ID   LPXB_CHLFF              Reviewed;         625 AA.
AC   Q255P5;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Lipid-A-disaccharide synthase;
DE            EC=2.4.1.182;
GN   Name=lpxB; OrderedLocusNames=CF0221;
OS   Chlamydia felis (strain Fe/C-56) (Chlamydophila felis).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=264202;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fe/C-56;
RX   PubMed=16766509; DOI=10.1093/dnares/dsi027;
RA   Azuma Y., Hirakawa H., Yamashita A., Cai Y., Rahman M.A., Suzuki H.,
RA   Mitaku S., Toh H., Goto S., Murakami T., Sugi K., Hayashi H., Fukushi H.,
RA   Hattori M., Kuhara S., Shirai M.;
RT   "Genome sequence of the cat pathogen, Chlamydophila felis.";
RL   DNA Res. 13:15-23(2006).
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; AP006861; BAE80993.1; -; Genomic_DNA.
DR   RefSeq; WP_011457775.1; NC_007899.1.
DR   AlphaFoldDB; Q255P5; -.
DR   SMR; Q255P5; -.
DR   STRING; 264202.CF0221; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   KEGG; cfe:CF0221; -.
DR   eggNOG; COG0763; Bacteria.
DR   eggNOG; COG3952; Bacteria.
DR   HOGENOM; CLU_430672_0_0_0; -.
DR   OMA; KIIHYVC; -.
DR   OrthoDB; 149100at2; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000001260; 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   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.
PE   3: Inferred from homology;
KW   Glycosyltransferase; Lipid A biosynthesis; Lipid biosynthesis;
KW   Lipid metabolism; Transferase.
FT   CHAIN           1..625
FT                   /note="Lipid-A-disaccharide synthase"
FT                   /id="PRO_0000255173"
FT   REGION          1..224
FT                   /note="Unknown"
FT   REGION          225..625
FT                   /note="Lipid-A-disaccharide synthase"
SQ   SEQUENCE   625 AA;  71007 MW;  52845D7E03BE19D7 CRC64;
     MLPLHLVHVL YPIGLIANLF FGSAFTIQWF LSERRKKACV PKSFWILSSI GAVMMIAHGF
     IQSQFPIALL HGANLVIYFR NLNVSSSHSL SLRATLFILV VTLLLTTLPF VLGSYYYPNM
     QWMASPNIFH LPLPPPNIYW HIAGCIGLFT FSSRFFIQWC HLEINNRSTL PALFWLVSFI
     GGFLAFLYFI RTGDPVNIIS YGCGLLPSLA NLLIIYKKSR LPEFHNHSYF LSAGEPSGDI
     LGSDLLHNIK TCDPTIRCFG VGGPLMRKEG FEPLIHMEEF QVSGFLEVFF SIFGLFKKYR
     RLYKAILQEN PETVFCIDFP DFHFFLIKKL RKCGYKGKII HYVCPSIWAW RPKRKKILEK
     YLDTLLLILP FEKDLFINSP LKTIYLGHPL VKTISNFQYC SSWKQQLSIS DQPIVALFPG
     SRPGDIFRNL QVQIRAFLAS SLAQSHQILV SSCNPKYDKN ILDVLEKEGC RGKIISSTFR
     YQLMRDCDCA LAKCGTIVLE AALNQTPTIV TCLLGPIDTF LAKYIFKILM PAYSLPNIIT
     GSIIFPEFIG GKHDFNPEEV AAAIDILAKP KSKEKQKLAC QQLLDTLMTN VVTPEECLRI
     ICSQNSHLHL EKGILKNLHP RDSSV