ID   LPXB_CHLTR              Reviewed;         607 AA.
AC   O84416;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Lipid-A-disaccharide synthase;
DE            EC=2.4.1.182;
GN   Name=lpxB; OrderedLocusNames=CT_411;
OS   Chlamydia trachomatis (strain D/UW-3/Cx).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=272561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D/UW-3/Cx;
RX   PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA   Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA   Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT   "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT   trachomatis.";
RL   Science 282:754-759(1998).
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. {ECO:0000250}.
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;
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the LpxB family.
CC       {ECO:0000305}.
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DR   EMBL; AE001273; AAC68008.1; -; Genomic_DNA.
DR   PIR; E71518; E71518.
DR   RefSeq; NP_219921.1; NC_000117.1.
DR   RefSeq; WP_009871763.1; NC_000117.1.
DR   AlphaFoldDB; O84416; -.
DR   SMR; O84416; -.
DR   STRING; 813.O172_02230; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   EnsemblBacteria; AAC68008; AAC68008; CT_411.
DR   GeneID; 884705; -.
DR   KEGG; ctr:CT_411; -.
DR   PATRIC; fig|272561.5.peg.442; -.
DR   HOGENOM; CLU_430672_0_0_0; -.
DR   InParanoid; O84416; -.
DR   OMA; KIIHYVC; -.
DR   BRENDA; 2.4.1.182; 1315.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000000431; Chromosome.
DR   GO; GO:0008915; F:lipid-A-disaccharide synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR   GO; GO:0009245; P:lipid A biosynthetic process; IBA:GO_Central.
DR   HAMAP; MF_00392; LpxB; 1.
DR   InterPro; IPR003835; Glyco_trans_19.
DR   InterPro; IPR011499; Lipid_A_biosynth_N.
DR   PANTHER; PTHR30372; PTHR30372; 1.
DR   Pfam; PF07578; LAB_N; 2.
DR   Pfam; PF02684; LpxB; 1.
DR   SMART; SM01259; LAB_N; 2.
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..607
FT                   /note="Lipid-A-disaccharide synthase"
FT                   /id="PRO_0000190161"
FT   REGION          1..224
FT                   /note="Unknown"
FT   REGION          225..607
FT                   /note="Lipid-A-disaccharide synthase"
SQ   SEQUENCE   607 AA;  69030 MW;  8DF4430905BD6991 CRC64;
     MFPQKITLWL YPLGLFANLF FGTAFCVQWS LTRKKGYSVV PKIFWYLSGT GAVFMICHGF
     IQSQYPIALL HSFNLIIYFR NLNIASLNPL PVSKIASLLV SVATAITVSF AIGTRYLPHM
     TWMASPNILH LNLPEASLSW QLIGCIGLTI FSLRFFIQWF YLEYKNQSAL PAPFWKASLL
     GGSICLLYFL RTGDLVNVLC YGCGLFPSLA NLRIASREAF RKPFSNSCFI SAGEHSGDTL
     GGNLLKEMHA KYPDIHCFGV GGPQMRAQNF HALFAMEKFQ VSGFWEVLLA LPKLWYRYQL
     LYRNILKTNP RTVICIDFPD FHFLLIKKLR SRGYKGKIVH YVCPSIWAWR PSRKTVLEKY
     LDLLLLILPF EQNLFKDSAL RTVYLGHPLS ETIKSFSPNL NWKDQLHLPT DKPFIAAFPG
     SRRSDILRNL TIQVQAFQAS SLASTHHLLV SSANPEYDHL ILEVLQQNRC LHSHIVPSQF
     RYELMRECDF ALAKCGTIVL ETALNLTPTI VTCQLRPLDT FLAKYIFNII LPAYSLPNII
     LGRTIFPEFI GGKKDFQYED VAAALNILKT SQAQEKQKDS CRDVYQAINE SASSMKECLS
     LIFETAS