ID   LPXB_METFK              Reviewed;         378 AA.
AC   Q1H152;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=Mfla_1517;
OS   Methylobacillus flagellatus (strain KT / ATCC 51484 / DSM 6875).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Methylophilaceae; Methylobacillus.
OX   NCBI_TaxID=265072;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KT / ATCC 51484 / DSM 6875;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Anderson I., Richardson P.;
RT   "Complete sequence of Methylobacillus flagellatus KT.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000284; ABE49785.1; -; Genomic_DNA.
DR   RefSeq; WP_011479739.1; NC_007947.1.
DR   AlphaFoldDB; Q1H152; -.
DR   SMR; Q1H152; -.
DR   STRING; 265072.Mfla_1517; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   PRIDE; Q1H152; -.
DR   EnsemblBacteria; ABE49785; ABE49785; Mfla_1517.
DR   KEGG; mfa:Mfla_1517; -.
DR   eggNOG; COG0763; Bacteria.
DR   HOGENOM; CLU_036577_3_0_4; -.
DR   OMA; PTVWAWR; -.
DR   OrthoDB; 1258510at2; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000002440; 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..378
FT                   /note="Lipid-A-disaccharide synthase"
FT                   /id="PRO_0000255198"
SQ   SEQUENCE   378 AA;  42525 MW;  3DECB4CCF6E36D31 CRC64;
     MPTIGIVAGE ASGDLLGSHL IRALKKQRPD LKFVGIAGPK MIAEGAETLF PMERLSVRGY
     VEVLRHLPGL LKIRKEVAQY FLDHRPDVFI GIDAPDFNFT LERKLKHQGI PTVHYVSPSI
     WAWRRGKIKK IQQAVSHMLA LFPFEPEIYR QAGVAVSYVG HPLADMLPME PDMEGAREEL
     KLPQDSLVVA MLPGSRQSEV QQLADLYIKT AKLILSERPD ARFLVPLITR ETRAIFERAL
     YANEGYDLPV SIMFGHAHQA MEAANAVIVA SGTATLEAAL IKRPMIITYR MPNLSWQILK
     RMKYLPYVGL PNVLAGRFIV PELLQHDAVP DKLAATLLQM LSDKSQIADI QTEFRRMHEL
     LRQNTEEKAA RAVLSFIK