L-arabinose-binding periplasmic protein
Details
- Name
- L-arabinose-binding periplasmic protein
- Synonyms
- ABP
- Gene Name
- araF
- Organism
- Escherichia coli (strain K12)
- Amino acid sequence
>lcl|BSEQ0011197|L-arabinose-binding periplasmic protein MHKFTKALAAIGLAAVMSQSAMAENLKLGFLVKQPEEPWFQTEWKFADKAGKDLGFEVIK IAVPDGEKTLNAIDSLAASGAKGFVICTPDPKLGSAIVAKARGYDMKVIAVDDQFVNAKG KPMDTVPLVMMAATKIGERQGQELYKEMQKRGWDVKESAVMAITANELDTARRRTTGSMD ALKAAGFPEKQIYQVPTKSNDIPGAFDAANSMLVQHPEVKHWLIVGMNDSTVLGGVRATE GQGFKAADIIGIGINGVDAVSELSKAQATGFYGSLLPSPDVHGYKSSEMLYNWVAKDVEP PKFTEVTDVVLITRDNFKEELEKKGLGGK
- Number of residues
- 329
- Molecular Weight
- 35540.67
- Theoretical pI
- 6.55
- GO Classification
- Functionsmonosaccharide binding / monosaccharide-transporting ATPase activityProcessesL-arabinose transport / monosaccharide transportComponentsouter membrane-bounded periplasmic space
- General Function
- Monosaccharide-transporting atpase activity
- Specific Function
- Involved 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).
- Pfam Domain Function
- Peripla_BP_1 (PF00532)
- Transmembrane Regions
- Not Available
- Cellular Location
- Periplasm
- 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
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P02924 UniProtKB Entry Name ARAF_ECOLI GenBank Protein ID 40944 GenBank Gene ID X06091 - General References
- 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. [Article]
- 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. [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]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]