(data stored in SCRATCH zone)

SWISSPROT: A4ATD8_MARSH

ID   A4ATD8_MARSH            Unreviewed;       344 AA.
AC   A4ATD8;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 72.
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=FB2170_16526 {ECO:0000313|EMBL:EAR00708.1};
OS   Maribacter sp. (strain HTCC2170 / KCCM 42371).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=313603 {ECO:0000313|EMBL:EAR00708.1, ECO:0000313|Proteomes:UP000001602};
RN   [1] {ECO:0000313|EMBL:EAR00708.1, ECO:0000313|Proteomes:UP000001602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2170 / KCCM 42371 {ECO:0000313|Proteomes:UP000001602};
RX   PubMed=21037013; DOI=10.1128/JB.01207-10;
RA   Oh H.M., Kang I., Yang S.J., Jang Y., Vergin K.L., Giovannoni S.J.,
RA   Cho J.C.;
RT   "Complete genome sequence of strain HTCC2170, a novel member of the
RT   genus Maribacter in the family Flavobacteriaceae.";
RL   J. Bacteriol. 193:303-304(2011).
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; CP002157; EAR00708.1; -; Genomic_DNA.
DR   STRING; 313603.FB2170_16526; -.
DR   EnsemblBacteria; EAR00708; EAR00708; FB2170_16526.
DR   KEGG; fbc:FB2170_16526; -.
DR   eggNOG; ENOG4105CHD; Bacteria.
DR   eggNOG; COG1663; LUCA.
DR   HOGENOM; HOG000004953; -.
DR   KO; K00912; -.
DR   OMA; MDDGFQN; -.
DR   BioCyc; MSP313603:G1GNS-83-MONOMER; -.
DR   UniPathway; UPA00359; UER00482.
DR   Proteomes; UP000001602; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; A4ATD8.
DR   SWISS-2DPAGE; A4ATD8.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00409,
KW   ECO:0000256|SAAS:SAAS00702524};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001602};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00409,
KW   ECO:0000256|SAAS:SAAS00702526, ECO:0000313|EMBL:EAR00708.1};
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}; Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00409,
KW   ECO:0000256|SAAS:SAAS00702552};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001602};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00409,
KW   ECO:0000256|SAAS:SAAS00702525};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM      7     30       Helical. {ECO:0000256|SAM:Phobius}.
FT   NP_BIND      59     66       ATP. {ECO:0000256|HAMAP-Rule:MF_00409}.
SQ   SEQUENCE   344 AA;  39659 MW;  41D814F2E10D3D12 CRC64;
     MLPKIKYYIF VLMQLLRKIA FPFSLIYALV VHIRNYLYDT GLFTSKSFKT PTICVGNLSV
     GGTGKTPMIE YLIENLSTSF KIAVLSRGYR RKSKGYVLAG TESKVEDIGD EPYQIHSKFP
     NISVAVDADR CRGIRKLQET IQPDVILLDD AFQHRKVQPQ FSLLLTSYDN LYIKDWYLPT
     GDLRDSKREA KRANIIIVTK CPVHLNKRIQ EEIIKNLNPK QDQQVLFCYY YYSEKLLGNN
     SSVSLDDFKG KRITLVTGIA NPKALVDYLA GKGIDFEHLE YKDHHFFTKQ EIDLINSKEH
     VLTTEKDFVR LNNEVENLHY ISVKHVFLDE GSSVLERSLQ QVMS
//

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