Maltoporin
Details
- Name
- Maltoporin
- Synonyms
- Lambda receptor protein
- malB
- Maltose-inducible porin
- Gene Name
- lamB
- Organism
- Escherichia coli (strain K12)
- Amino acid sequence
>lcl|BSEQ0020670|Maltoporin MMITLRKLPLAVAVAAGVMSAQAMAVDFHGYARSGIGWTGSGGEQQCFQTTGAQSKYRLG NECETYAELKLGQEVWKEGDKSFYFDTNVAYSVAQQNDWEATDPAFREANVQGKNLIEWL PGSTIWAGKRFYQRHDVHMIDFYYWDISGPGAGLENIDVGFGKLSLAATRSSEAGGSSSF ASNNIYDYTNETANDVFDVRLAQMEINPGGTLELGVDYGRANLRDNYRLVDGASKDGWLF TAEHTQSVLKGFNKFVVQYATDSMTSQGKGLSQGSGVAFDNEKFAYNINNNGHMLRILDH GAISMGDNWDMMYVGMYQDINWDNDNGTKWWTVGIRPMYKWTPIMSTVMEIGYDNVESQR TGDKNNQYKITLAQQWQAGDSIWSRPAIRVFATYAKWDEKWGYDYTGNADNNANFGKAVP ADFNGGSFGRGDSDEWTFGAQMEIWW
- Number of residues
- 446
- Molecular Weight
- 49912.005
- Theoretical pI
- 4.58
- GO Classification
- Functionsmaltodextrin transmembrane transporter activity / maltose transporting porin activity / porin activity / virus receptor activityProcessescellular response to DNA damage stimulus / ion transport / maltodextrin transport / transmembrane transportComponentscell outer membrane / integral component of cell outer membrane / pore complex
- General Function
- Virus receptor activity
- Specific Function
- Involved in the transport of maltose and maltodextrins, indispensable for translocation of dextrins containing more than three glucosyl moieties. A hydrophobic path ("greasy slide") of aromatic residues serves to guide and select the sugars for transport through the channel. Also acts as a receptor for several bacteriophages including lambda.
- Pfam Domain Function
- LamB (PF02264)
- Transmembrane Regions
- 27-35 65-78 81-93 105-115 123-130 149-159 162-173 192-205 210-222 235-248 251-263 291-305 308-323 327-341 344-359 363-378 386-400 431-445
- Cellular Location
- Cell outer membrane
- Gene sequence
>lcl|BSEQ0020671|Maltoporin (lamB) ATGATGATTACTCTGCGCAAACTTCCTCTGGCGGTTGCCGTCGCAGCGGGCGTAATGTCT GCTCAGGCAATGGCTGTTGATTTCCACGGCTATGCACGTTCCGGTATTGGTTGGACAGGT AGCGGCGGTGAACAACAGTGTTTCCAGACTACCGGTGCTCAAAGTAAATACCGTCTTGGC AACGAATGTGAAACTTATGCTGAATTAAAATTGGGTCAGGAAGTGTGGAAAGAGGGCGAT AAGAGCTTCTATTTCGACACTAACGTGGCCTATTCCGTCGCACAACAGAATGACTGGGAA GCTACCGATCCGGCCTTCCGTGAAGCAAACGTGCAGGGTAAAAACCTGATCGAATGGCTG CCAGGCTCCACCATCTGGGCAGGTAAGCGCTTCTACCAACGTCATGACGTTCATATGATC GACTTCTACTACTGGGATATTTCTGGTCCTGGTGCCGGTCTGGAAAACATCGATGTTGGC TTCGGTAAACTCTCTCTGGCAGCAACCCGCTCCTCTGAAGCTGGTGGTTCTTCCTCTTTC GCCAGCAACAATATTTATGACTATACCAACGAAACCGCGAACGACGTTTTCGATGTGCGT TTAGCGCAGATGGAAATCAACCCGGGCGGCACATTAGAACTGGGTGTCGACTACGGTCGT GCCAACTTGCGTGATAACTATCGTCTGGTTGATGGCGCATCGAAAGACGGCTGGTTATTC ACTGCTGAACATACTCAGAGTGTCCTGAAGGGCTTTAACAAGTTTGTTGTTCAGTACGCT ACTGACTCGATGACCTCGCAGGGTAAAGGGCTGTCGCAGGGTTCTGGCGTTGCATTTGAT AACGAAAAATTTGCCTACAATATCAACAACAACGGTCACATGCTGCGTATCCTCGACCAC GGTGCGATCTCCATGGGCGACAACTGGGACATGATGTACGTGGGTATGTACCAGGATATC AACTGGGATAACGACAACGGCACCAAGTGGTGGACCGTCGGTATTCGCCCGATGTACAAG TGGACGCCAATCATGAGCACCGTGATGGAAATCGGCTACGACAACGTCGAATCCCAGCGC ACCGGCGACAAGAACAATCAGTACAAAATTACCCTCGCACAACAATGGCAGGCTGGCGAC AGCATCTGGTCACGCCCGGCTATTCGTGTCTTCGCAACCTACGCCAAGTGGGATGAGAAA TGGGGTTACGACTACACCGGTAACGCTGATAACAACGCGAACTTCGGCAAAGCCGTTCCT GCTGATTTCAACGGCGGCAGCTTCGGTCGTGGCGACAGCGACGAGTGGACCTTCGGTGCC CAGATGGAAATCTGGTGGTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P02943 UniProtKB Entry Name LAMB_ECOLI GenBank Gene ID M26131 - General References
