Reviewed, UniProtKB/Swiss-Prot P37177 (PT1P_ECOLI)

Names and origin

Protein names

Recommended name:
    Phosphoenolpyruvate-protein phosphotransferase ptsP
    EC=2.7.3.9
Alternative name(s):
    Phosphotransferase system, enzyme I
    Enzyme I-Ntr

Gene names

Name:	ptsP
Synonyms:	ygdF, ygdO
Ordered Locus Names:	b2829, JW2797

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	748 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Component of the phosphoenolpyruvate-dependent nitrogen-metabolic phosphotransferase system (nitrogen-metabolic PTS), that seems to be involved in regulating nitrogen metabolism. Enzyme I-Ntr transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (NPr). Could function in the transcriptional regulation of sigma-54 dependent operons in conjunction with the NPr (ptsO) and EIIA-Ntr (ptsN) proteins. Ref.5
Catalytic activity	Phosphoenolpyruvate + protein L-histidine = pyruvate + protein N(pi)-phospho-L-histidine.
Cofactor	Magnesium By similarity.
Subcellular location	Cytoplasm Probable.
Domain	The EI N-terminal domain contains the HPr binding site, the central domain the pyrophosphate/phosphate carrier histidine, and the C-terminal domain the pyruvate binding site By similarity. The GAF domain is an important site of signal perception in prokaryotes and eukaryotes.
Miscellaneous	The reaction takes place in three steps, mediated by a phosphocarrier histidine residue located on the surface of the central domain. The two first partial reactions are catalyzed at an active site located on the N-terminal domain, and the third partial reaction is catalyzed at an active site located on the C-terminal domain. For catalytic turnover, the central domain swivels from the concave surface of the N-terminal domain to that of the C-terminal domain By similarity.
Sequence similarities	Belongs to the PEP-utilizing enzyme family. Contains 1 GAF domain.

Ontologies

Keywords
Biological process	Phosphotransferase system Sugar transport Transport
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding
Molecular function	Kinase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	phosphoenolpyruvate-dependent sugar phosphotransferase system Inferred from electronic annotation. Source: UniProtKB-KW phosphorylation Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	kinase activity Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoenolpyruvate-protein phosphotransferase activity Inferred from electronic annotation. Source: EC sugar:hydrogen symporter activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 748	748	Phosphoenolpyruvate-protein phosphotransferase ptsP		PRO_0000147095
Regions
	Domain	1 – 127	127	GAF
	Region	128 – 170	43	Linker
	Region	171 – 748	578	PTS EI
Sites
	Active site	356	1	Tele-phosphohistidine intermediate By similarity
	Active site	668	1	Proton donor By similarity
	Metal binding	597	1	Magnesium By similarity
	Metal binding	621	1	Magnesium By similarity
	Binding site	462	1	Substrate By similarity
	Binding site	498	1	Substrate By similarity
	Binding site	597	1	Substrate By similarity
	Binding site	618	1	Substrate; via carbonyl oxygen By similarity
	Binding site	619	1	Substrate; via amide nitrogen By similarity
	Binding site	620	1	Substrate By similarity
	Binding site	621	1	Substrate; via amide nitrogen By similarity

