LPXK_VIBCH
ID LPXK_VIBCH Reviewed; 336 AA.
AC Q9KQX0;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Tetraacyldisaccharide 4'-kinase {ECO:0000255|HAMAP-Rule:MF_00409};
DE EC=2.7.1.130 {ECO:0000255|HAMAP-Rule:MF_00409};
DE AltName: Full=Lipid A 4'-kinase {ECO:0000255|HAMAP-Rule:MF_00409};
GN Name=lpxK {ECO:0000255|HAMAP-Rule:MF_00409}; OrderedLocusNames=VC_1877;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
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:0000255|HAMAP-Rule:MF_00409}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + {2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-
CC glucosaminyl}-(1->6)-{2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-
CC D-glucosaminyl phosphate} = ADP + {2-N,3-O-bis[(3R)-3-
CC hydroxytetradecanoyl]-4-O-phospho-beta-D-glucosaminyl}-(1->6)-{2-N,3-
CC O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate}.;
CC EC=2.7.1.130; Evidence={ECO:0000255|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:0000255|HAMAP-
CC Rule:MF_00409}.
CC -!- SIMILARITY: Belongs to the LpxK family. {ECO:0000255|HAMAP-
CC Rule:MF_00409}.
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DR EMBL; AE003852; AAF95025.1; -; Genomic_DNA.
DR PIR; C82146; C82146.
DR RefSeq; NP_231511.1; NC_002505.1.
DR AlphaFoldDB; Q9KQX0; -.
DR SMR; Q9KQX0; -.
DR STRING; 243277.VC_1877; -.
DR DNASU; 2613631; -.
DR EnsemblBacteria; AAF95025; AAF95025; VC_1877.
DR KEGG; vch:VC_1877; -.
DR PATRIC; fig|243277.26.peg.1793; -.
DR eggNOG; COG1663; Bacteria.
DR HOGENOM; CLU_038816_2_0_6; -.
DR OMA; MDDGFQN; -.
DR BioCyc; VCHO:VC1877-MON; -.
DR UniPathway; UPA00359; UER00482.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009029; F:tetraacyldisaccharide 4'-kinase activity; IBA:GO_Central.
DR GO; GO:0009245; P:lipid A biosynthetic process; IBA:GO_Central.
DR GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR HAMAP; MF_00409; LpxK; 1.
DR InterPro; IPR003758; LpxK.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR42724; PTHR42724; 1.
DR Pfam; PF02606; LpxK; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00682; lpxK; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Lipid A biosynthesis; Lipid biosynthesis;
KW Lipid metabolism; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..336
FT /note="Tetraacyldisaccharide 4'-kinase"
FT /id="PRO_0000190953"
FT BINDING 60..67
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00409"
SQ SEQUENCE 336 AA; 37128 MW; 79AF426B94022647 CRC64;
MVIEKIWFHR HPLGYLLWPL LWPFSVLFGV ISRSRRKAYQ TGDKPSYRAP LPVVVVGNIT
AGGNGKTPVV VWLVETLQNL GYRPGVVSRG YGAKAPSYPL VVNEQTPAQH CGDEPKLIFQ
RTKAPVAVDP VRSQAVKALL EHGVNVIVTD DGLQHYALQR DIEIAVVDGV RRFGNQELIP
LGPLREPVSR LDEVDFIITN GGVAKANEIA MRLQPTDAVN LKTGERCAVS KLTRLCAMAG
IGHPSRFFNT LRELNADLVH CQGFADHQAF DAAQLNQLAQ QGAHLIMTEK DAVKCAEFAQ
PNWWYLPVSA QFAPEAEQRI VDKIKEVMEP YGSPSA