P95379 (LPXA_NEIMB) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 91.
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 | Neisseria meningitidis serogroup B (strain MC58) [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 122586 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria › ![]() |
Protein attributes
| Sequence length | 258 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 Reference 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 – 258 | 258 | Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase HAMAP-Rule MF_00387 | PRO_0000188055 | |||||
Experimental info | |||||||||
| Sequence conflict | 64 | 1 | L → F in AAC45424. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Isolation and characterization of the Neisseria meningitidis lpxD-fabZ-lpxA gene cluster involved in lipid A biosynthesis." Steeghs L., Jennings M.P., Poolman J.T., Der Ley P. Gene 190:263-270(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: MC58. |
| [2] | "Complete genome sequence of Neisseria meningitidis serogroup B strain MC58." Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H., Salzberg S.L., White O. Venter J.C.Science 287:1809-1815(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MC58. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U79481 Genomic DNA. Translation: AAC45424.1. AE002098 Genomic DNA. Translation: AAF40635.1. |
| PIR | C81228. |
| RefSeq | NP_273236.1. NC_003112.2. |
3D structure databases | |
| ProteinModelPortal | P95379. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 122586.NMB0178. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAF40635; AAF40635; NMB0178. |
| GeneID | 902285. |
| KEGG | nme:NMB0178. |
| PATRIC | 20355381. VBINeiMen85645_0220. |
Phylogenomic databases | |
| eggNOG | COG1043. |
| HOGENOM | HOG000294326. |
| KO | K00677. |
| OMA | REFCTFN. |
| ProtClustDB | PRK05289. |
Enzyme and pathway databases | |
| BioCyc | NMEN122586:GHGG-179-MONOMER. |
| UniPathway | UPA00359; UER00477. |
Family and domain databases | |
| HAMAP | MF_00387. LpxA. |
| InterPro | IPR001451. Hexapep_transf. IPR010137. Lipid_A_LpxA. IPR011004. Trimer_LpxA-like. [Graphical view] |
| Pfam | PF00132. Hexapep. 4 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. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | LPXA_NEIMB | ||||||||
| Accession | Primary (citable) accession number: P95379 Secondary accession number(s): Q9K1H3 | ||||||||
| 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