Sequences

	Sequence		Length	Mass (Da)
	P37177-1 [UniParc]. Last modified November 1, 1995. Version 2. Checksum: AC7137BD0AEBBF01	FASTA	748	83,716
	10 20 30 40 50 60 MLTRLREIVE KVASAPRLNE ALNILVTDIC LAMDTEVCSV YLADHDRRCY YLMATRGLKK 70 80 90 100 110 120 PRGRTVTLAF DEGIVGLVGR LAEPINLADA QKHPSFKYIP SVKEERFRAF LGVPIIQRRQ 130 140 150 160 170 180 LLGVLVVQQR ELRQYDESEE SFLVTLATQM AAILSQSQLT ALFGQYRQTR IRALPAAPGV 190 200 210 220 230 240 AIAEGWQDAT LPLMEQVYQA STLDPALERE RLTGALEEAA NEFRRYSKRF AAGAQKETAA 250 260 270 280 290 300 IFDLYSHLLS DTRLRRELFA EVDKGSVAEW AVKTVIEKFA EQFAALSDNY LKERAGDLRA 310 320 330 340 350 360 LGQRLLFHLD DANQGPNAWP ERFILVADEL SATTLAELPQ DRLVGVVVRD GAANSHAAIM 370 380 390 400 410 420 VRALGIPTVM GADIQPSVLH RRTLIVDGYR GELLVDPEPV LLQEYQRLIS EEIELSRLAE 430 440 450 460 470 480 DDVNLPAQLK SGERIKVMLN AGLSPEHEEK LGSRIDGIGL YRTEIPFMLQ SGFPSEEEQV 490 500 510 520 530 540 AQYQGMLQMF NDKPVTLRTL DVGADKQLPY MPISEENPCL GWRGIRITLD QPEIFLIQVR 550 560 570 580 590 600 AMLRANAATG NLNILLPMVT SLDEVDEARR LIERAGREVE EMIGYEIPKP RIGIMLEVPS 610 620 630 640 650 660 MVFMLPHLAK RVDFISVGTN DLTQYILAVD RNNTRVANIY DSLHPAMLRA LAMIAREAEI 670 680 690 700 710 720 HGIDLRLCGE MAGDPMCVAI LIGLGYRHLS MNGRSVARAK YLLRRIDYAE AENLAQRSLE 730 740 AQLATEVRHQ VAAFMERRGM GGLIRGGL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[2]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"The umpA gene of Escherichia coli encodes phosphatidylglycerol:prolipoprotein diacylglyceryl transferase (lgt) and regulates thymidylate synthase levels through translational coupling." Gan K., Sankaran K., Williams M.G., Aldea M., Rudd K.E., Kushner S.R., Wu H.C. J. Bacteriol. 177:1879-1882(1995) [PubMed: 7896715] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 656-748.
[4]	"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." Reizer J., Reizer A., Merrick M.J., Plunkett G. III, Rose D.J., Saier M.H. Jr. Gene 181:103-108(1996) [PubMed: 8973315] [Abstract] Cited for: DISCUSSION OF SEQUENCE.
[5]	"Enzyme I(Ntr) from Escherichia coli. A novel enzyme of the phosphoenolpyruvate-dependent phosphotransferase system exhibiting strict specificity for its phosphoryl acceptor, NPr." Rabus R., Reizer J., Paulsen I., Saier M.H. Jr. J. Biol. Chem. 274:26185-26191(1999) [PubMed: 10473571] [Abstract] Cited for: FUNCTION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U29581 Genomic DNA. Translation: AAB40476.1. U00096 Genomic DNA. Translation: AAC75868.1. AP009048 Genomic DNA. Translation: BAE76898.1. U12289 Genomic DNA. Translation: AAA69023.1.
PIR	F65065.
RefSeq	AP_003392.1. NP_417306.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	P37177.
Proteomic databases
PRIDE	P37177.
Genome annotation databases
GeneID	947301.
GenomeReviews	Gene locus JW2797 in contig AP009048_GR. Gene locus b2829 in contig U00096_GR.
KEGG	ecj:JW2797. eco:b2829.
Organism-specific databases
EchoBASE	EB2105.
EcoGene	EG12188. ptsP.
CMR	Search...
Phylogenomic databases
HOGENOM	P37177.
OMA	LVGQREE.
Enzyme and pathway databases
BioCyc	EcoCyc:EG12188-MON.
Gene expression databases
Genevestigator	P37177.
Family and domain databases
InterPro	IPR003018. GAF. IPR008279. PEP_mobile. IPR018274. PEP_mobile_CS. IPR006318. PEP_P_trans. IPR000121. PEP_utilizers. IPR008731. PTS_PEP_utilis_N. IPR015813. Pyrv/PenolPyrv_Kinase_cat. [Graphical view]
Gene3D	G3DSA:3.50.30.10. PEP_mobile. 1 hit. G3DSA:1.10.274.10. PTS_PEP_utilis_N. 1 hit. G3DSA:3.20.20.60. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
Pfam	PF01590. GAF. 1 hit. PF05524. PEP-utilisers_N. 1 hit. PF00391. PEP-utilizers. 1 hit. PF02896. PEP-utilizers_C. 1 hit. [Graphical view]
PRINTS	PR01736. PHPHTRNFRASE.
ProDom	PD000940. PEP_utilizers. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00065. GAF. 1 hit. [Graphical view]
TIGRFAMs	TIGR01417. PTS_I_fam. 1 hit.
PROSITE	PS00742. PEP_ENZYMES_2. 1 hit. PS00370. PEP_ENZYMES_PHOS_SITE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PT1P_ECOLI

Accession

Primary (citable) accession number: P37177
Secondary accession number(s): Q2MA08

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	November 1, 1995
Last modified:	November 3, 2009
This is version 80 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)