ID G5H0U6_9FIRM Unreviewed; 846 AA.
AC G5H0U6;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Tetraacyldisaccharide 4'-kinase {ECO:0000256|HAMAP-Rule:MF_00409};
DE EC=2.7.1.130 {ECO:0000256|HAMAP-Rule:MF_00409};
DE AltName: Full=Lipid A 4'-kinase {ECO:0000256|HAMAP-Rule:MF_00409};
GN Name=lpxK {ECO:0000256|HAMAP-Rule:MF_00409};
GN ORFNames=HMPREF9432_00364 {ECO:0000313|EMBL:EHG25863.1};
OS Selenomonas noxia F0398.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Selenomonas.
OX NCBI_TaxID=702437 {ECO:0000313|EMBL:EHG25863.1, ECO:0000313|Proteomes:UP000003175};
RN [1] {ECO:0000313|EMBL:EHG25863.1, ECO:0000313|Proteomes:UP000003175}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0398 {ECO:0000313|EMBL:EHG25863.1,
RC ECO:0000313|Proteomes:UP000003175};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Ganesan A.,
RA Blanton J.M., Baranova O.V., Tanner A.C., Dewhirst F.E., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Selenomonas noxia F0398.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transfers the gamma-phosphate of ATP to the 4'-position of a
CC tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form
CC tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
CC {ECO:0000256|HAMAP-Rule:MF_00409}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+);
CC Xref=Rhea:RHEA:67840, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:176343, ChEBI:CHEBI:176425, ChEBI:CHEBI:456216;
CC EC=2.7.1.130; Evidence={ECO:0000256|HAMAP-Rule:MF_00409};
CC -!- PATHWAY: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A)
CC from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-
CC acetyl-alpha-D-glucosamine: step 6/6. {ECO:0000256|HAMAP-
CC Rule:MF_00409}.
CC -!- SIMILARITY: Belongs to the LpxK family. {ECO:0000256|HAMAP-
CC Rule:MF_00409}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHG25863.1}.
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DR EMBL; ADGH01000003; EHG25863.1; -; Genomic_DNA.
DR RefSeq; WP_006695853.1; NZ_JH376857.1.
DR AlphaFoldDB; G5H0U6; -.
DR STRING; 702437.HMPREF9432_00364; -.
DR GeneID; 84786553; -.
DR PATRIC; fig|702437.3.peg.376; -.
DR eggNOG; COG1519; Bacteria.
DR eggNOG; COG1663; Bacteria.
DR HOGENOM; CLU_019506_0_0_9; -.
DR UniPathway; UPA00359; UER00482.
DR Proteomes; UP000003175; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009029; F:tetraacyldisaccharide 4'-kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 HAMAP; MF_00409; LpxK; 1.
DR InterPro; IPR007507; Glycos_transf_N.
DR InterPro; IPR038107; Glycos_transf_N_sf.
DR InterPro; IPR039901; Kdotransferase.
DR InterPro; IPR003758; LpxK.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR00682; lpxK; 1.
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.
DR Pfam; PF02606; LpxK; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00409};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_00409};
KW Lipid A biosynthesis {ECO:0000256|HAMAP-Rule:MF_00409};
KW Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00409};
KW Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_00409};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00409};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00409}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 33..215
FT /note="3-deoxy-D-manno-octulosonic-acid transferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF04413"
FT ACT_SITE 64
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR639901-1"
FT BINDING 520..527
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00409"
FT SITE 134
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR639901-2"
FT SITE 212
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR639901-2"
SQ SEQUENCE 846 AA; 94630 MW; 2263473CF0698AF8 CRC64;
MRFLYNLAAI LIVTIIIPIF MLRATRERGF VERIKQSFGF YPQETIDKVA GKNAIWVHAA
SVGEIVATSP LVREFRKAFP DSPILVSVVT TGGYEMAHRI IKDADAIIYF PLDLPFLASR
VVGRIRPRVF LPVETELWPN FLKKAKQLDV PVMMVNGRIS DRSVKQYKYL FGMLREMIGT
VKCFAMQSSI DADYIMRLGA PRELVTVTGN TKFDQAYTSV SPEERAALIK ELGLEGASRI
MIAGSTHRGE EELVLAAFAA VRAKDPNVRL IIAPREVLRT MEVEHLCRKA GFTVNTRKNL
QKGAAGGEDI VVLDTVGELG RVYGLGDVIY IGGSLIPHGG HNILEPAAHG KAIIVGSQMF
NFKDIHALFR NRNAVVTVTS GAELTRETLR LFGDDAERQR LERETLAIIN ENKGASKKSA
QILVDMLAAY EARRALRAQQ RISNHRVQAT QKVANFQTYF IDLVHDKEVR GVSRRLIMAI
FYGFSLIYEQ LVNLKLTMYR WGWVKKEQLD CFVISLGNVT VGGTGKTPTA QHLARAIHEM
GYRVAILNRG YRAKWRGDVG IVSDGRALKM DAETAGDEAF MLAKHLPNVP VLIGPKRAVT
GRYAIEHFGA EVAILDDGYQ HWQLERDMDI LLVDAVNVFG NGYLLPRGTL REPLSHIDRA
DVCLMTKVDQ AAPGAIPYIW ETFRSYNQDG LIIESIHQPR QFVRLSHWYE DIGAGGIPAT
EMEGKKVLAV SAIGNPASFE QTLTDLGVEM VESMRYPDHH DYGERDMAEV LYRAETLGVE
AIVITEKDAV KVPGDVVRAK WRVPIYVISV EVTFQKGREE FFRTLKEQLA AKLGNGRHMP
QEADVV
//
