Burkholderia cenocepacia J2315, BCAL3111 (kdoO)

Cytoplasmic
Cytoplasmic Membrane
Periplasmic
Outer Membrane
Extracellular
Unknown
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Gene Feature Overview

Strain Burkholderia cenocepacia J2315
GCF_000009485.1|latest
Locus Tag
BCAL3111
NCBI Locus TagQU43_RS52285
Name
kdoO
Synonym: wbxY
Replicon chromosome 1
Genomic location 3399895 - 3400779 (- strand)
CommentResponsible for Ko formation with Kdo2-lipid A as a substrate

Cross-References

RefSeq WP_006485119.1
GI 206561457
Entrez 6934235
GI 206561457
INSDC CAR53435.1
NCBI Locus Tag QU43_RS52285
NCBI Old Locus Tag BCAL3111
RefSeq WP_006485119.1,GeneID
UniParc UPI00017B994F
UniProtKB Acc B4ECD2
UniProtKB ID B4ECD2_BURCJ
UniRef100 UniRef100_B4ECD2
UniRef50 UniRef50_Q0WGC8
UniRef90 UniRef90_B4ECD2

Product

Feature Type CDS
Coding Frame 1
Product Name
Kdo 3-hydroxylase KdoO
Product Name Confidence: Class 2
Synonyms hypothetical protein
Evidence for Translation
Charge (pH 7) 3.59
Kyte-Doolittle Hydrophobicity Value -0.222
Molecular Weight (kDa) 32740.3
Isoelectric Point (pI) 8.48

Subcellular localization

Individual Mappings
Localization Confidence PMID
Cytoplasmic Class 3
Additional evidence for subcellular localization

Pathogen Association Analysis

Results
Common
Found in both pathogen and nonpathogenic strains
Hits to this gene were found in 28 genera

Orthologs/Comparative Genomics

Burkholderia Ortholog Group BG000751 (654 members)
Putative Inparalogs None Found

Interactions

STRING database Search for predicted protein-protein interactions using:
Search term: BCAL3111
Search term: kdoO

References

Reconstitution of O-specific lipopolysaccharide expression in Burkholderia cenocepacia strain J2315, which is associated with transmissible infections in patients with cystic fibrosis.
Ortega X, Hunt TA, Loutet S, Vinion-Dubiel AD, Datta A, Choudhury B, Goldberg JB, Carlson R, Valvano MA
J Bacteriol 2005 Feb;187(4):1324-33
PubMed ID: 15687196
The LpxL acyltransferase is required for normal growth and penta-acylation of lipid A in Burkholderia cenocepacia.
Fathy Mohamed Y, Hamad M, Ortega XP, Valvano MA
Mol Microbiol 2017 Apr;104(1):144-162
PubMed ID: 28085228
Dioxygenases in Burkholderia ambifaria and Yersinia pestis that hydroxylate the outer Kdo unit of lipopolysaccharide.
Chung HS, Raetz CR
Proc Natl Acad Sci U S A 2011 Jan 11;108(2):510-5
PubMed ID: 21178073
Kdo hydroxylase is an inner core assembly enzyme in the Ko-containing lipopolysaccharide biosynthesis.
Chung HS, Yang EG, Hwang D, Lee JE, Guan Z, Raetz CR
Biochem Biophys Res Commun 2014 Sep 26;452(3):789-94
PubMed ID: 25204504