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Q5L723 (LPXA_CHLAB) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 62. 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:
Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase

Short name=UDP-N-acetylglucosamine acyltransferase
EC=2.3.1.129
Gene names
Name:lpxA
Ordered Locus Names:CAB090
OrganismChlamydophila abortus (strain DSM 27085 / S26/3) [Complete proteome] [HAMAP]
Taxonomic identifier218497 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydophila

Protein attributes

Sequence length279 AA.
Sequence statusComplete.
Protein existenceInferred 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. HAMAP-Rule MF_00387

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00387.

Sequence similarities

Belongs to the transferase hexapeptide repeat family. LpxA subfamily.

Ontologies

Keywords
   Biological processLipid A biosynthesis
Lipid biosynthesis
Lipid metabolism
   Cellular componentCytoplasm
   DomainRepeat
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processlipid A biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionacyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 279279Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase HAMAP-Rule MF_00387
PRO_0000302569

Sequences

Sequence LengthMass (Da)Tools
Q5L723 [UniParc].

Last modified June 21, 2005. Version 1.
Checksum: 49236768240BE798

FASTA27930,603
        10         20         30         40         50         60 
MTNIHPTAII EPGAKIGRNV VIEPYVVIKS TVTLCDDVVV KSYAYIDGYT TIGRGTTIWP 

        70         80         90        100        110        120 
SAMIGNKPQD LKYQGEKTYV TIGENCEIRE FAIITSSTFE GTTVSIGNNC LIMPWAHVAH 

       130        140        150        160        170        180 
NCTIGNHVVL SNHAQLAGHV VVEDYAIIGG MVGVHQFVRI GAHAMVGALS GVRRDVPPYT 

       190        200        210        220        230        240 
IGTGNPYQLG GINKVGLQRR QVGFEIRLAL IKVFKKVYRS EDGFFEALLE AQEEYGHIPE 

       250        260        270 
VQNFIHFCRN PSKRGIERGA AKEAFQEESV DKEGALVES 

« Hide

References

[1]"The Chlamydophila abortus genome sequence reveals an array of variable proteins that contribute to interspecies variation."
Thomson N.R., Yeats C., Bell K., Holden M.T.G., Bentley S.D., Livingstone M., Cerdeno-Tarraga A.-M., Harris B., Doggett J., Ormond D., Mungall K., Clarke K., Feltwell T., Hance Z., Sanders M., Quail M.A., Price C., Barrell B.G., Parkhill J., Longbottom D.
Genome Res. 15:629-640(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 27085 / S26/3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR848038 Genomic DNA. Translation: CAH63547.1.
RefSeqYP_219519.1. NC_004552.2.

3D structure databases

ProteinModelPortalQ5L723.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING218497.CAB090.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAH63547; CAH63547; CAB090.
GeneID3337454.
KEGGcab:CAB090.
PATRIC20201544. VBIChlAbo21869_0098.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1043.
HOGENOMHOG000294326.
KOK00677.
OMAIMTSAHI.
OrthoDBEOG6F81P1.

Enzyme and pathway databases

BioCycCABO218497:GJB0-96-MONOMER.
UniPathwayUPA00359; UER00477.

Family and domain databases

Gene3D1.20.1180.10. 1 hit.
HAMAPMF_00387. LpxA.
InterProIPR029098. Acetyltransf_C.
IPR001451. Hexapep_transf.
IPR018357. Hexapep_transf_CS.
IPR010137. Lipid_A_LpxA.
IPR011004. Trimer_LpxA-like.
[Graphical view]
PfamPF13720. Acetyltransf_11. 1 hit.
PF00132. Hexapep. 4 hits.
[Graphical view]
PIRSFPIRSF000456. UDP-GlcNAc_acltr. 1 hit.
SUPFAMSSF51161. SSF51161. 1 hit.
TIGRFAMsTIGR01852. lipid_A_lpxA. 1 hit.
PROSITEPS00101. HEXAPEP_TRANSFERASES. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLPXA_CHLAB
AccessionPrimary (citable) accession number: Q5L723
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: June 21, 2005
Last modified: June 11, 2014
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways