ID   LPXB_PROM3              Reviewed;         392 AA.
AC   A2C745;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 76.
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=P9303_05531;
OS   Prochlorococcus marinus (strain MIT 9303).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=59922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9303;
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
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; CP000554; ABM77305.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2C745; -.
DR   SMR; A2C745; -.
DR   STRING; 59922.P9303_05531; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   EnsemblBacteria; ABM77305; ABM77305; P9303_05531.
DR   KEGG; pmf:P9303_05531; -.
DR   HOGENOM; CLU_036577_3_0_3; -.
DR   OMA; PTVWAWR; -.
DR   BioCyc; PMAR59922:G1G80-509-MON; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000002274; 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; Transferase.
FT   CHAIN           1..392
FT                   /note="Lipid-A-disaccharide synthase"
FT                   /id="PRO_1000049406"
SQ   SEQUENCE   392 AA;  43485 MW;  30F2DD5364FBC44A CRC64;
     MVRLLISTGE VSGDLQGSLL IQALQREVER RSLPLELMAL GGPRMQASGA ELLADTAPMG
     AIGLWEALPL VLPTLRLQSR VDHVLKQRPP DAVVLIDYMG ANVRLGHKLR RWFPRVPIIY
     YIAPQEWAWR FGDGGTTQLL SFTDRILAIF PVEAEFYAQR GAKVTWVGHP LLDTVSVLPD
     RQLARERLGL KSGQRLLLLL PASRQQELRY LMPTLAKAAA LLQQRDPSLE VIVPAGLASF
     ETSLQKALEA AAVRGRVLSA QQADELKPML YAAADLALGK SGTVNMELAL RGVPQVVGYK
     VSRITAFVAR HFLRFRVDHI SPVNLLLKER LVPELLQDEF TAEALVQAAI PLLEDPAQRH
     EMLEGYWRLR QTLGVPGVTD RAAKEILDLT KP