Phosphate-binding protein PstS

Details

Name
Phosphate-binding protein PstS
Synonyms
  • PBP
  • phoS
Gene Name
pstS
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0019222|Phosphate-binding protein PstS
MKVMRTTVATVVAATLSMSAFSVFAEASLTGAGATFPAPVYAKWADTYQKETGNKVNYQG
IGSSGGVKQIIANTVDFGASDAPLSDEKLAQEGLFQFPTVIGGVVLAVNIPGLKSGELVL
DGKTLGDIYLGKIKKWDDEAIAKLNPGLKLPSQNIAVVRRADGSGTSFVFTSYLAKVNEE
WKNNVGTGSTVKWPIGLGGKGNDGIAAFVQRLPGAIGYVEYAYAKQNNLAYTKLISADGK
PVSPTEENFANAAKGADWSKTFAQDLTNQKGEDAWPITSTTFILIHKDQKKPEQGTEVLK
FFDWAYKTGAKQANDLDYASLPDSVVEQVRAAWKTNIKDSSGKPLY
Number of residues
346
Molecular Weight
37023.665
Theoretical pI
8.97
GO Classification
Functions
phosphate ion binding / phosphate ion transmembrane-transporting ATPase activity
Processes
cellular response to DNA damage stimulus / cellular response to phosphate starvation / phosphate ion transport
Components
ATP-binding cassette (ABC) transporter complex / periplasmic space / plasma membrane
General Function
Phosphate ion transmembrane-transporting atpase activity
Specific Function
Part of the ABC transporter complex PstSACB involved in phosphate import.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Periplasm
Gene sequence
>lcl|BSEQ0019223|Phosphate-binding protein PstS (pstS)
ATGAAAGTTATGCGTACCACCGTCGCAACTGTTGTCGCCGCGACCTTATCGATGAGTGCT
TTCTCTGTGTTTGCAGAAGCAAGCCTGACAGGTGCAGGTGCAACCTTCCCTGCGCCGGTG
TATGCCAAATGGGCTGACACTTACCAGAAAGAAACCGGTAATAAAGTTAACTACCAGGGT
ATCGGTTCTTCCGGTGGCGTAAAACAGATTATCGCTAATACCGTTGATTTTGGTGCCTCT
GACGCGCCGCTGTCTGACGAAAAACTGGCTCAGGAAGGTCTGTTCCAGTTCCCGACCGTG
ATTGGCGGCGTGGTGCTGGCGGTTAACATTCCAGGGCTGAAGTCTGGCGAACTGGTGCTG
GATGGTAAAACCCTCGGCGACATCTACCTGGGCAAAATCAAGAAGTGGGATGATGAAGCC
ATCGCCAAACTGAATCCGGGTCTGAAACTGCCTTCACAAAACATTGCTGTAGTACGCCGC
GCAGATGGCTCCGGGACTTCCTTCGTCTTCACCAGCTACCTGGCGAAAGTGAACGAAGAG
TGGAAAAACAACGTTGGTACTGGCTCTACCGTAAAATGGCCGATCGGTCTGGGCGGTAAA
GGTAACGACGGTATCGCCGCGTTCGTTCAGCGTCTGCCGGGTGCAATTGGTTATGTTGAA
TATGCTTACGCGAAGCAGAACAACCTGGCGTACACCAAACTGATCTCCGCTGATGGTAAA
CCGGTTAGTCCGACCGAAGAAAACTTCGCTAATGCAGCAAAAGGTGCAGACTGGAGCAAA
ACCTTCGCTCAGGATCTGACCAACCAGAAAGGCGAAGATGCATGGCCTATTACCTCTACC
ACGTTCATTCTGATCCACAAAGATCAGAAGAAACCAGAACAAGGCACAGAAGTGCTGAAA
TTCTTCGACTGGGCGTACAAAACCGGGGCTAAACAGGCGAACGACCTGGATTACGCCAGC
CTGCCGGATAGTGTAGTTGAACAGGTTCGCGCTGCGTGGAAGACCAATATTAAAGACAGT
AGCGGTAAGCCGCTGTACTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP0AG82
UniProtKB Entry NamePSTS_ECOLI
GenBank Gene IDK01992
General References
  1. Surin BP, Jans DA, Fimmel AL, Shaw DC, Cox GB, Rosenberg H: Structural gene for the phosphate-repressible phosphate-binding protein of Escherichia coli has its own promoter: complete nucleotide sequence of the phoS gene. J Bacteriol. 1984 Mar;157(3):772-8. [Article]
  2. Magota K, Otsuji N, Miki T, Horiuchi T, Tsunasawa S, Kondo J, Sakiyama F, Amemura M, Morita T, Shinagawa H, et al.: Nucleotide sequence of the phoS gene, the structural gene for the phosphate-binding protein of Escherichia coli. J Bacteriol. 1984 Mar;157(3):909-17. [Article]
  3. Burland V, Plunkett G 3rd, Daniels DL, Blattner FR: DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication. Genomics. 1993 Jun;16(3):551-61. [Article]
  4. 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]
  5. 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]
  6. 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]
  7. Luecke H, Quiocho FA: High specificity of a phosphate transport protein determined by hydrogen bonds. Nature. 1990 Sep 27;347(6291):402-6. [Article]
  8. Wang Z, Luecke H, Yao N, Quiocho FA: A low energy short hydrogen bond in very high resolution structures of protein receptor--phosphate complexes. Nat Struct Biol. 1997 Jul;4(7):519-22. [Article]
  9. Hirshberg M, Henrick K, Haire LL, Vasisht N, Brune M, Corrie JE, Webb MR: Crystal structure of phosphate binding protein labeled with a coumarin fluorophore, a probe for inorganic phosphate. Biochemistry. 1998 Jul 21;37(29):10381-5. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB02799N-[2-(1-maleimidyl)ethyl]-7-diethylaminocoumarin-3-carboxamideexperimentalunknownDetails
DB02831DihydrogenphosphateexperimentalunknownDetails