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Escherichia coli K-12 substr. MG1655 Polypeptide: phosphoenolpyruvate-protein phosphotransferase PtsP, enzyme INtr



Gene: ptsP Accession Numbers: EG12188 (EcoCyc), b2829, ECK2825

Synonyms: ygdO, manY, ygdF, EINtr, EInitrogen

Regulation Summary Diagram: ?

Alternative forms of phosphoenolpyruvate-protein phosphotransferase PtsP, enzyme INtr: PtsP-phosphorylated (summary available)

Summary:
PtsP, also known as EINtr, is the first enzyme of the nitrogen phosphotransferase system (PTS Ntr) in E. coli K-12. The PTS Ntr system consisting of the three cytoplasmic proteins PtsP, PtsO and PtsN is believed to respond to nitrogen availability and is paralogous to the well-characterised PTSsugar.

PtsP contains an N-terminal 127 amino acid GAF domain attached to a larger C-terminal Enzyme I domain [Reizer96d]. Autophosphorylation of PtsP by PEP in vitro is inhibited by glutamine and stimulated by α-ketoglutarate. PtsP lacking the N-terminal GAF domain is insensitive to these effectors [Lee13e]. PtsP catalyses phosphoryl transfer from phosphoenolpyruvate (PEP) to PtsO (also known as NPr) in vitro. This reaction occurs at an optimum pH of 8.0, is dependent on Mg2+, is stimulated by high ionic strength, and has two Km values for NPr of 2 and 10 μM [Rabus99].

ptsP mutants are more resistant than the wild-type to leucine-containing peptides [Lee05j].

Locations: cytosol

Map Position: [2,964,210 <- 2,966,456] (63.89 centisomes)
Length: 2247 bp / 748 aa

Molecular Weight of Polypeptide: 83.716 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0009274 , EchoBASE:EB2105 , EcoGene:EG12188 , EcoliWiki:b2829 , ModBase:P37177 , OU-Microarray:b2829 , PortEco:ptsP , PR:PRO_000023636 , Pride:P37177 , Protein Model Portal:P37177 , RefSeq:NP_417306 , RegulonDB:EG12188 , SMR:P37177 , String:511145.b2829 , Swiss-Model:P37177 , UniProt:P37177

Relationship Links: InterPro:IN-FAMILY:IPR000121 , InterPro:IN-FAMILY:IPR003018 , InterPro:IN-FAMILY:IPR006318 , InterPro:IN-FAMILY:IPR008279 , InterPro:IN-FAMILY:IPR008731 , InterPro:IN-FAMILY:IPR015813 , InterPro:IN-FAMILY:IPR018274 , InterPro:IN-FAMILY:IPR023151 , Panther:IN-FAMILY:PTHR22931:SF10 , Pfam:IN-FAMILY:PF00391 , Pfam:IN-FAMILY:PF01590 , Pfam:IN-FAMILY:PF02896 , Pfam:IN-FAMILY:PF05524 , Prints:IN-FAMILY:PR01736 , Prosite:IN-FAMILY:PS00370 , Prosite:IN-FAMILY:PS00742 , Smart:IN-FAMILY:SM00065

In Paralogous Gene Group: 259 (4 members) , 336 (3 members)

In Reactions of unknown directionality:

Not in pathways:
PtsP-phosphorylated + Npr = Npr phosphorylated + PtsP
phosphoenolpyruvate + PtsP = pyruvate + PtsP-phosphorylated

GO Terms:

Biological Process: GO:0006468 - protein phosphorylation Inferred from experiment [Lee13e]
GO:0010243 - response to organonitrogen compound Inferred from experiment [Lee13e]
GO:0006810 - transport Inferred by computational analysis [UniProtGOA11a]
GO:0008643 - carbohydrate transport Inferred by computational analysis [UniProtGOA11a]
GO:0009401 - phosphoenolpyruvate-dependent sugar phosphotransferase system Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0016310 - phosphorylation Inferred by computational analysis [UniProtGOA11a, GOA01a]
Molecular Function: GO:0008965 - phosphoenolpyruvate-protein phosphotransferase activity Inferred from experiment Inferred by computational analysis [GOA01, Rabus99]
GO:0003824 - catalytic activity Inferred by computational analysis [GOA01a]
GO:0016301 - kinase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016772 - transferase activity, transferring phosphorus-containing groups Inferred by computational analysis [GOA01a]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005737 - cytoplasm Inferred by computational analysis [UniProtGOA11, UniProtGOA11a]
GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]

