P95379 (LPXA_NEIMB) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 80.
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 | Neisseria meningitidis serogroup B | ||||
| Taxonomic identifier | 491 [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 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 | 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 – 258 | 258 | Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase HAMAP 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: 9197543] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: MC58 / Serogroup B. |
| [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: 10710307] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MC58 / Serogroup B. |
| + | Additional computationally mapped references. |
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... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBNEIT00000010785; EBNEIP00000010405; EBNEIG00000010785. |
| GeneID | 902285. |
| GenomeReviews | Gene locus NMB0178 in contig AE002098_GR. |
| KEGG | nme:NMB0178. |
| NMPDR | fig|122586.1.peg.170. |
| PATRIC | 20355381. VBINeiMen85645_0220. |
| TIGR | NMB0178. |
Phylogenomic databases | |
| GeneTree | EBGT00050000020532. |
| HOGENOM | HBG659295. |
| OMA | REFCTFN. |
| ProtClustDB | PRK05289. |
Enzyme and pathway databases | |
| BioCyc | NMEN122586:NMB_0178-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00387. LpxA. [Tree] |
| InterPro | IPR001451. Hexapep_transf. IPR010137. Lipid_A_lpxA. IPR011004. Trimer_LpxA-like. [Graphical view] |
| KO | K00677. |
| 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 |

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