Q3KLU2 (LPXB_CHLTA) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 48.
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: Lipid-A-disaccharide synthase EC=2.4.1.182 | ||||
| Gene names |
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| Organism | Chlamydia trachomatis serovar A (strain HAR-13 / ATCC VR-571B) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 315277 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Chlamydiae › Chlamydiales › Chlamydiaceae › Chlamydia/Chlamydophila group › Chlamydia › ![]() |
Protein attributes
| Sequence length | 607 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell By similarity. HAMAP-Rule MF_00392 |
| Catalytic activity | UDP-2,3-bis(3-hydroxytetradecanoyl)glucosamine + 2,3-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl 1-phosphate = UDP + 2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl-1,6-beta-D-2,3-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl 1-phosphate. HAMAP-Rule MF_00392 |
| 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 5/6. HAMAP-Rule MF_00392 |
| Sequence similarities | In the C-terminal section; belongs to the LpxB family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Lipid A biosynthesis Lipid biosynthesis Lipid metabolism |
| Molecular function | Glycosyltransferase Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | lipid A biosynthetic process Inferred from electronic annotation. Source: HAMAP |
| Molecular_function | lipid-A-disaccharide synthase 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 – 607 | 607 | Lipid-A-disaccharide synthase HAMAP-Rule MF_00392 | PRO_0000255171 | ||||
Regions | ||||||||
| Region | 1 – 224 | 224 | Unknown HAMAP-Rule MF_00392 | |||||
| Region | 225 – 607 | 383 | Lipid-A-disaccharide synthase HAMAP-Rule MF_00392 | |||||
Sequences
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References
| [1] | "Comparative genomic analysis of Chlamydia trachomatis oculotropic and genitotropic strains." Carlson J.H., Porcella S.F., McClarty G., Caldwell H.D. Infect. Immun. 73:6407-6418(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: HAR-13 / ATCC VR-571B. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000051 Genomic DNA. Translation: AAX50680.1. |
| RefSeq | YP_328228.1. NC_007429.1. |
3D structure databases | |
| ProteinModelPortal | Q3KLU2. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 315277.CTA_0446. |
Protein family/group databases | |
| CAZy | GT19. Glycosyltransferase Family 19. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAX50680; AAX50680; CTA_0446. |
| GeneID | 3687903. |
| KEGG | cta:CTA_0446. |
| PATRIC | 32022780. VBIChlTra31516_0456. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG3952. |
| HOGENOM | HOG000034725. |
| KO | K00748. |
| OMA | IPRILGI. |
| ProtClustDB | PRK01021. |
Enzyme and pathway databases | |
| BioCyc | CTRA315277:GI4C-480-MONOMER. |
| UniPathway | UPA00359; UER00481. |
Family and domain databases | |
| HAMAP | MF_00392. LpxB. Fused. |
| InterPro | IPR003835. Glyco_trans_19. IPR011499. Lipid_A_biosynth. [Graphical view] |
| Pfam | PF07578. LAB_N. 2 hits. PF02684. LpxB. 1 hit. [Graphical view] |
| ProDom | PD339292. LAB_N. 2 hits. [Graphical view] [Entries sharing at least one domain] |
| TIGRFAMs | TIGR00215. lpxB. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | LPXB_CHLTA | ||||||||
| Accession | Primary (citable) accession number: Q3KLU2 | ||||||||
| 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
