Apolipoprotein N-acyltransferase (P23930)

Identification
Name:Apolipoprotein N-acyltransferase
Synonyms:
  • ALP N-acyltransferase
  • Copper homeostasis protein cutE
Gene Name:lnt
Enzyme Class:Not Available
Biological Properties
General Function:Involved in N-acyltransferase activity
Specific Function:Transfers the fatty acyl group on membrane lipoproteins
Cellular Location:Cell inner membrane; Multi-pass membrane protein
SMPDB Pathways:Not Available
KEGG Pathways:Not Available
Complex Reactions:
1.0applipoprotein+1.0Thumb → 1.0Thumb+1.0lipoprotein
1.0applipoprotein + 1.0PE(14:0/14:0) → 1.02-Acyl-sn-glycero-3-phosphoethanolamine (N-C16:0) + 1.0lipoprotein
ReactionCard
1.0applipoprotein+1.0Thumb → 1.0Thumb+1.0lipoprotein
1.0applipoprotein + 1.0PG(16:0/16:0) → 1.02-Acyl-sn-glycero-3-phosphoglycerol (N-C16:0) + 1.0lipoprotein
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB211422-Acyl-sn-glycero-3-phosphoethanolamine (N-C16:0)MetaboCard
ECMDB211492-Acyl-sn-glycero-3-phosphoglycerol (N-C16:0)MetaboCard
ECMDB08821PE(14:0/14:0)MetaboCard
ECMDB10570PG(16:0/16:0)MetaboCard
GO Classification:
Component
cell part
integral to membrane
intrinsic to membrane
membrane part
Function
acyltransferase activity
catalytic activity
hydrolase activity
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
N-acyltransferase activity
transferase activity
transferase activity, transferring acyl groups
transferase activity, transferring acyl groups other than amino-acyl groups
Process
biosynthetic process
cellular macromolecule biosynthetic process
lipoprotein biosynthetic process
macromolecule biosynthetic process
metabolic process
nitrogen compound metabolic process
Gene Properties
Blattner:b0657
Gene OrientationCounterclockwise
Centisome Percentage:14.84
Left Sequence End688566
Right Sequence End690104
Gene Sequence:
>1539 bp
ATGGCTTTTGCCTCATTAATTGAACGCCAGCGCATTCGCCTGCTGCTGGCGTTATTATTC
GGTGCCTGCGGAACGCTGGCCTTCTCTCCTTACGACGTCTGGCCTGCGGCGATTATTTCG
CTGATGGGGCTTCAGGCGTTGACCTTTAACCGCCGTCCACTCCAGTCTGCCGCTATTGGC
TTTTGCTGGGGATTTGGCCTCTTTGGCAGCGGTATTAACTGGGTCTATGTCAGCATCGCG
ACCTTTGGCGGAATGCCTGGCCCGGTTAACATCTTCCTGGTGGTGCTGCTGGCGGCGTAT
TTGTCGCTGTATACCGGACTGTTTGCTGGCGTGCTGTCGCGTCTGTGGCCGAAAACCACC
TGGCTGCGCGTAGCGATTGCCGCCCCTGCCCTCTGGCAAGTGACCGAGTTTCTGCGCGGT
TGGGTACTGACCGGCTTCCCGTGGTTACAGTTCGGCTATAGCCAGATTGATGGCCCGTTA
AAAGGGCTGGCACCGATAATGGGCGTGGAAGCCATTAACTTCCTGCTGATGATGGTTAGT
GGCCTGCTGGCACTGGCGTTGGTCAAACGCAACTGGCGTCCGCTGGTGGTGGCCGTCGTG
CTGTTTGCCCTTCCCTTCCCGCTGCGTTACATCCAGTGGTTTACCCCACAACCGGAGAAA
ACCATTCAGGTTTCGATGGTTCAGGGCGATATTCCGCAATCGCTGAAATGGGACGAAGGC
CAGCTTCTTAATACGCTGAAGATTTACTACAACGCAACGGCACCGCTGATGGGCAAATCA
TCGTTGATTATCTGGCCGGAGTCGGCGATAACCGATCTGGAAATTAATCAGCAACCGTTC
CTCAAAGCACTGGACGGTGAGTTGCGTGATAAAGGTAGCTCGCTGGTAACCGGGATTGTC
