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LPXK_PSEAE
ID   LPXK_PSEAE              Reviewed;         332 AA.
AC   Q9HZM3;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 111.
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=PA2981;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(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; AE004091; AAG06369.1; -; Genomic_DNA.
DR   PIR; E83274; E83274.
DR   RefSeq; NP_251671.1; NC_002516.2.
DR   RefSeq; WP_003091159.1; NZ_QZGE01000009.1.
DR   AlphaFoldDB; Q9HZM3; -.
DR   SMR; Q9HZM3; -.
DR   STRING; 287.DR97_4958; -.
DR   PaxDb; Q9HZM3; -.
DR   PRIDE; Q9HZM3; -.
DR   EnsemblBacteria; AAG06369; AAG06369; PA2981.
DR   GeneID; 880503; -.
DR   KEGG; pae:PA2981; -.
DR   PATRIC; fig|208964.12.peg.3128; -.
DR   PseudoCAP; PA2981; -.
DR   HOGENOM; CLU_038816_2_0_6; -.
DR   InParanoid; Q9HZM3; -.
DR   OMA; MDDGFQN; -.
DR   PhylomeDB; Q9HZM3; -.
DR   BioCyc; PAER208964:G1FZ6-3033-MON; -.
DR   BRENDA; 2.7.1.130; 5087.
DR   UniPathway; UPA00359; UER00482.
DR   Proteomes; UP000002438; 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   3: Inferred from homology;
KW   ATP-binding; Kinase; Lipid A biosynthesis; Lipid biosynthesis;
KW   Lipid metabolism; Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..332
FT                   /note="Tetraacyldisaccharide 4'-kinase"
FT                   /id="PRO_0000190937"
FT   BINDING         60..67
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00409"
SQ   SEQUENCE   332 AA;  36746 MW;  CA1D830F1CFDDB6E CRC64;
     MSFSERLLAA WYQGHPALAL LRPLEALYRR VANGRRADFL SGRKPAYRAP LPVLVVGNIT
     VGGTGKTPMI LWMIEHCRAR GLRVGVISRG YGARPPTTPW RVRAEQDAAE AGDEPLMIVR
     RSGVPLMIDP DRPRALQALL AEEQLDLVLC DDGLQHYRLA RDLELVLIDA ARGLGNGRCL
     PAGPLREPAE RLESVDALLY NGADEDPDGG YAFRLQPTAL INLQSGERRP LEHFPAGQEV
     HALAGIGNPQ RFFRTLEALH WRAIPHAFPD HATYTAAELA FSPPLPLLMT EKDAVKCRAF
     AAADWWYLAV DAVPSPAFVA WFDARLEHLL AR
 
 
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