Lipid A biosynthesis (KDO)2-(lauroyl)-lipid IVA acyltransferase (P24205)

Identification
Name:Lipid A biosynthesis (KDO)2-(lauroyl)-lipid IVA acyltransferase
Synonyms:Not Available
Gene Name:msbB
Enzyme Class:
Biological Properties
General Function:Involved in transferase activity, transferring acyl groups
Specific Function:Transfers myristate or laurate, activated on ACP, to the lipid IVA moiety of (KDO)2-(lauroyl)-lipid IVA. Decanoyl, palmitoyl, palmitoleoyl, and (R)-3-hydroxymyristoyl-ACP are poor acyl donors. Functions optimally after laurate incorporation by htrB has taken place. Acylates (KDO)2-(lauroyl)-lipid IVA about 100 times faster than (KDO)2-lipid IVA. Displays a preference for myristoyl-ACP over lauroyl-ACP
Cellular Location:Cell inner membrane; Single-pass membrane protein (Potential)
SMPDB Pathways:
KEGG Pathways:
  • Lipopolysaccharide biosynthesis ec00540
KEGG Reactions:
1.0Thumb+1.0Acyl-carrier protein+1.0Tetradecanoyl-[acp]+1.0Thumb ↔ 1.0Tetradecanoyl-[acp]+1.0Lauroyl-KDO2-lipid IV(A)+1.0Acyl-carrier protein
1.0KDO2-Lipid A + 1.0Acyl-carrier protein + 1.0Tetradecanoyl-[acp] + 1.0Lauroyl-KDO2-lipid IV(A) ↔ 1.0Tetradecanoyl-[acp] + 1.0Lauroyl-KDO2-lipid IV(A) + 1.0Acyl-carrier protein
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0 myristoyl-[acp] → 1.0a holo-[acyl-carrier protein]+1.0Thumb
1.0Lauroyl-KDO2-lipid IV(A) + 1.0 myristoyl-[acp] → 1.0a holo-[acyl-carrier protein] + 1.0(KDO)2-lipid A
ReactionCard
1.0Thumb+1.0 myristoyl-[acp] → 1.0Thumb+1.0a holo-[acyl-carrier protein]
1.0KDO2-(palmitoleoyl)-lipid IVA + 1.0 myristoyl-[acp] → 1.0KDO2-lipid A, cold adapted + 1.0a holo-[acyl-carrier protein]
ReactionCard
Complex Reactions:
1.0Thumb+1.0Myristoyl-ACP (n-C14:0ACP) → 1.0acyl carrier protein+1.0Thumb
1.0KDO(2)-lipid IV(A) with laurate + 1.0Myristoyl-ACP (n-C14:0ACP) → 1.0acyl carrier protein + 1.0KDO2-Lipid A
ReactionCard
1.0KDO(2)-lipid IV(A) with palmitoleoyl+1.0Myristoyl-ACP (n-C14:0ACP) → 1.0acyl carrier protein+1.0cold adapted KDO(2)-lipid (A)
1.0KDO(2)-lipid IV(A) with palmitoleoyl + 1.0Myristoyl-ACP (n-C14:0ACP) → 1.0acyl carrier protein + 1.0cold adapted KDO(2)-lipid (A)
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB24179(KDO)2-lipid AMetaboCard
ECMDB21234KDO(2)-lipid IV(A) with laurateMetaboCard
ECMDB20572KDO2-(palmitoleoyl)-lipid IVAMetaboCard
ECMDB21031KDO2-Lipid AMetaboCard
ECMDB20571KDO2-lipid A, cold adaptedMetaboCard
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
lipid biosynthetic process
lipid metabolic process
lipopolysaccharide biosynthetic process
lipopolysaccharide core region biosynthetic process
metabolic process
oligosaccharide biosynthetic process
oligosaccharide metabolic process
primary metabolic process
Gene Properties
Blattner:b1855
Gene OrientationCounterclockwise
Centisome Percentage:41.75
Left Sequence End1937246
Right Sequence End1938217
Gene Sequence:
>972 bp
GTGGCACAGGAATATACTGTTGAACAACTAAACCACGGCCGTAAAGTCTATGACTTTATG
