LPXK_CHLPN
ID LPXK_CHLPN Reviewed; 365 AA.
AC Q9Z823;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 121.
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};
GN OrderedLocusNames=CPn_0529, CP_0223, CpB0550;
OS Chlamydia pneumoniae (Chlamydophila pneumoniae).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=83558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CWL029;
RX PubMed=10192388; DOI=10.1038/7716;
RA Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W.,
RA Olinger L., Grimwood J., Davis R.W., Stephens R.S.;
RT "Comparative genomes of Chlamydia pneumoniae and C. trachomatis.";
RL Nat. Genet. 21:385-389(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR39;
RX PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA Salzberg S.L., Eisen J.A., Fraser C.M.;
RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT AR39.";
RL Nucleic Acids Res. 28:1397-1406(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J138;
RX PubMed=10871362; DOI=10.1093/nar/28.12.2311;
RA Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K.,
RA Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.;
RT "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from
RT Japan and CWL029 from USA.";
RL Nucleic Acids Res. 28:2311-2314(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TW-183;
RA Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P.,
RA Schneider S., Pohl T., Essig A., Marre R., Melchers K.;
RT "The genome sequence of Chlamydia pneumoniae TW183 and comparison with
RT other Chlamydia strains based on whole genome sequence analysis.";
RL Submitted (MAY-2002) 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: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; AE001363; AAD18669.1; -; Genomic_DNA.
DR EMBL; AE002161; AAF38091.1; -; Genomic_DNA.
DR EMBL; BA000008; BAA98735.1; -; Genomic_DNA.
DR EMBL; AE009440; AAP98479.1; -; Genomic_DNA.
DR PIR; E86556; E86556.
DR PIR; H72068; H72068.
DR RefSeq; NP_224725.1; NC_000922.1.
DR RefSeq; WP_010883167.1; NZ_LN847257.1.
DR AlphaFoldDB; Q9Z823; -.
DR SMR; Q9Z823; -.
DR STRING; 115711.CP_0223; -.
DR EnsemblBacteria; AAD18669; AAD18669; CPn_0529.
DR EnsemblBacteria; AAF38091; AAF38091; CP_0223.
DR GeneID; 45050571; -.
DR KEGG; cpa:CP_0223; -.
DR KEGG; cpj:ycaH; -.
DR KEGG; cpn:CPn_0529; -.
DR KEGG; cpt:CpB0550; -.
DR PATRIC; fig|115713.3.peg.589; -.
DR eggNOG; COG1663; Bacteria.
DR HOGENOM; CLU_038816_6_0_0; -.
DR OrthoDB; 1382484at2; -.
DR UniPathway; UPA00359; UER00482.
DR Proteomes; UP000000583; Chromosome.
DR Proteomes; UP000000801; Chromosome.
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 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; Transferase.
FT CHAIN 1..365
FT /note="Tetraacyldisaccharide 4'-kinase"
FT /id="PRO_0000190920"
FT BINDING 68..75
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00409"
SQ SEQUENCE 365 AA; 40615 MW; D6AAAE76D96794DA CRC64;
MKKRFPSTLF LFYRRVTIAI SLEGILGWGW LGSLLSKVFA FLVACWNRFS WSTPYRARST
VISVGNIVVG GAGKTPTVLW LAEALRLRGY SCGVLSRGYK SQSSRQKKLT VVDSKVHSAS
YVGDEPLLMA EKLPEGSVWV HKDRRISAAR AAEKFGILLL DDGLQYRKLH KDVEIAVVNG
QDPLGGRAFF PKGRLRDFPL RLKTVDAIIV NGGGKEAGTV VKRVSNAPQI FVKPTIASVV
WTHNGERIPK EALRELRVGV FCGLGFPQGF LNMLREEGIH ILGKYLLPDH AAITKKELNY
FCQQMAMRQG QGLLCTEKDS VKLPRLSGEV SLLPIAKVEM RLSVNQDDTL SLLNMIEQIH
KNRGN
