LPXB_CHRSD
ID LPXB_CHRSD Reviewed; 386 AA.
AC Q1R020;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 25-MAY-2022, entry version 92.
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=Csal_0576;
OS Chromohalobacter salexigens (strain ATCC BAA-138 / DSM 3043 / CIP 106854 /
OS NCIMB 13768 / 1H11).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Chromohalobacter.
OX NCBI_TaxID=290398;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-138 / DSM 3043 / CIP 106854 / NCIMB 13768 / 1H11;
RX PubMed=22675587; DOI=10.4056/sigs.2285059;
RA Copeland A., O'Connor K., Lucas S., Lapidus A., Berry K.W., Detter J.C.,
RA Del Rio T.G., Hammon N., Dalin E., Tice H., Pitluck S., Bruce D.,
RA Goodwin L., Han C., Tapia R., Saunders E., Schmutz J., Brettin T.,
RA Larimer F., Land M., Hauser L., Vargas C., Nieto J.J., Kyrpides N.C.,
RA Ivanova N., Goker M., Klenk H.P., Csonka L.N., Woyke T.;
RT "Complete genome sequence of the halophilic and highly halotolerant
RT Chromohalobacter salexigens type strain (1H11(T)).";
RL Stand. Genomic Sci. 5:379-388(2011).
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; CP000285; ABE57938.1; -; Genomic_DNA.
DR RefSeq; WP_011505884.1; NC_007963.1.
DR AlphaFoldDB; Q1R020; -.
DR SMR; Q1R020; -.
DR STRING; 290398.Csal_0576; -.
DR CAZy; GT19; Glycosyltransferase Family 19.
DR EnsemblBacteria; ABE57938; ABE57938; Csal_0576.
DR KEGG; csa:Csal_0576; -.
DR eggNOG; COG0763; Bacteria.
DR HOGENOM; CLU_036577_3_0_6; -.
DR OMA; PTVWAWR; -.
DR OrthoDB; 1258510at2; -.
DR UniPathway; UPA00973; -.
DR Proteomes; UP000000239; 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..386
FT /note="Lipid-A-disaccharide synthase"
FT /id="PRO_0000255174"
SQ SEQUENCE 386 AA; 42361 MW; DE844FE223171A53 CRC64;
MRIYLVAGEL SGDILGAGLM QALKRRHPDA EFRGIGGPRM LAEGMQSLYP LETLSVMGLV
EVLKHLPGLI KVRRHLRRDA LAWQPDVMIG IDAPDFNLGL ERQLRATGMR TVHYVSPSVW
AWRQGRVKTI ARSVDAMLTF LPFEAAFYAR HQVPVAFVGH PLADELPLVN DRQAARTALG
LSSTAPLLAV LPGSRGNEIR FLGPTFLDSA VWLRERVPGL QVVIPAASPA RRQELEVLLA
THPAREFVHL RDGESRQAMT AADAVLLASG TAALEAMLCH RPMVVAYKMA AATHWLAKRM
VKTEWISLPN LIAQETLVPE LVQEDASCEA IGEALLTWLG DETHRQATET RFAALHATLQ
RGASERAAEA IDSLVVHGRL PEEPTA