ID   LPXB_SYNAS              Reviewed;         383 AA.
AC   Q2LVL8;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2006, sequence version 1.
DT   25-MAY-2022, entry version 75.
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=SYNAS_22450;
GN   ORFNames=SYN_01565;
OS   Syntrophus aciditrophicus (strain SB).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophales; Syntrophaceae;
OC   Syntrophus.
OX   NCBI_TaxID=56780;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB;
RX   PubMed=17442750; DOI=10.1073/pnas.0610456104;
RA   McInerney M.J., Rohlin L., Mouttaki H., Kim U., Krupp R.S.,
RA   Rios-Hernandez L., Sieber J., Struchtemeyer C.G., Bhattacharyya A.,
RA   Campbell J.W., Gunsalus R.P.;
RT   "The genome of Syntrophus aciditrophicus: life at the thermodynamic limit
RT   of microbial growth.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:7600-7605(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; CP000252; ABC78124.1; -; Genomic_DNA.
DR   RefSeq; WP_011418144.1; NC_007759.1.
DR   AlphaFoldDB; Q2LVL8; -.
DR   SMR; Q2LVL8; -.
DR   STRING; 56780.SYN_01565; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   EnsemblBacteria; ABC78124; ABC78124; SYN_01565.
DR   KEGG; sat:SYN_01565; -.
DR   eggNOG; COG0763; Bacteria.
DR   HOGENOM; CLU_036577_3_1_7; -.
DR   OMA; PTVWAWR; -.
DR   OrthoDB; 1258510at2; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000001933; 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..383
FT                   /note="Lipid-A-disaccharide synthase"
FT                   /id="PRO_0000255228"
SQ   SEQUENCE   383 AA;  41277 MW;  6086447ADAB7F983 CRC64;
     MNSKLVLIVA GEASGDLHGA SLVGAMVKRE PGIRFYGIGG VNLKTAGVDL WADAADMAVV
     GLTEVASKLR GILTVMHRLK KSMQLLKPDL VILIDYPDFN LPLARSAKKN GIPVFYYISP
     QVWAWRKGRL RTISGLVDRM AVILPFEEPL YRQAGVDVSF VGHPLLDVVQ ATSSRDETLR
     MFGLREDVTT VALLPGSRKG EVTRLLPVML KAARILTENI CPVQFLLPMA NTLDETWMKD
     QIAKADPPGV RLIRGATYDA VAAADAAVVV SGTATLETAL LGTPLIVIYK VSALSYLIGR
     MLISVDHIGL VNIVAGKTVA PELIQGAANP ERIAAEILAI LGQPDRRKAI QEELSHLRDK
     LGLPGAAERA AVMALTLIKK SDC