Spermidine/putrescine-binding periplasmic protein
Details
- Name
- Spermidine/putrescine-binding periplasmic protein
- Synonyms
- SPBP
- Gene Name
- potD
- Organism
- Escherichia coli (strain K12)
- Amino acid sequence
>lcl|BSEQ0011465|Spermidine/putrescine-binding periplasmic protein MKKWSRHLLAAGALALGMSAAHADDNNTLYFYNWTEYVPPGLLEQFTKETGIKVIYSTYE SNETMYAKLKTYKDGAYDLVVPSTYYVDKMRKEGMIQKIDKSKLTNFSNLDPDMLNKPFD PNNDYSIPYIWGATAIGVNGDAVDPKSVTSWADLWKPEYKGSLLLTDDAREVFQMALRKL GYSGNTTDPKEIEAAYNELKKLMPNVAAFNSDNPANPYMEGEVNLGMIWNGSAFVARQAG TPIDVVWPKEGGIFWMDSLAIPANAKNKEGALKLINFLLRPDVAKQVAETIGYPTPNLAA RKLLSPEVANDKTLYPDAETIKNGEWQNDVGAASSIYEEYYQKLKAGR
- Number of residues
- 348
- Molecular Weight
- 38866.745
- Theoretical pI
- 5.0
- GO Classification
- Functionspolyamine binding / polyamine-transporting ATPase activityProcessespolyamine transmembrane transport / polyamine transportComponentsouter membrane-bounded periplasmic space
- General Function
- Polyamine-transporting atpase activity
- Specific Function
- Required for the activity of the bacterial periplasmic transport system of putrescine and spermidine. Polyamine binding protein.
- Pfam Domain Function
- SBP_bac_1 (PF01547)
- Transmembrane Regions
- Not Available
- Cellular Location
- Periplasm
- Gene sequence
>lcl|BSEQ0011466|Spermidine/putrescine-binding periplasmic protein (potD) ATGAAAAAATGGTCACGCCACCTGCTCGCGGCGGGTGCTCTGGCACTGGGCATGAGCGCC GCTCACGCCGATGACAACAACACGCTGTATTTCTACAACTGGACCGAGTACGTGCCGCCA GGACTGCTTGAACAGTTCACCAAAGAAACCGGTATTAAGGTTATCTATTCGACTTACGAG TCGAACGAAACCATGTACGCCAAGCTGAAAACATACAAAGACGGTGCCTATGATCTGGTG GTTCCTTCAACCTATTACGTTGATAAAATGCGTAAAGAAGGGATGATCCAGAAGATCGAC AAGTCGAAGTTAACAAACTTCAGCAATCTCGATCCAGACATGCTCAACAAGCCTTTTGAC CCGAATAACGACTACTCCATTCCGTATATCTGGGGTGCGACGGCGATTGGTGTTAACGGT GATGCGGTGGATCCGAAATCTGTCACCAGCTGGGCCGATCTGTGGAAGCCAGAGTACAAA GGCAGCCTGCTGTTGACCGACGATGCCCGTGAAGTGTTCCAGATGGCGCTGCGTAAGCTG GGCTACTCCGGTAACACCACCGATCCGAAAGAGATTGAAGCTGCATATAACGAGCTGAAA AAACTGATGCCAAACGTGGCAGCCTTTAACTCCGATAACCCGGCGAACCCGTACATGGAA GGCGAAGTTAACCTCGGCATGATCTGGAACGGTTCTGCTTTCGTTGCACGCCAGGCGGGT ACGCCAATTGACGTGGTGTGGCCGAAAGAAGGCGGCATTTTCTGGATGGACAGCCTGGCG ATCCCGGCAAATGCCAAAAACAAAGAAGGCGCGCTGAAATTGATCAACTTCCTGCTGCGC CCGGATGTGGCAAAACAGGTTGCTGAAACTATCGGTTATCCAACGCCAAACCTTGCGGCG CGTAAGCTGTTAAGTCCAGAAGTGGCGAACGATAAAACACTCTACCCGGATGCTGAAACC ATTAAAAATGGCGAATGGCAGAATGACGTTGGCGCAGCCAGCAGCATTTATGAAGAGTAT TATCAGAAGCTGAAAGCAGGACGTTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P0AFK9 UniProtKB Entry Name POTD_ECOLI GenBank Gene ID M64519 - General References
- Furuchi T, Kashiwagi K, Kobayashi H, Igarashi K: Characteristics of the gene for a spermidine and putrescine transport system that maps at 15 min on the Escherichia coli chromosome. J Biol Chem. 1991 Nov 5;266(31):20928-33. [Article]
- 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 al.: 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. 1996 Jun 30;3(3):137-55. [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]
- 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]
- Matsuo Y, Nishikawa K: Prediction of the structural similarity between spermidine/putrescine-binding protein and maltose-binding protein. FEBS Lett. 1994 May 23;345(1):23-6. [Article]
- Sugiyama S, Vassylyev DG, Matsushima M, Kashiwagi K, Igarashi K, Morikawa K: Crystal structure of PotD, the primary receptor of the polyamine transport system in Escherichia coli. J Biol Chem. 1996 Apr 19;271(16):9519-25. [Article]
- Sugiyama S, Matsuo Y, Maenaka K, Vassylyev DG, Matsushima M, Kashiwagi K, Igarashi K, Morikawa K: The 1.8-A X-ray structure of the Escherichia coli PotD protein complexed with spermidine and the mechanism of polyamine binding. Protein Sci. 1996 Oct;5(10):1984-90. [Article]