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Q9Z6U3 (LPXB_CHLPN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 88. 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:CPn_0965, CP_0895, CpB1002
OrganismChlamydia pneumoniae (Chlamydophila pneumoniae) [Complete proteome] [HAMAP]
Taxonomic identifier83558 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia

Protein attributes

Sequence length604 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 – 604604Lipid-A-disaccharide synthase HAMAP-Rule MF_00392
PRO_0000190160

Regions

Region1 – 220220Unknown HAMAP-Rule MF_00392
Region221 – 604384Lipid-A-disaccharide synthase HAMAP-Rule MF_00392

Sequences

Sequence LengthMass (Da)Tools
Q9Z6U3 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 094BF1B7013E07C8

FASTA60469,014
        10         20         30         40         50         60 
MIPSGLVYLL YPLGFLASLF FGSAFSIQWW LSKKRKEVYA PRSFWILSSI GATLMIVHGT 

        70         80         90        100        110        120 
IQSQFPVTVL HVINLIIYLR NLNITSSRPI SFRATLVLMA LSVVFVTLPF LYVNMEWMAS 

       130        140        150        160        170        180 
PNIFHLPLPP AQLSWHLIGC LGLAIFSGRF LIQWFYIESN NTKDFPLLFW KIGLLGGLLA 

       190        200        210        220        230        240 
LVYFIRIGDP INILCYGCGL FPSIANLRLF YKEQRSTPYL DTHCFLSAGE ASGDILGGKL 

       250        260        270        280        290        300 
IQSIKSLYPN IRFWGVGGPA MRQEGLQPIL NMEEFQVSGF AEVLGSLFRL YRNYRKILKT 

       310        320        330        340        350        360 
ILKHKPATLI FIDFPDFHLL LIKKLRKHGY RGKIIHYVCP SIWAWRPKRK RILEQHLDML 

       370        380        390        400        410        420 
LLILPFEEGL FKNTSLETVY LGHPLVEEIS DYKEQASWKE KFLNSDRPIV AAFPGSRRGD 

       430        440        450        460        470        480 
ISRNLRIQVQ AFLNSSLSQT HQFVVSSSSA KYDEIIEDTL KAEGCQHSQI IPMNFRYELM 

       490        500        510        520        530        540 
RSCDCALAKC GTIVLETALN QTPTIVMCRL RPFDTFLAKY IFKILLPAYS LPNIIMNSVI 

       550        560        570        580        590        600 
FPEFIGGKKD FHPEEIATAL DLLNQHGSKE KQKEDCRKLC KVMTTGQIAS EEFLKRIFDT 


LPAV 

« Hide

References

[1]"Comparative genomes of Chlamydia pneumoniae and C. trachomatis."
Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W., Olinger L., Grimwood J., Davis R.W., Stephens R.S.
Nat. Genet. 21:385-389(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CWL029.
[2]"Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae AR39."
Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J., Gwinn M.L. expand/collapse author list , Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G., Salzberg S.L., Eisen J.A., Fraser C.M.
Nucleic Acids Res. 28:1397-1406(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AR39.
[3]"Comparison of whole genome sequences of Chlamydia pneumoniae J138 from Japan and CWL029 from USA."
Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K., Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.
Nucleic Acids Res. 28:2311-2314(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: J138.
[4]"The genome sequence of Chlamydia pneumoniae TW183 and comparison with other Chlamydia strains based on whole genome sequence analysis."
Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P., Schneider S., Pohl T., Essig A., Marre R., Melchers K.
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TW-183.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE001363 Genomic DNA. Translation: AAD19101.1.
AE002161 Genomic DNA. Translation: AAF38682.1.
BA000008 Genomic DNA. Translation: BAA99173.1.
AE009440 Genomic DNA. Translation: AAP98931.1.
PIRB72014.
C86611.
RefSeqNP_225158.1. NC_000922.1.
NP_301022.1. NC_002491.1.
NP_445433.1. NC_002179.2.
NP_877274.1. NC_005043.1.

3D structure databases

ProteinModelPortalQ9Z6U3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING115713.CPn0965.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD19101; AAD19101; CPn_0965.
AAF38682; AAF38682; CP_0895.
AAP98931; AAP98931; CpB1002.
BAA99173; BAA99173; BAA99173.
GeneID1467681.
895627.
919726.
963352.
KEGGcpa:CP0895.
cpj:CPj0965.
cpn:CPn0965.
cpt:CpB1002.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3952.
HOGENOMHOG000034725.
KOK00748.
OMAKIIHYVC.
OrthoDBEOG6FBWZR.
ProtClustDBPRK01021.

Enzyme and pathway databases

BioCycCPNE115711:GI7B-924-MONOMER.
CPNE115713:GHEY-1007-MONOMER.
CPNE138677:GH8N-999-MONOMER.
CPNE182082:GH4N-1035-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_CHLPN
AccessionPrimary (citable) accession number: Q9Z6U3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: May 1, 1999
Last modified: February 19, 2014
This is version 88 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