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LPXK_VIBC3
ID   LPXK_VIBC3              Reviewed;         335 AA.
AC   A5F728; C3M1R9;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 2.
DT   03-AUG-2022, entry version 65.
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=VC0395_A1468, VC395_1992;
OS   Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS   O395).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=345073;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA   Heidelberg J.;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX   PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA   Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA   Wang W., Wang J., Qian W., Li D., Wang L.;
RT   "A recalibrated molecular clock and independent origins for the cholera
RT   pandemic clones.";
RL   PLoS ONE 3:E4053-E4053(2008).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABQ21048.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=ACP09985.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000627; ABQ21048.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP001235; ACP09985.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_002034410.1; NZ_JAACZH010000001.1.
DR   AlphaFoldDB; A5F728; -.
DR   SMR; A5F728; -.
DR   STRING; 345073.VC395_1992; -.
DR   EnsemblBacteria; ABQ21048; ABQ21048; VC0395_A1468.
DR   KEGG; vco:VC0395_A1468; -.
DR   KEGG; vcr:VC395_1992; -.
DR   PATRIC; fig|345073.21.peg.1925; -.
DR   eggNOG; COG1663; Bacteria.
DR   HOGENOM; CLU_038816_2_0_6; -.
DR   UniPathway; UPA00359; UER00482.
DR   Proteomes; UP000000249; Chromosome 2.
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..335
FT                   /note="Tetraacyldisaccharide 4'-kinase"
FT                   /id="PRO_0000340866"
FT   BINDING         59..66
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00409"
SQ   SEQUENCE   335 AA;  37073 MW;  ED9A2F75CDE52DBF CRC64;
     MIEKIWFHRH PLGYLLWPLL WPFSVLFGVI SRSRRKAYQT GDKPSYRAPL PVVVVGNITA
     GGNGKTPVVV WLVETLQNLG YRPGVVSRGY GAKAPSYPLV VNEQTPAQHC GDEPKLIFQR
     TKAPVAVDPV RSQAVKALLE HGVNVIVTDD GLQHYALQRD IEIAVVDGVR RFGNQELIPL
     GPLREPVSRL DEVDFIITNG GVAKANEIAM RLQPTDAVNL KTGERCAVSK LTRLCAMAGI
     GHPSRFFNTL RELNADLVHC QGFADHQAFD AAQLNQLAQQ GDHLIMTEKD AVKCAEFAQP
     NWWYLPVSAQ FAPEAEQRIV DKIKEVMEPY GSPSA
 
 
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