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LPXK_BACTN
ID   LPXK_BACTN              Reviewed;         380 AA.
AC   Q8A6K1;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 98.
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=BT_1880;
OS   Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS   CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=226186;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC   VPI-5482 / E50;
RX   PubMed=12663928; DOI=10.1126/science.1080029;
RA   Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA   Hooper L.V., Gordon J.I.;
RT   "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL   Science 299:2074-2076(2003).
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; AE015928; AAO76987.1; -; Genomic_DNA.
DR   RefSeq; NP_810793.1; NC_004663.1.
DR   RefSeq; WP_008765467.1; NZ_UYXG01000021.1.
DR   AlphaFoldDB; Q8A6K1; -.
DR   SMR; Q8A6K1; -.
DR   STRING; 226186.BT_1880; -.
DR   PaxDb; Q8A6K1; -.
DR   PRIDE; Q8A6K1; -.
DR   DNASU; 1076171; -.
DR   EnsemblBacteria; AAO76987; AAO76987; BT_1880.
DR   GeneID; 60927867; -.
DR   KEGG; bth:BT_1880; -.
DR   PATRIC; fig|226186.12.peg.1932; -.
DR   eggNOG; COG1663; Bacteria.
DR   HOGENOM; CLU_038816_6_0_10; -.
DR   InParanoid; Q8A6K1; -.
DR   OMA; MDDGFQN; -.
DR   UniPathway; UPA00359; UER00482.
DR   Proteomes; UP000001414; 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..380
FT                   /note="Tetraacyldisaccharide 4'-kinase"
FT                   /id="PRO_0000340822"
FT   BINDING         51..58
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00409"
SQ   SEQUENCE   380 AA;  43636 MW;  C6D34EABF62B330F CRC64;
     MDEHFIKIHK WLYPVSWIYG AVVTVRNKLF DWGFLRSKSF GVPVICIGNL SVGGTGKTPH
     TEYLIKLLRD NYHVAVLSRG YKRHSRGYVL ATPQSTARSI GDEPYQMHTK FPSVTLAVDE
     NRCHGIEQLL SIKEPSIEVV LLDDAFQHRY VKPGLSILLT DYHRLFCDDT LLPAGRLRES
     VNGKNRAQIV IVTKCPQDIK PIDYNIITKR LNLYPYQQLY FSSFRYGNLQ PVFPSANSEI
     DSTVNELPLS ALTNTDILLV TGIASPAPIL EELKMYTDQI DSLSFDDHHH FSHRDIQQIK
     ERFGKLKGEH KLIVTTEKDA TRLIHHPVLS EELKPFIYAL PIEIEILQNQ QDKFNQHIIG
     YVRENTRNSS FSERENAHQS
 
 
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