Lipid A biosynthesis lauroyl acyltransferase (P0ACV0)

Identification
Name:Lipid A biosynthesis lauroyl acyltransferase
Synonyms:
  • Heat shock protein B
Gene Name:htrB
Enzyme Class:
Biological Properties
General Function:Involved in transferase activity, transferring acyl groups
Specific Function:Acylates the intermediate (KDO)2-lipid IVA to form (KDO)2-(lauroyl)-lipid IVA. Has 10 fold selectivity for lauroyl- ACP over myristoyl-ACP
Cellular Location:Cell inner membrane; Single-pass membrane protein (Potential)
SMPDB Pathways:
KEGG Pathways:
  • Lipopolysaccharide biosynthesis ec00540
KEGG Reactions:
1.0Lauroyl-KDO2-lipid IV(A)+1.0Acyl-carrier protein+1.0Dodecanoyl-[acyl-carrier protein]+1.0Thumb ↔ 1.0Dodecanoyl-[acyl-carrier protein]+1.0Di[3-deoxy-D-manno-octulosonyl]-lipid IV(A)+1.0Thumb+1.0Acyl-carrier protein
1.0Lauroyl-KDO2-lipid IV(A) + 1.0Acyl-carrier protein + 1.0Dodecanoyl-[acyl-carrier protein] + 1.0KDO(2)-lipid IV(A) ↔ 1.0Dodecanoyl-[acyl-carrier protein] + 1.0Di[3-deoxy-D-manno-octulosonyl]-lipid IV(A) + 1.0Lauroyl-KDO2-lipid IV(A) + 1.0Acyl-carrier protein
ReactionCard
SMPDB Reactions:
1.0a-Kdo-(2->4)-a-Kdo-(2->6)-lipid IVA+1.0dodecanoyl-[acp] +1.0Thumb → 1.0Thumb+1.0a holo-[acyl-carrier protein]
1.0a-Kdo-(2->4)-a-Kdo-(2->6)-lipid IVA + 1.0dodecanoyl-[acp]  + 1.0a-Kdo-(2->4)-a-Kdo-(2->6)-lipid IVA → 1.0Lauroyl-KDO2-lipid IV(A) + 1.0a holo-[acyl-carrier protein]
ReactionCard
Complex Reactions:
1.0Dodecanoyl-ACP (n-C12:0ACP)+1.0Thumb → 1.0acyl carrier protein+1.0Thumb
1.0Dodecanoyl-ACP (n-C12:0ACP) + 1.0KDO(2)-lipid IV(A) → 1.0acyl carrier protein + 1.0KDO(2)-lipid IV(A) with laurate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB24178a-Kdo-(2->4)-a-Kdo-(2->6)-lipid IVAMetaboCard
ECMDB21235KDO(2)-lipid IV(A)MetaboCard
ECMDB21234KDO(2)-lipid IV(A) with laurateMetaboCard
ECMDB23769Lauroyl-KDO2-lipid IV(A)MetaboCard
GO Classification:
Component
cell part
cell wall
external encapsulating structure
Gram-negative-bacterium-type cell wall
integral to membrane
intrinsic to membrane
membrane part
peptidoglycan-based cell wall
Function
acyltransferase activity
catalytic activity
transferase activity
transferase activity, transferring acyl groups
transferase activity, transferring acyl groups other than amino-acyl groups
Process
carbohydrate metabolic process
lipopolysaccharide core region biosynthetic process
metabolic process
oligosaccharide biosynthetic process
oligosaccharide metabolic process
primary metabolic process
Gene Properties
Blattner:b1054
Gene OrientationCounterclockwise
Centisome Percentage:24.03
Left Sequence End1114885
Right Sequence End1115805
Gene Sequence:
>921 bp
ATGACTGATAAAATCGCGGTCCTGTTGGGTGGGACCTCCGCTGAGCGGGAAGTTTCTCTG
AATTCTGGCGCAGCGGTGTTAGCCGGACTGCGTGAAGGCGGTATTGACGCGTATCCTGTC
GACCCGAAAGAAGTCGACGTGACGCAACTGAAGTCGATGGGCTTTCAGAAAGTGTTTATC
GCGCTACACGGTCGCGGCGGTGAAGATGGTACGCTGCAGGGGATGCTCGAGCTGATGGGC