MultiFun Terms: metabolism metabolism of other compounds nitrogen metabolism

Essentiality data for ptsP knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

Credits:
Last-Curated ? 22-Apr-2013 by Mackie A , Macquarie University


Sequence Features

Feature Class Location Citations Comment
Conserved-Region 1 -> 127
[UniProt09]
UniProt: GAF;
Protein-Segment 128 -> 170
[UniProt10]
UniProt: Linker; Sequence Annotation Type: region of interest;
Protein-Segment 171 -> 748
[UniProt10]
UniProt: PTS EI; Sequence Annotation Type: region of interest;
Active-Site 356
[UniProt13]
UniProt: Tele-phosphohistidine intermediate; Non-Experimental Qualifier: by similarity.
Phosphorylation-Modification 356
[UniProt10]
UniProt: Tele-phosphohistidine intermediate; Non-Experimental Qualifier: by similarity;
Amino-Acid-Sites-That-Bind 462
[UniProt10]
UniProt: Substrate; Non-Experimental Qualifier: by similarity;
Amino-Acid-Sites-That-Bind 498
[UniProt10]
UniProt: Substrate; Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 597
[UniProt10]
UniProt: Magnesium; Non-Experimental Qualifier: by similarity;
Amino-Acid-Sites-That-Bind 618
[UniProt10]
UniProt: Substrate; via carbonyl oxygen; Non-Experimental Qualifier: by similarity;
Amino-Acid-Sites-That-Bind 619
[UniProt10]
UniProt: Substrate; via amide nitrogen; Non-Experimental Qualifier: by similarity;
Amino-Acid-Sites-That-Bind 620
[UniProt10]
UniProt: Substrate; Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 621
[UniProt10]
UniProt: Magnesium; Non-Experimental Qualifier: by similarity;
Active-Site 668
[UniProt10]
UniProt: Proton donor; Non-Experimental Qualifier: by similarity;


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
1/26/1998 (pkarp) Merged genes G7981/ptsP and EG12188/ygdF


References

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

GOA01: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Lee05j: Lee CR, Koo BM, Cho SH, Kim YJ, Yoon MJ, Peterkofsky A, Seok YJ (2005). "Requirement of the dephospho-form of enzyme IIANtr for derepression of Escherichia coli K-12 ilvBN expression." Mol Microbiol 58(1);334-44. PMID: 16164569

Lee13e: Lee CR, Park YH, Kim M, Kim YR, Park S, Peterkofsky A, Seok YJ (2013). "Reciprocal regulation of the autophosphorylation of enzyme INtr by glutamine and α-ketoglutarate in Escherichia coli." Mol Microbiol 88(3);473-85. PMID: 23517463

Rabus99: Rabus R, Reizer J, Paulsen I, Saier MH (1999). "Enzyme I(Ntr) from Escherichia coli. A novel enzyme of the phosphoenolpyruvate-dependent phosphotransferase system exhibiting strict specificity for its phosphoryl acceptor, NPr." J Biol Chem 274(37);26185-91. PMID: 10473571

Reizer96d: Reizer J, Reizer A, Merrick MJ, Plunkett G, Rose DJ, Saier MH (1996). "Novel phosphotransferase-encoding genes revealed by analysis of the Escherichia coli genome: a chimeric gene encoding an Enzyme I homologue that possesses a putative sensory transduction domain." Gene 181(1-2);103-8. PMID: 8973315

UniProt09: UniProt Consortium (2009). "UniProt version 15.8 released on 2009-10-01 00:00:00." Database.

UniProt10: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProt13: UniProt Consortium (2013). "UniProt version 2013-08 released on 2013-08-01 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

Other References Related to Gene Regulation

Raghavan11: Raghavan R, Sage A, Ochman H (2011). "Genome-wide identification of transcription start sites yields a novel thermosensing RNA and new cyclic AMP receptor protein-regulated genes in Escherichia coli." J Bacteriol 193(11);2871-4. PMID: 21460078


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Sat Nov 22, 2014, biocyc13.