Skip Header

Contribute Send feedback
Read comments (?) or add your own

B0B7F9 (LPXD_CHLT2) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 31. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
UDP-3-O-acylglucosamine N-acyltransferase

EC=2.3.1.-
Gene names
Name:lpxD
Ordered Locus Names:CTL0495
OrganismChlamydia trachomatis serovar L2 (strain 434/Bu / ATCC VR-902B) [Complete proteome] [HAMAP]
Taxonomic identifier471472 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia

Protein attributes

Sequence length354 AA.
Sequence statusComplete.
Protein existenceInferred 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 processLipid A biosynthesis
Lipid synthesis
   DomainRepeat
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processlipid A biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functiontransferase activity, transferring acyl groups other than amino-acyl groups

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 354354UDP-3-O-acylglucosamine N-acyltransferase HAMAP MF_00523
PRO_1000127669

Sites

Active site2471Proton acceptor By similarity

Experimental info

Sequence conflict21S → C in AAC35947. Ref.1
Sequence conflict71S → F in AAC35947. Ref.1
Sequence conflict2261G → A in AAC35947. Ref.1

Sequences

Sequence LengthMass (Da)Tools
B0B7F9 [UniParc].

Last modified February 26, 2008. Version 1.
Checksum: 7DD4084538E68E77

FASTA35438,403
        10         20         30         40         50         60 
MSQSTYSLEQ LADFLKVEFQ GNGATLLSGV EEIEEAKTAH ITFLDNEKYA KHLKSSEAGA 

        70         80         90        100        110        120 
IIISRTQFQK YRDLNKNFLI TSESPSLVFQ KCLELFITPV DSGFPGIHPT AVIHPTAIIE 

       130        140        150        160        170        180 
DHVCIEPYAV VCQHAHVGSA CHIGSGSVIG AYSTVGQHSY IHPRVVIRER VSIGKRVIIQ 

       190        200        210        220        230        240 
PGAVIGSCGF GYVTSAFGQH KHLKHLGKVI IEDDVEIGAN TTIDRGRFKH SVVREGSKID 

       250        260        270        280        290        300 
NLVQIAHQVE VGQHSMIVAQ AGIAGSTKIG NHVIIGGQAG ITGHICIADH VIMMAQTGVT 

       310        320        330        340        350 
KSITSPGIYG GAPARPYQEI HRQVAKVRNL PRLEERIAAL EKLVQKLEAL SEQH 

« Hide

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.
RefSeqYP_001654572.1. NC_010287.1.

3D structure databases

ProteinModelPortalB0B7F9.
SMRB0B7F9. Positions 3-348.
ModBaseSearch...

Protein-protein interaction databases

STRINGB0B7F9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5858495.
GenomeReviewsGene locus CTL0495 in contig AM884176_GR.
KEGGctb:CTL0495.
PATRIC20376534. VBIChlTra32542_0533.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG469615.
OMASYPAKIM.
ProtClustDBPRK00892.

Enzyme and pathway databases

BioCycCTRA471472:CTL0495-MONOMER.

Family and domain databases

HAMAPMF_00523. LpxD.
[Tree]
InterProIPR001451. Hexapep_transf.
IPR011004. Trimer_LpxA-like.
IPR007691. UDP-3-O_GlcNAc_AcTrfase.
IPR020573. UDP_GlcNAc_AcTrfase_non-rep.
[Graphical view]
KOK02536.
PfamPF00132. Hexapep. 6 hits.
PF04613. LpxD. 1 hit.
[Graphical view]
SUPFAMSSF51161. Trimer_LpxA_like. 1 hit.
TIGRFAMsTIGR01853. Lipid_A_lpxD. 1 hit.
PROSITEPS00101. HEXAPEP_TRANSFERASES. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLPXD_CHLT2
AccessionPrimary (citable) accession number: B0B7F9
Secondary accession number(s): O84245, Q9S530
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 26, 2008
Last modified: January 25, 2012
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families