TTGCCTTATACCGGAAGCGGAGTGATGGCATCTGCGCTTTCAATGGATAAACTACGCAGC
AAACTTCTATGGCAAGGTGCCGGTTTACCGGTCGCGCCGTGGGTAGCGTTAACCCGCGCA
GAGTTTGAAAAAGGCCTGAGCGATAAGCAGTTAGCAGAAATTTCTGCTCTGGGTTTGCCG
GTTATCGTTAAGCCGAGCCGCGAAGGTTCCAGTGTGGGAATGTCAAAAGTAGTAGCAGAA
AATGCTCTACAAGATGCATTAAGATTGGCATTTCAGCACGATGAAGAAGTATTGATTGAA
AAATGGCTAAGTGGGCCGGAGTTCACGGTTGCGATACTCGGTGAAGAAATTTTACCGTCA
ATACGTATTCAACCGTCCGGAACCTTCTATGATTATGAGGCGAAGTATCTCTCTGATGAG
ACACAGTATTTCTGCCCCGCAGGTCTGGAAGCGTCACAAGAGGCCAATTTGCAGGCATTA
GTGCTGAAAGCATGGACGACGTTAGGTTGCAAAGGATGGGGACGTATTGACGTTATGCTG
GACAGCGATGGACAGTTTTATCTGCTGGAAGCCAATACCTCACCGGGTATGACCAGCCAC
AGCCTGGTGCCGATGGCGGCACGTCAGGCAGGTATGAGCTTCTCGCAGTTGGTAGTACGA
ATTCTGGAACTGGCGGACTAA
Protein Properties
Pfam Domain Function:
Protein Residues:306
Protein Molecular Weight:35407
Protein Theoretical pI:10
Signaling Regions:
  • None
Transmembrane Regions:
  • 17-37
Protein Sequence:
>Lipid A biosynthesis lauroyl acyltransferase
MTNLPKFSTALLHPRYWLTWLGIGVLWLVVQLPYPVIYRLGCGLGKLALRFMKRRAKIVH
RNLELCFPEMSEQERRKMVVKNFESVGMGLMETGMAWFWPDRRIARWTEVIGMEHIRDVQ
AQKRGILLVGIHFLTLELGARQFGMQEPGIGVYRPNDNPLIDWLQTWGRLRSNKSMLDRK
DLKGMIKALKKGEVVWYAPDHDYGPRSSVFVPLFAVEQAATTTGTWMLARMSGACLVPFV
PRRKPDGKGYQLIMLPPECSPPLDDAETTAAWMNKVVEKCIMMAPEQYMWLHRRFKTRPE
GVPSRY
References
External Links:
ResourceLink
Uniprot ID:P0ACV0
Uniprot Name:HTRB_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:21321973
Ecogene ID:EG10464
Ecocyc:EG10464
ColiBase:b1054
Kegg Gene:b1054
EchoBASE ID:EB0459
CCDB:HTRB_ECOLI
BacMap:16129017
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Brozek, K. A., Raetz, C. R. (1990). "Biosynthesis of lipid A in Escherichia coli. Acyl carrier protein-dependent incorporation of laurate and myristate." J Biol Chem 265:15410-15417. Pubmed: 2203778
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Karow, M., Fayet, O., Cegielska, A., Ziegelhoffer, T., Georgopoulos, C. (1991). "Isolation and characterization of the Escherichia coli htrB gene, whose product is essential for bacterial viability above 33 degrees C in rich media." J Bacteriol 173:741-750. Pubmed: 1846149
  • Karow, M., Georgopoulos, C. (1991). "Sequencing, mutational analysis, and transcriptional regulation of the Escherichia coli htrB gene." Mol Microbiol 5:2285-2292. Pubmed: 1840644
  • Oshima, T., Aiba, H., Baba, T., Fujita, K., Hayashi, K., Honjo, A., Ikemoto, K., Inada, T., Itoh, T., Kajihara, M., Kanai, K., Kashimoto, K., Kimura, S., Kitagawa, M., Makino, K., Masuda, S., Miki, T., Mizobuchi, K., Mori, H., Motomura, K., Nakamura, Y., Nashimoto, H., Nishio, Y., Saito, N., Horiuchi, T., et, a. l. .. (1996). "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." DNA Res 3:137-155. Pubmed: 8905232
  • Ueguchi, C., Ito, K. (1992). "Multicopy suppression: an approach to understanding intracellular functioning of the protein export system." J Bacteriol 174:1454-1461. Pubmed: 1537791