B0B7F9 (LPXD_CHLT2) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 31.
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: UDP-3-O-acylglucosamine N-acyltransferase EC=2.3.1.- | ||||
| Gene names |
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| Organism | Chlamydia trachomatis serovar L2 (strain 434/Bu / ATCC VR-902B) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 471472 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Chlamydiae › Chlamydiales › Chlamydiaceae › Chlamydia/Chlamydophila group › Chlamydia |
Protein attributes
| Sequence length | 354 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is 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_00523 |
| Catalytic activity | (3R)-3-hydroxyacyl-[acyl-carrier-protein] + UDP-3-O-acyl-alpha-D-glucosamine = UDP-2,3-diacyl-alpha-D-glucosamine + [acyl-carrier-protein]. HAMAP MF_00523 |
| Pathway | Bacterial outer membrane biogenesis; LPS lipid A biosynthesis. HAMAP MF_00523 |
| Subunit structure | Homotrimer By similarity. HAMAP MF_00523 |
| Sequence similarities | Belongs to the transferase hexapeptide repeat family. LpxD subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Lipid A biosynthesis Lipid synthesis |
| Domain | Repeat |
| Molecular function | Acyltransferase Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | lipid A biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | transferase activity, transferring acyl groups other than amino-acyl groups Inferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 354 | 354 | UDP-3-O-acylglucosamine N-acyltransferase HAMAP MF_00523 | PRO_1000127669 | |||||
Sites | |||||||||
| Active site | 247 | 1 | Proton acceptor By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 2 | 1 | S → C in AAC35947. Ref.1 | ||||||
| Sequence conflict | 7 | 1 | S → F in AAC35947. Ref.1 | ||||||
| Sequence conflict | 226 | 1 | G → A in AAC35947. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Use of primate model system to identify Chlamydia trachomatis protein antigens recognized uniquely in the context of infection." Bannantine J.P., Rockey D.D. Microbiology 145:2077-2085(1999) [PubMed: 10463174] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Chlamydia trachomatis: genome sequence analysis of lymphogranuloma venereum isolates." Thomson N.R., Holden M.T.G., Carder C., Lennard N., Lockey S.J., Marsh P., Skipp P., O'Connor C.D., Goodhead I., Norbertzcak H., Harris B., Ormond D., Rance R., Quail M.A., Parkhill J., Stephens R.S., Clarke I.N. Genome Res. 18:161-171(2008) [PubMed: 18032721] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 434/Bu / ATCC VR-902B. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF077009 Genomic DNA. Translation: AAC35947.1. AM884176 Genomic DNA. Translation: CAP03935.1. |
| RefSeq | YP_001654572.1. NC_010287.1. |
3D structure databases | |
| ProteinModelPortal | B0B7F9. |
| SMR | B0B7F9. Positions 3-348. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | B0B7F9. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 5858495. |
| GenomeReviews | Gene locus CTL0495 in contig AM884176_GR. |
| KEGG | ctb:CTL0495. |
| PATRIC | 20376534. VBIChlTra32542_0533. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG469615. |
| OMA | SYPAKIM. |
| ProtClustDB | PRK00892. |
Enzyme and pathway databases | |
| BioCyc | CTRA471472:CTL0495-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00523. LpxD. [Tree] |
| InterPro | IPR001451. Hexapep_transf. IPR011004. Trimer_LpxA-like. IPR007691. UDP-3-O_GlcNAc_AcTrfase. IPR020573. UDP_GlcNAc_AcTrfase_non-rep. [Graphical view] |
| KO | K02536. |
| Pfam | PF00132. Hexapep. 6 hits. PF04613. LpxD. 1 hit. [Graphical view] |
| SUPFAM | SSF51161. Trimer_LpxA_like. 1 hit. |
| TIGRFAMs | TIGR01853. Lipid_A_lpxD. 1 hit. |
| PROSITE | PS00101. HEXAPEP_TRANSFERASES. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | LPXD_CHLT2 | ||||||||
| Accession | Primary (citable) accession number: B0B7F9 Secondary accession number(s): O84245, Q9S530 | ||||||||
| 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