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Q255P5 (LPXB_CHLFF) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 49. 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:CF0221
OrganismChlamydophila felis (strain Fe/C-56) [Complete proteome] [HAMAP]
Taxonomic identifier264202 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydophila

Protein attributes

Sequence length625 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 – 625625Lipid-A-disaccharide synthase HAMAP-Rule MF_00392
PRO_0000255173

Regions

Region1 – 224224Unknown HAMAP-Rule MF_00392
Region225 – 625401Lipid-A-disaccharide synthase HAMAP-Rule MF_00392

Sequences

Sequence LengthMass (Da)Tools
Q255P5 [UniParc].

Last modified April 18, 2006. Version 1.
Checksum: 52845D7E03BE19D7

FASTA62571,007
        10         20         30         40         50         60 
MLPLHLVHVL YPIGLIANLF FGSAFTIQWF LSERRKKACV PKSFWILSSI GAVMMIAHGF 

        70         80         90        100        110        120 
IQSQFPIALL HGANLVIYFR NLNVSSSHSL SLRATLFILV VTLLLTTLPF VLGSYYYPNM 

       130        140        150        160        170        180 
QWMASPNIFH LPLPPPNIYW HIAGCIGLFT FSSRFFIQWC HLEINNRSTL PALFWLVSFI 

       190        200        210        220        230        240 
GGFLAFLYFI RTGDPVNIIS YGCGLLPSLA NLLIIYKKSR LPEFHNHSYF LSAGEPSGDI 

       250        260        270        280        290        300 
LGSDLLHNIK TCDPTIRCFG VGGPLMRKEG FEPLIHMEEF QVSGFLEVFF SIFGLFKKYR 

       310        320        330        340        350        360 
RLYKAILQEN PETVFCIDFP DFHFFLIKKL RKCGYKGKII HYVCPSIWAW RPKRKKILEK 

       370        380        390        400        410        420 
YLDTLLLILP FEKDLFINSP LKTIYLGHPL VKTISNFQYC SSWKQQLSIS DQPIVALFPG 

       430        440        450        460        470        480 
SRPGDIFRNL QVQIRAFLAS SLAQSHQILV SSCNPKYDKN ILDVLEKEGC RGKIISSTFR 

       490        500        510        520        530        540 
YQLMRDCDCA LAKCGTIVLE AALNQTPTIV TCLLGPIDTF LAKYIFKILM PAYSLPNIIT 

       550        560        570        580        590        600 
GSIIFPEFIG GKHDFNPEEV AAAIDILAKP KSKEKQKLAC QQLLDTLMTN VVTPEECLRI 

       610        620 
ICSQNSHLHL EKGILKNLHP RDSSV 

« Hide

References

[1]"Genome sequence of the cat pathogen, Chlamydophila felis."
Azuma Y., Hirakawa H., Yamashita A., Cai Y., Rahman M.A., Suzuki H., Mitaku S., Toh H., Goto S., Murakami T., Sugi K., Hayashi H., Fukushi H., Hattori M., Kuhara S., Shirai M.
DNA Res. 13:15-23(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Fe/C-56.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006861 Genomic DNA. Translation: BAE80993.1.
RefSeqYP_515138.1. NC_007899.1.

3D structure databases

ProteinModelPortalQ255P5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING264202.CF0221.

Protein family/group databases

CAZyGT19. Glycosyltransferase Family 19.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3958442.
KEGGcfe:CF0221.
PATRIC20204013. VBIChlFel51660_0229.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3952.
HOGENOMHOG000034725.
KOK00748.
OMAKIIHYVC.
OrthoDBEOG6FBWZR.

Enzyme and pathway databases

BioCycCFEL264202:GJCG-230-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]
ProtoNetSearch...

Entry information

Entry nameLPXB_CHLFF
AccessionPrimary (citable) accession number: Q255P5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: April 18, 2006
Last modified: May 14, 2014
This is version 49 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