProtClustDB | PRK05289. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BioCyc | CJEJ192222:CJ0274-MONOMER. | ||||||||||||
Family and domain databases | |||||||||||||
| HAMAP | MF_00387. LpxA. [Tree] | ||||||||||||
| InterPro | IPR001451. Hexapep_transf. IPR018357. Hexapep_transf_CS. IPR010137. Lipid_A_lpxA. IPR011004. Trimer_LpxA-like. [Graphical view] | ||||||||||||
| KO | K00677. | ||||||||||||
| Pfam | PF00132. Hexapep. 3 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. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | LPXA_CAMJE | ||||||||
| Accession | Primary (citable) accession number: Q9PIM1 Secondary accession number(s): Q0PBN1 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with