LPXK_AQUAE
ID LPXK_AQUAE Reviewed; 315 AA.
AC O67572;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 117.
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=aq_1656;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
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; AE000657; AAC07542.1; -; Genomic_DNA.
DR PIR; C70443; C70443.
DR RefSeq; NP_214138.1; NC_000918.1.
DR RefSeq; WP_010881075.1; NC_000918.1.
DR PDB; 4EHW; X-ray; 2.30 A; A=1-315.
DR PDB; 4EHX; X-ray; 1.90 A; A=1-315.
DR PDB; 4EHY; X-ray; 2.20 A; A=1-315.
DR PDB; 4ITL; X-ray; 2.09 A; A=1-315.
DR PDB; 4ITM; X-ray; 2.20 A; A=1-315.
DR PDB; 4ITN; X-ray; 2.19 A; A=1-315.
DR PDB; 4LKV; X-ray; 3.51 A; A/B/C/D=1-315.
DR PDBsum; 4EHW; -.
DR PDBsum; 4EHX; -.
DR PDBsum; 4EHY; -.
DR PDBsum; 4ITL; -.
DR PDBsum; 4ITM; -.
DR PDBsum; 4ITN; -.
DR PDBsum; 4LKV; -.
DR AlphaFoldDB; O67572; -.
DR SMR; O67572; -.
DR STRING; 224324.aq_1656; -.
DR PRIDE; O67572; -.
DR EnsemblBacteria; AAC07542; AAC07542; aq_1656.
DR KEGG; aae:aq_1656; -.
DR PATRIC; fig|224324.8.peg.1278; -.
DR eggNOG; COG1663; Bacteria.
DR HOGENOM; CLU_038816_6_0_0; -.
DR InParanoid; O67572; -.
DR OMA; MDDGFQN; -.
DR OrthoDB; 1382484at2; -.
DR BRENDA; 2.7.1.130; 396.
DR UniPathway; UPA00359; UER00482.
DR Proteomes; UP000000798; Chromosome.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Kinase; Lipid A biosynthesis;
KW Lipid biosynthesis; Lipid metabolism; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..315
FT /note="Tetraacyldisaccharide 4'-kinase"
FT /id="PRO_0000190907"
FT BINDING 45..52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00409"
FT HELIX 3..6
FT /evidence="ECO:0007829|PDB:4EHX"
FT HELIX 7..25
FT /evidence="ECO:0007829|PDB:4EHX"
FT STRAND 38..47
FT /evidence="ECO:0007829|PDB:4EHX"
FT HELIX 51..61
FT /evidence="ECO:0007829|PDB:4EHX"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:4EHX"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:4EHX"
FT STRAND 80..86
FT /evidence="ECO:0007829|PDB:4EHX"
FT HELIX 94..97
FT /evidence="ECO:0007829|PDB:4EHX"
FT HELIX 99..107
FT /evidence="ECO:0007829|PDB:4EHX"
FT STRAND 111..118
FT /evidence="ECO:0007829|PDB:4EHX"
FT HELIX 119..130
FT /evidence="ECO:0007829|PDB:4EHX"
FT STRAND 133..139
FT /evidence="ECO:0007829|PDB:4EHX"
FT STRAND 149..156
FT /evidence="ECO:0007829|PDB:4EHX"
FT HELIX 157..160
FT /evidence="ECO:0007829|PDB:4EHX"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:4EHX"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:4EHX"
FT HELIX 174..179
FT /evidence="ECO:0007829|PDB:4EHX"
FT STRAND 181..186
FT /evidence="ECO:0007829|PDB:4EHX"
FT TURN 188..190
FT /evidence="ECO:0007829|PDB:4EHX"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:4EHW"
FT STRAND 201..212
FT /evidence="ECO:0007829|PDB:4EHX"
FT HELIX 221..224
FT /evidence="ECO:0007829|PDB:4EHX"
FT STRAND 229..235
FT /evidence="ECO:0007829|PDB:4EHX"
FT HELIX 237..248
FT /evidence="ECO:0007829|PDB:4EHX"
FT STRAND 252..257
FT /evidence="ECO:0007829|PDB:4EHX"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:4EHX"
FT HELIX 279..282
FT /evidence="ECO:0007829|PDB:4EHX"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:4ITN"
FT STRAND 291..300
FT /evidence="ECO:0007829|PDB:4EHX"
FT HELIX 303..312
FT /evidence="ECO:0007829|PDB:4EHX"
SQ SEQUENCE 315 AA; 36542 MW; 24B90E8C1D15BE9C CRC64;
MLRSSLLPFS YLYEKIINFR NTLYDKGFLK IKKLPVPVIS VGNLSVGGSG KTSFVMYLAD
LLKDKRVCIL SRGYKRKSKG TLIVSEYGNL KVSWEEAGDE PYLMAKLLPH VSVVASEDRY
KGGLLALEKL SPEVFILDDG FQHRKLHRDL NILLLKKKDL KDRLLPAGNL REPLKEIRRA
DALVLTYQEV EPFEFFTGKP TFKMFREFCC LLNSDFEEVP FDILKEREVI AFSGLGDNGQ
FRKVLKNLGI KVKEFMSFPD HYDYSDFTPE EGEIYLTTPK DLIKLQGYEN VFALNFKVKL
EREEKLKKLI YRIFY
