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Q9PJY4 (LPXB_CHLMU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 78. 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:TC_0692
OrganismChlamydia muridarum (strain MoPn / Nigg) [Complete proteome] [HAMAP]
Taxonomic identifier243161 [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_0000190159

Regions

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

Sequences

Sequence LengthMass (Da)Tools
Q9PJY4 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: F794FD9B10FBB259

FASTA60769,198
        10         20         30         40         50         60 
MFPQKITLWL YPLGLFANLF FGTAFCVQWF LIKKRGCSFV PKIFWHLSCS GAVLMICHGF 

        70         80         90        100        110        120 
IQSQYPIALL HSFNLIIYFR NLNIASSTPL PISKIVSLLV VSATAITLSF AIGTQYLPHM 

       130        140        150        160        170        180 
TWMASPNILH LNLPEANFLW QLIGCIGLTI FSLRFFIQWF YLEYKNQSSL PTPFWKASLV 

       190        200        210        220        230        240 
GGSICLIYFL RTGDIVNVLC YGCGLFPSLA NLRIASREAI QKPFSCSCFI SAGEHSGDTL 

       250        260        270        280        290        300 
GGNLLKEIHA KYPDIHCFGV GGPQMRAQNF CTLFSMEKFQ ISGFWEVLLA LPKLWYRRRI 

       310        320        330        340        350        360 
LYKTILKRNP QAVICIDFPD FHFLLIKKLR SLGYKGKIVH YVCPSIWAWR PSRKTTLEKY 

       370        380        390        400        410        420 
LDLLLLILPF EQKLFKDSPL RTVYIGHPLS ETIKLFCPKQ NWKERLHLPT DKPFVAAFPG 

       430        440        450        460        470        480 
SRHSDILRNL TIQVQAFQAS DFASTHHLLV SSANPAYDHL ILEILQQNRC LHSNIVPSQF 

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

       550        560        570        580        590        600 
LGRTIFPEFI GGKKDFRYED VAAALNILKT SQAQEKQKNA CKDVYQAINE SASTIKECLP 


FIFEASY 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE002160 Genomic DNA. Translation: AAF39508.1.
PIRE81676.
RefSeqNP_297066.1. NC_002620.2.

3D structure databases

ProteinModelPortalQ9PJY4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243161.TC0692.

Protein family/group databases

CAZyGT19. Glycosyltransferase Family 19.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF39508; AAF39508; TC_0692.
GeneID1246053.
KEGGcmu:TC_0692.
PATRIC20372840. VBIChlMur19118_0732.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3952.
KOK00748.
OMAKIIHYVC.
OrthoDBEOG6FBWZR.
ProtClustDBPRK01021.

Enzyme and pathway databases

BioCycCMUR243161:GHYU-715-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_CHLMU
AccessionPrimary (citable) accession number: Q9PJY4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: October 1, 2000
Last modified: February 19, 2014
This is version 78 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