ID   KDTA_RICTY              Reviewed;         462 AA.
AC   Q68XV7;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 93.
DE   RecName: Full=3-deoxy-D-manno-octulosonic acid transferase;
DE            Short=Kdo transferase;
DE            EC=2.4.99.12;
DE   AltName: Full=Lipid IV(A) 3-deoxy-D-manno-octulosonic acid transferase;
GN   Name=waaA; Synonyms=kdtA; OrderedLocusNames=RT0048;
OS   Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=257363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA   McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA   Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA   Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT   of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
CC   -!- FUNCTION: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes
CC       the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP-
CC       Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate
CC       precursor of lipid A. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CMP-3-deoxy-beta-D-manno-octulosonate + lipid IVA (E. coli) =
CC         alpha-Kdo-(2->6)-lipid IVA (E. coli) + CMP + H(+);
CC         Xref=Rhea:RHEA:28066, ChEBI:CHEBI:15378, ChEBI:CHEBI:58603,
CC         ChEBI:CHEBI:60364, ChEBI:CHEBI:60377, ChEBI:CHEBI:85987;
CC         EC=2.4.99.12;
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Single-pass
CC       membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC       {ECO:0000305}.
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DR   EMBL; AE017197; AAU03535.1; -; Genomic_DNA.
DR   RefSeq; WP_011190522.1; NC_006142.1.
DR   AlphaFoldDB; Q68XV7; -.
DR   SMR; Q68XV7; -.
DR   CAZy; GT30; Glycosyltransferase Family 30.
DR   KEGG; rty:RT0048; -.
DR   eggNOG; COG1519; Bacteria.
DR   HOGENOM; CLU_036146_2_0_5; -.
DR   OrthoDB; 9789797at2; -.
DR   UniPathway; UPA00958; -.
DR   Proteomes; UP000000604; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043842; F:Kdo transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.11720; 3-Deoxy-D-manno-octulosonic-acid transferase, N-terminal domain; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1.
DR   InterPro; IPR007507; Glycos_transf_N.
DR   InterPro; IPR038107; Glycos_transf_N_sf.
DR   InterPro; IPR039901; Kdotransferase.
DR   PANTHER; PTHR42755:SF1; 3-DEOXY-D-MANNO-OCTULOSONIC ACID TRANSFERASE, MITOCHONDRIAL-RELATED; 1.
DR   PANTHER; PTHR42755; 3-DEOXY-MANNO-OCTULOSONATE CYTIDYLYLTRANSFERASE; 1.
DR   Pfam; PF04413; Glycos_transf_N; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Lipopolysaccharide biosynthesis;
KW   Membrane; Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..462
FT                   /note="3-deoxy-D-manno-octulosonic acid transferase"
FT                   /id="PRO_0000286457"
FT   TRANSMEM        2..22
FT                   /note="Helical; Signal-anchor"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          47..90
FT                   /note="RPE1 insert"
FT   ACT_SITE        104
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         308..309
FT                   /ligand="CMP"
FT                   /ligand_id="ChEBI:CHEBI:60377"
FT                   /evidence="ECO:0000250"
FT   BINDING         349..351
FT                   /ligand="CMP"
FT                   /ligand_id="ChEBI:CHEBI:60377"
FT                   /evidence="ECO:0000250"
FT   BINDING         374..377
FT                   /ligand="CMP"
FT                   /ligand_id="ChEBI:CHEBI:60377"
FT                   /evidence="ECO:0000250"
FT   SITE            174
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   SITE            249
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   462 AA;  52900 MW;  D23F37C837B00178 CRC64;
     MMLLYYILSF ILLPVYFIII FIRLLIGKED IRRIQERFAI GKQRQNSLLD LQMSVNQEGF
     KVDTEHKATS YVYIHRNASL MYKLSLERSY AQSLVWIHAA SVGEVMTSLT LIHNICKLAP
     NVRFLITSWT NTSAKILSTK LPKIATHQFL PIDNVIFTRK FLSNWKPDLG IFIESELWPC
     IINEGAKHCK LLLVNARISN KSFKTWLKRK KFFQLIIKNF SKIIVQSECD LQKFNALGIS
     DAMNLGNIKF ANEKLLVNQE KLSKLSLHLD NRRVVVFAST HPEDEEVILP IINNLKEQFV
     DCYIILIPRH PERVKSILNN CKCHNLLATA KSQNDLPVLS DDIYIVDRFG EMGLFFSVAT
     ISFIGGSFKQ GGHNILEAAY FSNCIIFGPD MSKNTDIAKG ILQNNAAIQI KNGEDLLNTL
     KSLLNANNAL KLKAYRENAL KFVEHNQKIL DEYLHVIKPF LP
//