ID   LPXB_PROMM              Reviewed;         392 AA.
AC   Q7V5X6;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 88.
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=PMT_1409;
OS   Prochlorococcus marinus (strain MIT 9313).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=74547;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9313;
RX   PubMed=12917642; DOI=10.1038/nature01947;
RA   Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA   Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA   Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA   Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA   Chisholm S.W.;
RT   "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT   differentiation.";
RL   Nature 424:1042-1047(2003).
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; BX548175; CAE21584.1; -; Genomic_DNA.
DR   RefSeq; WP_011130777.1; NC_005071.1.
DR   AlphaFoldDB; Q7V5X6; -.
DR   SMR; Q7V5X6; -.
DR   STRING; 74547.PMT_1409; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   EnsemblBacteria; CAE21584; CAE21584; PMT_1409.
DR   KEGG; pmt:PMT_1409; -.
DR   eggNOG; COG0763; Bacteria.
DR   HOGENOM; CLU_036577_3_0_3; -.
DR   OMA; PTVWAWR; -.
DR   OrthoDB; 1258510at2; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000001423; 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..392
FT                   /note="Lipid-A-disaccharide synthase"
FT                   /id="PRO_0000190176"
SQ   SEQUENCE   392 AA;  43534 MW;  19C05F7DC3E23062 CRC64;
     MVRLLISTGE VSGDLQGSLL IQALQREVER RSLPLELMAL GGPRMQASGA ELLADTAPMG
     AIGLWEALPL VLPTLRLQSR VDHVLKQRPP DAVVLIDYMG ANVRLGHKLR RWFPRVPIIY
     YIAPQEWAWR FGDGGTTQLL SFTDRILAIF PVEAEFYSQR GAKVTWVGHP LLDTVSVLPD
     RQQARERLGL KPGQRLLLLL PASRQQELRY LMPTLAKAAA LLQQRDQSLE VIVPAGLASF
     EKSLQEALEA AAVRGRVLSA QQADELKPML YAAADLALGK SGTVNMEMAL RGVPQVVGYK
     VSRITAFVAR HFLRFRVEHI SPVNLLLKER LVPELLQDEL TAEALVQAAI PLLEDPAQRN
     EMLEGYRRLR QTLGVPGVTD RAAKEILDLT KT