LPXK_VEREI
ID LPXK_VEREI Reviewed; 430 AA.
AC A1WSH4;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Tetraacyldisaccharide 4'-kinase;
DE EC=2.7.1.130;
DE AltName: Full=Lipid A 4'-kinase;
GN Name=lpxK; OrderedLocusNames=Veis_4893;
OS Verminephrobacter eiseniae (strain EF01-2).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Verminephrobacter.
OX NCBI_TaxID=391735;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EF01-2;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT "Complete sequence of chromosome 1 of Verminephrobacter eiseniae EF01-2.";
RL Submitted (DEC-2006) 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). {ECO:0000250}.
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;
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.
CC -!- SIMILARITY: In the N-terminal section; belongs to the LpxK family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the UPF0434 family.
CC {ECO:0000305}.
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DR EMBL; CP000542; ABM60581.1; -; Genomic_DNA.
DR AlphaFoldDB; A1WSH4; -.
DR SMR; A1WSH4; -.
DR STRING; 391735.Veis_4893; -.
DR EnsemblBacteria; ABM60581; ABM60581; Veis_4893.
DR KEGG; vei:Veis_4893; -.
DR eggNOG; COG1663; Bacteria.
DR eggNOG; COG2835; Bacteria.
DR HOGENOM; CLU_038816_2_0_4; -.
DR OMA; MDDGFQN; -.
DR UniPathway; UPA00359; UER00482.
DR Proteomes; UP000000374; 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 HAMAP; MF_01187; UPF0434; 1.
DR InterPro; IPR003758; LpxK.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005651; Trm112-like.
DR PANTHER; PTHR42724; PTHR42724; 2.
DR Pfam; PF02606; LpxK; 1.
DR Pfam; PF03966; Trm112p; 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..430
FT /note="Tetraacyldisaccharide 4'-kinase"
FT /id="PRO_0000291253"
FT REGION 1..370
FT /note="Tetraacyldisaccharide 4'-kinase"
FT REGION 371..396
FT /note="UPF0434"
FT BINDING 70..77
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 430 AA; 46357 MW; F609EA03F6D3A864 CRC64;
MGALRPQPPR MPAGHVAPAY WQKRGLAAWA LWPLAQLYRA LVAARRGLYR AGWLKAQHPG
RPVIVVGNVI AGGAGKTPVV IALARHLQAR GLRVGVIARG HGRSRRDCRA VLPDSPASAV
GDEPALIARH FANGPAVPVF VARRRISAAR ALLAAHPDTD VLLCDDGLQH LALRRDLEIC
VFNDQGLGNG FLQPAGPLRE PWPRSVDFVL HAGAAPGGSP APAFGVQRSL APCALRSDGA
AVPLARLQGQ PLHALAAVAR PGEFFAMLQA RGLTLAHTEA LPDHYDLQRW ERMTDPRLTL
ICTEKDAVKL WPLHPDALAV PLVLHIDPGF FAALDAWLPA RRAMPEIAPG SDAAAIIAGT
EPTLPENHRP MDPKLLQLLV CPVTKGPLRY DRAAQELISR SARLAYPVRD GIPVLLENEA
RPLTDEELEQ