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Database: UniProt
Entry: A0A3R5XZ64_9BACT
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ID   A0A3R5XZ64_9BACT        Unreviewed;       347 AA.
AC   A0A3R5XZ64;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=lipopolysaccharide heptosyltransferase II {ECO:0000256|ARBA:ARBA00044042};
DE            EC=2.4.99.24 {ECO:0000256|ARBA:ARBA00044042};
GN   Name=waaF {ECO:0000313|EMBL:QAR34304.1};
GN   ORFNames=EP073_13065 {ECO:0000313|EMBL:QAR34304.1};
OS   Geovibrio thiophilus.
OC   Bacteria; Deferribacterota; Deferribacteres; Deferribacterales;
OC   Geovibrionaceae; Geovibrio.
OX   NCBI_TaxID=139438 {ECO:0000313|EMBL:QAR34304.1, ECO:0000313|Proteomes:UP000287502};
RN   [1] {ECO:0000313|EMBL:QAR34304.1, ECO:0000313|Proteomes:UP000287502}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11263 {ECO:0000313|EMBL:QAR34304.1,
RC   ECO:0000313|Proteomes:UP000287502};
RA   Spring S., Bunk B., Sproer C.;
RT   "Geovibrio thiophilus DSM 11263, complete genome.";
RL   Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ADP-L-glycero-beta-D-manno-heptose + an L-alpha-D-Hep-(1->5)-
CC         [alpha-Kdo-(2->4)]-alpha-Kdo-(2->6)-lipid A = ADP + an L-alpha-D-Hep-
CC         (1->3)-L-alpha-D-Hep-(1->5)-[alpha-Kdo-(2->4)]-alpha-Kdo-(2->6)-lipid
CC         A + H(+); Xref=Rhea:RHEA:74071, ChEBI:CHEBI:15378, ChEBI:CHEBI:61506,
CC         ChEBI:CHEBI:193068, ChEBI:CHEBI:193069, ChEBI:CHEBI:456216;
CC         EC=2.4.99.24; Evidence={ECO:0000256|ARBA:ARBA00043830};
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 9 family.
CC       {ECO:0000256|ARBA:ARBA00043995}.
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DR   EMBL; CP035108; QAR34304.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3R5XZ64; -.
DR   KEGG; gtl:EP073_13065; -.
DR   OrthoDB; 9783989at2; -.
DR   Proteomes; UP000287502; Chromosome.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:InterPro.
DR   GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:InterPro.
DR   CDD; cd03789; GT9_LPS_heptosyltransferase; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   InterPro; IPR002201; Glyco_trans_9.
DR   InterPro; IPR011910; RfaF.
DR   NCBIfam; TIGR02195; heptsyl_trn_II; 1.
DR   PANTHER; PTHR30160:SF1; LIPOPOLYSACCHARIDE 1,2-N-ACETYLGLUCOSAMINETRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR30160; TETRAACYLDISACCHARIDE 4'-KINASE-RELATED; 1.
DR   Pfam; PF01075; Glyco_transf_9; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000287502};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:QAR34304.1}.
SQ   SEQUENCE   347 AA;  38214 MW;  59369B61C9135491 CRC64;
     MKGIFLKILV FNPSFLGDSV LTTPLIKAVR HYFPDSSVDF CVRPENAPLF QGMELINEVI
     VFDKRKSAGG AGGIFRFARE LKKRDYDIII SCHKSFRSTL TMALTGVLRR MGFRQSALSF
     LYTETADRDM SKHEAERNLM LLEPLVADFD LEDAKKHAGR AEVFTDERLR ANAAKYIKSA
     SGGRRLIGIN AGSVWATKKW QSEKFAEVSD MLYEEGFFCV LFGAPTDSEA CGQVMANAKR
     PLMNLCGKLP LGQLPSYIKA MDALITNDSG PLHIASAVGT PAVAIFGPTV KALGFFPYDD
     KSIVVEKELY CRPCGLHGGN ECPEGHFRCM GEISAGDVFE AVGKVLK
//
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