KDTA_RICTY
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 03-AUG-2022, entry version 88.
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; Proteobacteria; 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 + CMP + H(+); Xref=Rhea:RHEA:28066,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58603, ChEBI:CHEBI:60364,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:85987; 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 STRING; 257363.RT0048; -.
DR CAZy; GT30; Glycosyltransferase Family 30.
DR EnsemblBacteria; AAU03535; AAU03535; RT0048.
DR KEGG; rty:RT0048; -.
DR eggNOG; COG1519; Bacteria.
DR HOGENOM; CLU_036146_2_0_5; -.
DR OMA; FIKYEFW; -.
DR OrthoDB; 1163086at2; -.
DR UniPathway; UPA00958; -.
DR Proteomes; UP000000604; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; -; 1.
DR InterPro; IPR007507; Glycos_transf_N.
DR InterPro; IPR038107; Glycos_transf_N_sf.
DR InterPro; IPR039901; Kdotransferase.
DR PANTHER; PTHR42755; PTHR42755; 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
