(data stored in SCRATCH zone)

SWISSPROT: C6B2L9_RHILS

ID   C6B2L9_RHILS            Unreviewed;       347 AA.
AC   C6B2L9;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   08-MAY-2019, entry version 64.
DE   RecName: Full=Tetraacyldisaccharide 4'-kinase {ECO:0000256|HAMAP-Rule:MF_00409, ECO:0000256|SAAS:SAAS00093884};
DE            EC=2.7.1.130 {ECO:0000256|HAMAP-Rule:MF_00409, ECO:0000256|SAAS:SAAS00702544};
DE   AltName: Full=Lipid A 4'-kinase {ECO:0000256|HAMAP-Rule:MF_00409};
GN   Name=lpxK {ECO:0000256|HAMAP-Rule:MF_00409};
GN   OrderedLocusNames=Rleg_0534 {ECO:0000313|EMBL:ACS54839.1};
OS   Rhizobium leguminosarum bv. trifolii (strain WSM1325).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=395491 {ECO:0000313|EMBL:ACS54839.1, ECO:0000313|Proteomes:UP000002256};
RN   [1] {ECO:0000313|EMBL:ACS54839.1, ECO:0000313|Proteomes:UP000002256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM1325 {ECO:0000313|EMBL:ACS54839.1,
RC   ECO:0000313|Proteomes:UP000002256};
RX   PubMed=21304718;
RA   Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K.,
RA   Tiwari R., Copeland A., Nolan M., Han C., Brettin T., Land M.,
RA   Ovchinikova G., Ivanova N., Mavromatis K., Markowitz V., Kyrpides N.,
RA   Melino V., Denton M., Yates R., Howieson J.;
RT   "Complete genome sequence of Rhizobium leguminosarum bv. trifolii
RT   strain WSM1325, an effective microsymbiont of annual Mediterranean
RT   clovers.";
RL   Stand. Genomic Sci. 2:347-356(2010).
CC   -!- FUNCTION: Transfers the gamma-phosphate of ATP to the 4'-position
CC       of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-
CC       P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
CC       {ECO:0000256|HAMAP-Rule:MF_00409, ECO:0000256|SAAS:SAAS00702551}.
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)-
CC         alpha-D-glucosaminyl phosphate) = ADP + (2-N,3-O-bis((3R)-3-
CC         hydroxytetradecanoyl)-4-O-phospho-beta-D-glucosaminyl)-(1->6)-
CC         (2-N,3-O-bis((3R)-3-hydroxytetradecanoyl)-alpha-D-glucosaminyl
CC         phosphate).; EC=2.7.1.130; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00409, ECO:0000256|SAAS:SAAS01125012};
CC   -!- PATHWAY: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid
CC       IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and
CC       UDP-N-acetyl-alpha-D-glucosamine: step 6/6. {ECO:0000256|HAMAP-
CC       Rule:MF_00409, ECO:0000256|SAAS:SAAS00702534}.
CC   -!- SIMILARITY: Belongs to the LpxK family. {ECO:0000256|HAMAP-
CC       Rule:MF_00409, ECO:0000256|SAAS:SAAS00573394}.
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DR   EMBL; CP001622; ACS54839.1; -; Genomic_DNA.
DR   RefSeq; WP_012756222.1; NC_012850.1.
DR   EnsemblBacteria; ACS54839; ACS54839; Rleg_0534.
DR   KEGG; rlg:Rleg_0534; -.
DR   HOGENOM; HOG000004954; -.
DR   KO; K00912; -.
DR   OMA; MDDGFQN; -.
DR   OrthoDB; 1382484at2; -.
DR   UniPathway; UPA00359; UER00482.
DR   Proteomes; UP000002256; 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   HAMAP; MF_00409; LpxK; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR003758; Tetraacyldisaccharide_4-kinase.
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;
DR   PRODOM; C6B2L9.
DR   SWISS-2DPAGE; C6B2L9.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00409,
KW   ECO:0000256|SAAS:SAAS00702524};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002256};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00409,
KW   ECO:0000256|SAAS:SAAS00702526, ECO:0000313|EMBL:ACS54839.1};
KW   Lipid A biosynthesis {ECO:0000256|HAMAP-Rule:MF_00409,
KW   ECO:0000256|SAAS:SAAS00702533};
KW   Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00409,
KW   ECO:0000256|SAAS:SAAS00702535};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_00409,
KW   ECO:0000256|SAAS:SAAS00702523};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00409,
KW   ECO:0000256|SAAS:SAAS00702552};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00409,
KW   ECO:0000256|SAAS:SAAS00702525, ECO:0000313|EMBL:ACS54839.1}.
FT   NP_BIND      54     61       ATP. {ECO:0000256|HAMAP-Rule:MF_00409}.
SQ   SEQUENCE   347 AA;  37426 MW;  70EB20CA7143E30E CRC64;
     MISEAPPFWW RKADWRAWLL LPLSFLYGRI ASHRMAHARR ASVPIPVICV GNFTVGGAGK
     TPTALTIARA AKAKGLKPGF LSRGYGGSLD VTTVVDPDHH RAIAVGDEPL LLAQEALTVI
     SRRRVEGAAR LVAEGADLII MDDGFQSARL AIDYALLVID ATRGLGNGHI VPGGPVRAPI
     RQQLRSATAL LKVGGGNAAD RIVRMAARAA KPYFTASLKV RGDNTLAGTK VLAFAGIADP
     AKFFRTVESR GAEIVVAKSF GDHEHLTEEE IDDILTTAER QGLLIVTTSK DFVRLSGHQG
     KAARLVEKSR VIEVDMVFED HLAPSLIIDR AIVACRERRL REMKAGA
//

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