GACGCGCGTCTCAATAAGCAGAACCGCTACGATACCTACAACACCATCATCACGCTGGGT
AAAGGTGCGCCGTACAGCTACGAATCAGCCGATCGCTATAACAAAAACCATCTGGTGCCG
TTTGGCGAGTTTGTCCCGCTGGAGTCGATTCTGCGTCCGTTAGCACCGTTCTTTGATCTG
CCGATGTCGTCGTTCAGCCGTGGGCCATATATCCAGCCGCCGCTGTCGGCAAATGGTATT
GAGCTTACTGCGGCTATTTGCTACGAGATCATTCTCGGCGAGCAAGTGCGCGATAACTTC
CGCCCGGATACCGACTATCTGCTGACTATCTCCAACGATGCGTGGTTTGGTAAATCTATT
GGTCCATGGCAACACTTCCAGATGGCGCGAATGCGTGCGCTGGAGCTGGCGCGCCCACTG
TTGCGCAGCACCAACAACGGCATTACGGCGGTGATTGGCCCGCAGGGTGAGATTCAGGCG
ATGATCCCGCAGTTCACCCGCGAGGTGTTAACCACTAACGTGACGCCGACCACCGGACTC
ACACCATACGCACGTACCGGCAACTGGCCGCTGTGGGTGCTGACGGCATTGTTTGGTTTT
GCTGCTGTGTTGATGAGTCTGCGTCAGCGACGTAAATAA
Protein Properties
Pfam Domain Function:
Protein Residues:512
Protein Molecular Weight:57065
Protein Theoretical pI:10
Signaling Regions:
  • None
Transmembrane Regions:
  • 12-28
  • 57-77
  • 91-111
  • 168-188
  • 194-214
  • 487-507
Protein Sequence:
>Apolipoprotein N-acyltransferase
MAFASLIERQRIRLLLALLFGACGTLAFSPYDVWPAAIISLMGLQALTFNRRPLQSAAIG
FCWGFGLFGSGINWVYVSIATFGGMPGPVNIFLVVLLAAYLSLYTGLFAGVLSRLWPKTT
WLRVAIAAPALWQVTEFLRGWVLTGFPWLQFGYSQIDGPLKGLAPIMGVEAINFLLMMVS
GLLALALVKRNWRPLVVAVVLFALPFPLRYIQWFTPQPEKTIQVSMVQGDIPQSLKWDEG
QLLNTLKIYYNATAPLMGKSSLIIWPESAITDLEINQQPFLKALDGELRDKGSSLVTGIV
DARLNKQNRYDTYNTIITLGKGAPYSYESADRYNKNHLVPFGEFVPLESILRPLAPFFDL
PMSSFSRGPYIQPPLSANGIELTAAICYEIILGEQVRDNFRPDTDYLLTISNDAWFGKSI
GPWQHFQMARMRALELARPLLRSTNNGITAVIGPQGEIQAMIPQFTREVLTTNVTPTTGL
TPYARTGNWPLWVLTALFGFAAVLMSLRQRRK
References
External Links:
ResourceLink
Uniprot ID:P23930
Uniprot Name:LNT_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674734
Ecogene ID:EG10168
Ecocyc:EG10168
ColiBase:b0657
Kegg Gene:b0657
EchoBASE ID:EB0166
CCDB:LNT_ECOLI
BacMap:16128640
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
  • Daley, D. O., Rapp, M., Granseth, E., Melen, K., Drew, D., von Heijne, G. (2005). "Global topology analysis of the Escherichia coli inner membrane proteome." Science 308:1321-1323. Pubmed: 15919996
  • Gupta, S. D., Gan, K., Schmid, M. B., Wu, H. C. (1993). "Characterization of a temperature-sensitive mutant of Salmonella typhimurium defective in apolipoprotein N-acyltransferase." J Biol Chem 268:16551-16556. Pubmed: 8344936
  • Gupta, S. D., Wu, H. C. (1991). "Identification and subcellular localization of apolipoprotein N-acyltransferase in Escherichia coli." FEMS Microbiol Lett 62:37-41. Pubmed: 2032623
  • 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
  • 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
  • Rogers, S. D., Bhave, M. R., Mercer, J. F., Camakaris, J., Lee, B. T. (1991). "Cloning and characterization of cutE, a gene involved in copper transport in Escherichia coli." J Bacteriol 173:6742-6748. Pubmed: 1938881