L-arabinose-binding periplasmic protein

NameL-arabinose-binding periplasmic protein
Synonyms
  • ABP
Gene NamearaF
OrganismEscherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0011197|L-arabinose-binding periplasmic protein
MHKFTKALAAIGLAAVMSQSAMAENLKLGFLVKQPEEPWFQTEWKFADKAGKDLGFEVIK
IAVPDGEKTLNAIDSLAASGAKGFVICTPDPKLGSAIVAKARGYDMKVIAVDDQFVNAKG
KPMDTVPLVMMAATKIGERQGQELYKEMQKRGWDVKESAVMAITANELDTARRRTTGSMD
ALKAAGFPEKQIYQVPTKSNDIPGAFDAANSMLVQHPEVKHWLIVGMNDSTVLGGVRATE
GQGFKAADIIGIGINGVDAVSELSKAQATGFYGSLLPSPDVHGYKSSEMLYNWVAKDVEP
PKFTEVTDVVLITRDNFKEELEKKGLGGK
Number of residuesNone
Molecular Weight35540.67
Theoretical pI6.55
GO Classification
Functions
  • monosaccharide binding
  • monosaccharide-transporting ATPase activity
Processes
  • L-arabinose transport
  • monosaccharide transport
Components
  • outer membrane-bounded periplasmic space
General FunctionMonosaccharide-transporting atpase activity
Specific FunctionInvolved in the high-affinity L-arabinose membrane transport system. Binds with high affinity to arabinose, but can also bind D-galactose (approximately 2-fold reduction) and D-fucose (approximately 40-fold reduction).
Transmembrane Regions
GenBank Protein ID
UniProtKB IDP02924
UniProtKB Entry Name
Cellular LocationPeriplasm
Gene sequence
>lcl|BSEQ0011198|L-arabinose-binding periplasmic protein (araF)
ATGCACAAATTTACTAAAGCCCTGGCAGCCATTGGTCTGGCAGCCGTTATGTCACAATCC
GCTATGGCGGAGAACCTGAAGCTCGGTTTTCTGGTGAAGCAACCGGAAGAGCCGTGGTTC
CAGACCGAATGGAAGTTTGCCGATAAAGCCGGGAAGGATTTAGGGTTTGAGGTTATTAAG
ATTGCCGTGCCGGATGGCGAAAAAACATTGAACGCGATCGACAGCCTGGCTGCCAGTGGC
GCAAAAGGTTTCGTTATTTGTACTCCGGACCCCAAACTCGGCTCTGCCATCGTCGCGAAA
GCGCGTGGCTACGATATGAAAGTCATTGCCGTGGATGACCAGTTTGTTAACGCCAAAGGT
AAGCCAATGGATACCGTTCCGCTGGTGATGATGGCGGCGACTAAAATTGGCGAACGTCAG
GGCCAGGAACTGTATAAAGAGATGCAGAAACGTGGCTGGGATGTCAAAGAAAGCGCGGTG
ATGGCGATTACCGCCAACGAACTGGATACCGCCCGCCGCCGTACTACGGGATCTATGGAT
GCGCTGAAAGCGGCCGGATTCCCGGAAAAACAAATTTATCAGGTACCTACCAAATCTAAC
GACATCCCGGGGGCATTTGACGCTGCCAACTCAATGCTGGTTCAACATCCGGAAGTTAAA
CATTGGCTGATCGTCGGTATGAACGACAGCACCGTGCTGGGCGGCGTACGCGCGACGGAA
GGTCAGGGCTTTAAAGCGGCCGATATCATCGGCATTGGCATTAACGGTGTGGATGCGGTG
AGCGAACTGTCTAAAGCACAGGCAACCGGCTTCTACGGTTCCCTGCTGCCAAGCCCGGAC
GTACATGGCTATAAATCCAGCGAAATGCTTTACAACTGGGTAGCAAAAGACGTTGAACCG
CCAAAATTTACCGAAGTTACCGACGTGGTACTGATCACGCGTGACAACTTTAAAGAAGAA
CTGGAGAAAAAAGGTTTAGGCGGTAAGTAA
GenBank Gene ID
GeneCard IDNone
GenAtlas ID
HGNC ID
Chromosome LocationNone
LocusNone
References
  1. Scripture JB, Voelker C, Miller S, O'Donnell RT, Polgar L, Rade J, Horazdovsky BF, Hogg RW: High-affinity L-arabinose transport operon. Nucleotide sequence and analysis of gene products. J Mol Biol. 1987 Sep 5;197(1):37-46. [2445996 ]
  2. 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 al.: 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. 1996 Dec 31;3(6):379-92. [9097040 ]
  3. 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. [9278503 ]
  4. 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. [16738553 ]
  5. Scripture JB, Hogg RW: The nucleotide sequences defining the signal peptides of the galactose-binding protein and the arabinose-binding protein. J Biol Chem. 1983 Sep 25;258(18):10853-5. [6885805 ]
  6. Hogg RW, Hermodson MA: Amino acid sequence of the L-arabinose-binding protein from Escherichia coli B/r. J Biol Chem. 1977 Jul 25;252(14):5135-41. [326784 ]
  7. Link AJ, Robison K, Church GM: Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12. Electrophoresis. 1997 Aug;18(8):1259-313. [9298646 ]
  8. VanBogelen RA, Abshire KZ, Moldover B, Olson ER, Neidhardt FC: Escherichia coli proteome analysis using the gene-protein database. Electrophoresis. 1997 Aug;18(8):1243-51. [9298644 ]
  9. Newcomer ME, Gilliland GL, Quiocho FA: L-Arabinose-binding protein-sugar complex at 2.4 A resolution. Stereochemistry and evidence for a structural change. J Biol Chem. 1981 Dec 25;256(24):13213-7. [7031057 ]
  10. Quiocho FA, Gilliland GL, Phillips GN Jr: The 2.8-A resolution structure of the L-arabinose-binding protein from Escherichia coli. Polypeptide chain folding, domain similarity, and probable location of sugar-binding site. J Biol Chem. 1977 Jul 25;252(14):5142-9. [326785 ]
  11. Vermersch PS, Tesmer JJ, Lemon DD, Quiocho FA: A Pro to Gly mutation in the hinge of the arabinose-binding protein enhances binding and alters specificity. Sugar-binding and crystallographic studies. J Biol Chem. 1990 Sep 25;265(27):16592-603. [2204627 ]

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