TCDB is operated by the Saier Lab Bioinformatics Group
« See all members of the family


3.A.1.7.1
Phosphate porter, PhoSPstABC.  Serves as both a transporter and a sensor for transcriptional activation of the pho regulon in the presence of low external phosphate.  The unphosphorylated EIIANtr protein of the PTS (TC# 4.A) activates PhoR, the senor kinase that phosphorylates the response regulator, PhoB, that activates the pho regulon (Lüttmann et al. 2012).

Accession Number:P0AG82
Protein Name:Phosphate-binding protein PstS aka PhoS aka B3728
Length:346
Molecular Weight:37024.00
Species:Escherichia coli [83333]
Number of TMSs:1
Location1 / Topology2 / Orientation3: Periplasm1
Substrate phosphate

Cross database links:

Genevestigator: P0AG82
EchoBASE: EB0727
EcoGene: EG10734
eggNOG: COG0226
HEGENOM: HBG428828
DIP: DIP-48241N
RefSeq: AP_004059.1    NP_418184.1   
Entrez Gene ID: 948237   
Pfam: PF01547   
Drugbank: Drugbank Link   
BioCyc: EcoCyc:PSTS-MONOMER    ECOL168927:B3728-MONOMER   
KEGG: ecj:JW3706    eco:b3728   

Gene Ontology

GO:0042597 C:periplasmic space
GO:0005315 F:inorganic phosphate transmembrane transport...
GO:0006817 P:phosphate transport
GO:0006950 P:response to stress

References (9)

[1] “Structural gene for the phosphate-repressible phosphate-binding protein of Escherichia coli has its own promoter: complete nucleotide sequence of the phoS gene.”  Surin B.P.et.al.   6321434
[2] “Nucleotide sequence of the phoS gene, the structural gene for the phosphate-binding protein of Escherichia coli.”  Magota K.et.al.   6365894
[3] “DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication.”  Burland V.D.et.al.   7686882
[4] “The complete genome sequence of Escherichia coli K-12.”  Blattner F.R.et.al.   9278503
[5] “Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.”  Hayashi K.et.al.   16738553
[6] “Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.”  Link A.J.et.al.   9298646
[7] “High specificity of a phosphate transport protein determined by hydrogen bonds.”  Luecke H.et.al.   2215649
[8] “A low energy short hydrogen bond in very high resolution structures of protein receptor-phosphate complexes.”  Wang Z.et.al.   9228942
[9] “Crystal structure of phosphate binding protein labeled with a coumarin fluorophore, a probe for inorganic phosphate.”  Hirshberg M.et.al.   9671506
Structure:
1A40   1A54   1A55   1IXG   1IXH   1IXI   1OIB   1PBP   1QUI   1QUJ   [...more]

External Searches:

  • Search: DB with
  • BLAST ExPASy (Swiss Institute of Bioinformatics (SIB) BLAST)
  • CDD Search (Conserved Domain Database)
  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)

Analyze:

Predict TMSs (Predict number of transmembrane segments)
Window Size: Angle:  
Window Size: Angle:  
FASTA formatted sequence
1:	MKVMRTTVAT VVAATLSMSA FSVFAEASLT GAGATFPAPV YAKWADTYQK ETGNKVNYQG 
61:	IGSSGGVKQI IANTVDFGAS DAPLSDEKLA QEGLFQFPTV IGGVVLAVNI PGLKSGELVL 
121:	DGKTLGDIYL GKIKKWDDEA IAKLNPGLKL PSQNIAVVRR ADGSGTSFVF TSYLAKVNEE 
181:	WKNNVGTGST VKWPIGLGGK GNDGIAAFVQ RLPGAIGYVE YAYAKQNNLA YTKLISADGK 
241:	PVSPTEENFA NAAKGADWSK TFAQDLTNQK GEDAWPITST TFILIHKDQK KPEQGTEVLK 
301:	FFDWAYKTGA KQANDLDYAS LPDSVVEQVR AAWKTNIKDS SGKPLY