CGCTGGGACTACTGGGCTTTCGGCATCTCTGGTCTGCTGTTAATCGCTGCTATCGTTATT
ATGGGCGTGCGCGGCTTTAACTGGGGGCTGGATTTCACCGGTGGTACGGTTATTGAAATT
ACGCTCGAAAAACCGGCTGAAATTGACGTAATGCGTGATGCATTGCAAAAAGCCGGTTTT
GAAGAGCCGATGCTGCAAAACTTTGGTAGCAGCCATGACATCATGGTCCGTATGCCGCCT
GCTGAAGGCGAAACCGGCGGTCAGGTGTTGGGCAGCCAGGTTCTGAAGGTGATTAACGAA
TCCACCAATCAGAATGCAGCAGTGAAGCGTATTGAGTTCGTCGGTCCGAGCGTGGGGGCA
GACCTTGCGCAAACCGGTGCGATGGCGTTGATGGCAGCGCTGCTGTCTATCCTCGTGTAC
GTAGGTTTCCGCTTTGAGTGGCGACTGGCGGCAGGGGTGGTTATTGCGCTGGCGCACGAC
GTTATCATTACGCTGGGTATTTTGTCGTTATTCCATATCGAGATTGACCTGACCATTGTG
GCATCGTTGATGTCGGTTATCGGTTACTCGCTTAACGACAGTATCGTGGTATCGGACCGT
ATTCGTGAAAACTTCCGCAAGATCCGTCGCGGTACGCCTTACGAAATCTTTAACGTGTCC
TTGACCCAGACGCTGCACCGTACCTTGATCACATCCGGTACTACCTTGATGGTTATCCTG
ATGCTGTACCTCTTCGGTGGTCCGGTACTGGAAGGCTTCTCGCTGACCATGCTTATCGGT
GTTTCCATCGGTACTGCATCTTCCATCTATGTGGCATCTGCGTTGGCTCTGAAACTGGGT
ATGAAGCGCGAACACATGTTGCAGCAGAAAGTGGAAAAAGAAGGGGCGGATCAGCCGTCA
ATTCTGCCGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:323
Protein Molecular Weight:37410
Protein Theoretical pI:10
Signaling Regions:
  • None
Transmembrane Regions:
  • 23-43
Protein Sequence:
>Lipid A biosynthesis (KDO)2-(lauroyl)-lipid IVA acyltransferase
METKKNNSEYIPEFDKSFRHPRYWGAWLGVAAMAGIALTPPKFRDPILARLGRFAGRLGK
SSRRRALINLSLCFPERSEAEREAIVDEMFATAPQAMAMMAELAIRGPEKIQPRVDWQGL
EIIEEMRRNNEKVIFLVPHGWAVDIPAMLMASQGQKMAAMFHNQGNPVFDYVWNTVRRRF
GGRLHARNDGIKPFIQSVRQGYWGYYLPDQDHGPEHSEFVDFFATYKATLPAIGRLMKVC
RARVVPLFPIYDGKTHRLTIQVRPPMDDLLEADDHTIARRMNEEVEIFVGPRPEQYTWIL
KLLKTRKPGEIQPYKRKDLYPIK
References
External Links:
ResourceLink
Uniprot ID:P24205
Uniprot Name:MSBB_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674549
Ecogene ID:EG10614
Ecocyc:EG10614
ColiBase:b1855
Kegg Gene:b1855
EchoBASE ID:EB0609
CCDB:MSBB_ECOLI
BacMap:16129808
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
  • Clementz, T., Zhou, Z., Raetz, C. R. (1997). "Function of the Escherichia coli msbB gene, a multicopy suppressor of htrB knockouts, in the acylation of lipid A. Acylation by MsbB follows laurate incorporation by HtrB." J Biol Chem 272:10353-10360. Pubmed: 9099672
  • Engel, H., Smink, A. J., van Wijngaarden, L., Keck, W. (1992). "Murein-metabolizing enzymes from Escherichia coli: existence of a second lytic transglycosylase." J Bacteriol 174:6394-6403. Pubmed: 1356966
  • 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
  • Itoh, T., Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Kasai, H., Kimura, S., Kitakawa, M., Kitagawa, M., Makino, K., Miki, T., Mizobuchi, K., Mori, H., Mori, T., Motomura, K., Nakade, S., Nakamura, Y., Nashimoto, H., Nishio, Y., Oshima, T., Saito, N., Sampei, G., Seki, Y., Horiuchi, T., et, a. l. .. (1996). "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map." DNA Res 3:379-392. Pubmed: 9097040
  • Karow, M., Georgopoulos, C. (1992). "Isolation and characterization of the Escherichia coli msbB gene, a multicopy suppressor of null mutations in the high-temperature requirement gene htrB." J Bacteriol 174:702-710. Pubmed: 1732206