LPXB_RUEPO
ID LPXB_RUEPO Reviewed; 401 AA.
AC Q5LSU1;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Lipid-A-disaccharide synthase {ECO:0000255|HAMAP-Rule:MF_00392};
DE EC=2.4.1.182 {ECO:0000255|HAMAP-Rule:MF_00392};
GN Name=lpxB {ECO:0000255|HAMAP-Rule:MF_00392}; OrderedLocusNames=SPO1675;
OS Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter
OS pomeroyi).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria.
OX NCBI_TaxID=246200;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX PubMed=15602564; DOI=10.1038/nature03170;
RA Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.M.,
RA Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., Sheldon W.M.,
RA Ye W., Miller T.R., Carlton J., Rasko D.A., Paulsen I.T., Ren Q.,
RA Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA Nelson W.C., Sullivan S.A., Rosovitz M.J., Haft D.H., Selengut J., Ward N.;
RT "Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine
RT environment.";
RL Nature 432:910-913(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA Rivers A.R., Smith C.B., Moran M.A.;
RT "An updated genome annotation for the model marine bacterium Ruegeria
RT pomeroyi DSS-3.";
RL Stand. Genomic Sci. 9:11-11(2014).
CC -!- FUNCTION: Condensation of UDP-2,3-diacylglucosamine and 2,3-
CC diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor
CC of lipid A, a phosphorylated glycolipid that anchors the
CC lipopolysaccharide to the outer membrane of the cell.
CC {ECO:0000255|HAMAP-Rule:MF_00392}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a lipid X + a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-
CC glucosamine = a lipid A disaccharide + H(+) + UDP;
CC Xref=Rhea:RHEA:67828, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:137748, ChEBI:CHEBI:176338, ChEBI:CHEBI:176343;
CC EC=2.4.1.182; Evidence={ECO:0000255|HAMAP-Rule:MF_00392};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00392}.
CC -!- SIMILARITY: Belongs to the LpxB family. {ECO:0000255|HAMAP-
CC Rule:MF_00392}.
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DR EMBL; CP000031; AAV94960.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5LSU1; -.
DR SMR; Q5LSU1; -.
DR STRING; 246200.SPO1675; -.
DR CAZy; GT19; Glycosyltransferase Family 19.
DR EnsemblBacteria; AAV94960; AAV94960; SPO1675.
DR KEGG; sil:SPO1675; -.
DR eggNOG; COG0763; Bacteria.
DR HOGENOM; CLU_036577_3_0_5; -.
DR OMA; PTVWAWR; -.
DR UniPathway; UPA00973; -.
DR Proteomes; UP000001023; Chromosome.
DR GO; GO:0008915; F:lipid-A-disaccharide synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00392; LpxB; 1.
DR InterPro; IPR003835; Glyco_trans_19.
DR PANTHER; PTHR30372; PTHR30372; 1.
DR Pfam; PF02684; LpxB; 1.
DR TIGRFAMs; TIGR00215; lpxB; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase; Lipid A biosynthesis; Lipid biosynthesis;
KW Lipid metabolism; Reference proteome; Transferase.
FT CHAIN 1..401
FT /note="Lipid-A-disaccharide synthase"
FT /id="PRO_0000255226"
SQ SEQUENCE 401 AA; 42664 MW; AAE8DB2FA164182D CRC64;
MRPAGPVPVC CRAGRLMRVF ILAGEPSGDR LGGALMAGLR QLCPDVQFDG VGGPAMESEG
LSSRFPMAEL SIMGLVEVLP KYFHLKRRIA ETAQAVLAMR PDVMITIDSP DFSLRVARLV
KDASDIRTVH YVAPSVWAWR PGRADKMAKV IDHVLALLPF EPPYMERAGM ECDFVGHPVV
TEPEATGADI AALRTELGLG AAPVLLALPG SRRGEVERLA PVFGAALRRF LPEHPDMRVV
VPVVPHVADQ VAQQVAEWPG APVLVDPRGL APAQAAMRKR AAFAAADLAL AASGTVSLEL
AAAGTPMVIA YKVNWLTQKI AERMVTIDTV TLVNLVSETR VVPECLGPAC TPENIAARLA
AVHADPAAQD AAMRLTMERL GRGGTPPGLR AAQAVLDRLP G