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Q3KLU2 (LPXB_CHLTA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 53. 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:
Lipid-A-disaccharide synthase

EC=2.4.1.182
Gene names
Name:lpxB
Ordered Locus Names:CTA_0446
OrganismChlamydia trachomatis serovar A (strain HAR-13 / ATCC VR-571B) [Complete proteome] [HAMAP]
Taxonomic identifier315277 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia

Protein attributes

Sequence length607 AA.
Sequence statusComplete.
Protein existenceInferred 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 processLipid A biosynthesis
Lipid biosynthesis
Lipid metabolism
   Molecular functionGlycosyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processlipid A biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionlipid-A-disaccharide synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 607607Lipid-A-disaccharide synthase HAMAP-Rule MF_00392
PRO_0000255171

Regions

Region1 – 224224Unknown HAMAP-Rule MF_00392
Region225 – 607383Lipid-A-disaccharide synthase HAMAP-Rule MF_00392

Sequences

Sequence LengthMass (Da)Tools
Q3KLU2 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: 8DF4430905BD6991

FASTA60769,030
        10         20         30         40         50         60 
MFPQKITLWL YPLGLFANLF FGTAFCVQWS LTRKKGYSVV PKIFWYLSGT GAVFMICHGF 

        70         80         90        100        110        120 
IQSQYPIALL HSFNLIIYFR NLNIASLNPL PVSKIASLLV SVATAITVSF AIGTRYLPHM 

       130        140        150        160        170        180 
TWMASPNILH LNLPEASLSW QLIGCIGLTI FSLRFFIQWF YLEYKNQSAL PAPFWKASLL 

       190        200        210        220        230        240 
GGSICLLYFL RTGDLVNVLC YGCGLFPSLA NLRIASREAF RKPFSNSCFI SAGEHSGDTL 

       250        260        270        280        290        300 
GGNLLKEMHA KYPDIHCFGV GGPQMRAQNF HALFAMEKFQ VSGFWEVLLA LPKLWYRYQL 

       310        320        330        340        350        360 
LYRNILKTNP RTVICIDFPD FHFLLIKKLR SRGYKGKIVH YVCPSIWAWR PSRKTVLEKY 

       370        380        390        400        410        420 
LDLLLLILPF EQNLFKDSAL RTVYLGHPLS ETIKSFSPNL NWKDQLHLPT DKPFIAAFPG 

       430        440        450        460        470        480 
SRRSDILRNL TIQVQAFQAS SLASTHHLLV SSANPEYDHL ILEVLQQNRC LHSHIVPSQF 

       490        500        510        520        530        540 
RYELMRECDF ALAKCGTIVL ETALNLTPTI VTCQLRPLDT FLAKYIFNII LPAYSLPNII 

       550        560        570        580        590        600 
LGRTIFPEFI GGKKDFQYED VAAALNILKT SQAQEKQKDS CRDVYQAINE SASSMKECLS 


LIFETAS 

« Hide

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.
RefSeqYP_328228.1. NC_007429.1.

3D structure databases

ProteinModelPortalQ3KLU2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING315277.CTA_0446.

Protein family/group databases

CAZyGT19. Glycosyltransferase Family 19.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAX50680; AAX50680; CTA_0446.
GeneID3687903.
KEGGcta:CTA_0446.
PATRIC32022780. VBIChlTra31516_0456.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3952.
HOGENOMHOG000034725.
KOK00748.
OMAKIIHYVC.
OrthoDBEOG6FBWZR.

Enzyme and pathway databases

BioCycCTRA315277:GI4C-446-MONOMER.
UniPathwayUPA00359; UER00481.

Family and domain databases

HAMAPMF_00392. LpxB.
InterProIPR003835. Glyco_trans_19.
IPR011499. Lipid_A_biosynth.
[Graphical view]
PfamPF07578. LAB_N. 2 hits.
PF02684. LpxB. 1 hit.
[Graphical view]
ProDomPD339292. LAB_N. 2 hits.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00215. lpxB. 1 hit.
ProtoNetSearch...

Entry information

Entry nameLPXB_CHLTA
AccessionPrimary (citable) accession number: Q3KLU2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: November 8, 2005
Last modified: May 14, 2014
This is version 53 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