- Clement JM, Hofnung M: Gene sequence of the lambda receptor, an outer membrane protein of E. coli K12. Cell. 1981 Dec;27(3 Pt 2):507-14. [Article]
- Blattner FR, Burland V, Plunkett G 3rd, Sofia HJ, Daniels DL: Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes. Nucleic Acids Res. 1993 Nov 25;21(23):5408-17. [Article]
- Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
- Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
- Heine HG, Kyngdon J, Ferenci T: Sequence determinants in the lamB gene of Escherichia coli influencing the binding and pore selectivity of maltoporin. Gene. 1987;53(2-3):287-92. [Article]
- Clement JM, Hedgpeth J, Hofnung M: [DNA sequence encoding the signal peptide of the lambda receptor in E. coli K 12]. C R Seances Acad Sci D. 1979 Nov 26;289(14):1033-6. [Article]
- Hedgpeth J, Clement JM, Marchal C, Perrin D, Hofnung M: DNA sequence encoding the NH2-terminal peptide involved in transport of lambda receptor, an Escherichia coli secretory protein. Proc Natl Acad Sci U S A. 1980 May;77(5):2621-5. [Article]
- Heine HG, Francis G, Lee KS, Ferenci T: Genetic analysis of sequences in maltoporin that contribute to binding domains and pore structure. J Bacteriol. 1988 Apr;170(4):1730-8. [Article]
- Luckey M, Ling R, Dose A, Malloy B: Role of a disulfide bond in the thermal stability of the LamB protein trimer in Escherichia coli outer membrane. J Biol Chem. 1991 Jan 25;266(3):1866-71. [Article]
- Charbit A, Ronco J, Michel V, Werts C, Hofnung M: Permissive sites and topology of an outer membrane protein with a reporter epitope. J Bacteriol. 1991 Jan;173(1):262-75. [Article]
- Klebba PE, Hofnung M, Charbit A: A model of maltodextrin transport through the sugar-specific porin, LamB, based on deletion analysis. EMBO J. 1994 Oct 3;13(19):4670-5. [Article]
- Van Gelder P, Dutzler R, Dumas F, Koebnik R, Schirmer T: Sucrose transport through maltoporin mutants of Escherichia coli. Protein Eng. 2001 Nov;14(11):943-8. [Article]
- Stenberg F, Chovanec P, Maslen SL, Robinson CV, Ilag LL, von Heijne G, Daley DO: Protein complexes of the Escherichia coli cell envelope. J Biol Chem. 2005 Oct 14;280(41):34409-19. Epub 2005 Aug 3. [Article]
- Schirmer T, Keller TA, Wang YF, Rosenbusch JP: Structural basis for sugar translocation through maltoporin channels at 3.1 A resolution. Science. 1995 Jan 27;267(5197):512-4. [Article]
- Dutzler R, Wang YF, Rizkallah P, Rosenbusch JP, Schirmer T: Crystal structures of various maltooligosaccharides bound to maltoporin reveal a specific sugar translocation pathway. Structure. 1996 Feb 15;4(2):127-34. [Article]
- Wang YF, Dutzler R, Rizkallah PJ, Rosenbusch JP, Schirmer T: Channel specificity: structural basis for sugar discrimination and differential flux rates in maltoporin. J Mol Biol. 1997 Sep 12;272(1):56-63. [Article]