P08839 (PT1_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphoenolpyruvate-protein phosphotransferase
EC=2.7.3.9

Alternative name(s):
Phosphotransferase system, enzyme I

Gene names

Name:	ptsI
Ordered Locus Names:	b2416, JW2409

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	575 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr). Ref.9
Catalytic activity	Phosphoenolpyruvate + protein L-histidine = pyruvate + protein N(pi)-phospho-L-histidine.
Cofactor	Magnesium.
Subunit structure	Homodimer. Ref.15
Subcellular location	Cytoplasm.
Domain	The 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.
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. Enzyme I of the sugar PTS has been shown in Ref.9 to phosphorylate NPr of the nitrogen-metabolic PTS, though much less efficiently than it does HPr. This process may link carbon and nitrogen assimilation.
Sequence similarities	Belongs to the PEP-utilizing enzyme family.

Ontologies

Keywords
Biological process	Phosphotransferase system Sugar transport Transport
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding
Molecular function	Kinase Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	phosphoenolpyruvate-dependent sugar phosphotransferase system Inferred from direct assay PubMed 6986909PubMed 6992959. Source: EcoCyc
Cellular_component	cytosol Inferred from direct assay PubMed 16858726. Source: UniProtKB phosphoenolpyruvate-dependent sugar phosphotransferase complex Inferred from direct assay PubMed 6986909PubMed 6992959. Source: EcoCyc
Molecular_function	kinase activity Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from direct assay Ref.15. Source: EcoCyc phosphoenolpyruvate-protein phosphotransferase activity Inferred from direct assay PubMed 6986909PubMed 6992959. Source: EcoCyc sugar:hydrogen symporter activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ptsH	P0AA04	1	EBI-551533,EBI-902853

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 575

575

Phosphoenolpyruvate-protein phosphotransferase

PRO_0000147067

Sites

Active site

189

1

Tele-phosphohistidine intermediate Ref.15

Active site

502

1

Proton donor Probable

Metal binding

431

1

Magnesium

Metal binding

455

1

Magnesium

Binding site

296

1

Substrate By similarity

Binding site

332

1

Substrate

Binding site

431

1

Substrate By similarity

Binding site

452

1

Substrate; via carbonyl oxygen By similarity

Binding site

453

1

Substrate; via amide nitrogen By similarity

Binding site

454

1

Substrate; via amide nitrogen

Binding site

455

1

Substrate; via amide nitrogen

Secondary structure

1

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575

Helix Strand Turn

Details...

Beta strand

5 – 8

4

Beta strand

12 – 18

7

Turn

33 – 35

3

Helix

36 – 65

30

Helix

67 – 80

14

Helix

83 – 96

14

Helix

100 – 112

13

Turn

113 – 115

3

Beta strand

116 – 118

3

Helix

121 – 142

22

Helix

149 – 151

3

Beta strand

156 – 159

4

Helix

165 – 170

6

Helix

173 – 175

3

Beta strand

176 – 180

5

Beta strand

183 – 185

3

Beta strand

186 – 188

3

Helix

189 – 197

9

Beta strand

201 – 203

3

Helix

208 – 211

4

Beta strand

217 – 220

4

Turn

222 – 225

4

Beta strand

227 – 230

4

Helix

233 – 239

7

Turn

240 – 243

4

Helix

244 – 247

4

Helix

254 – 256

3

Beta strand

270 – 277

8

Helix

279 – 286

8

Beta strand

290 – 296

7

Helix

297 – 301

5

Beta strand

304 – 306

3

Helix

310 – 323

14

Turn

324 – 326

3

Beta strand

329 – 332

4

Beta strand

337 – 339

3

Helix

343 – 345

3

Helix

353 – 355

3

Helix

360 – 363

4

Helix

367 – 380

14

Beta strand

386 – 392

7

Helix

396 – 415

20

Beta strand

425 – 430

6

Helix

433 – 437

5

Helix

439 – 443

5

Beta strand

447 – 451

5

Helix

453 – 461

9

Helix

468 – 473

6

Beta strand

476 – 478

3

Helix

479 – 494

16

Beta strand

498 – 501

4

Turn

504 – 507

4

Turn

509 – 511

3

Helix

512 – 517

6

Beta strand

522 – 525

4

Helix

527 – 529

3

Helix

530 – 538

9

Helix

542 – 554

13

Helix

558 – 572

15

Sequences

	Sequence		Length	Mass (Da)
	P08839 [UniParc]. Last modified November 1, 1988. Version 1. Checksum: 4278F0838855E950	FASTA	575	63,562
	10 20 30 40 50 60 MISGILASPG IAFGKALLLK EDEIVIDRKK ISADQVDQEV ERFLSGRAKA SAQLETIKTK 70 80 90 100 110 120 AGETFGEEKE AIFEGHIMLL EDEELEQEII ALIKDKHMTA DAAAHEVIEG QASALEELDD 130 140 150 160 170 180 EYLKERAADV RDIGKRLLRN ILGLKIIDLS AIQDEVILVA ADLTPSETAQ LNLKKVLGFI 190 200 210 220 230 240 TDAGGRTSHT SIMARSLELP AIVGTGSVTS QVKNDDYLIL DAVNNQVYVN PTNEVIDKMR 250 260 270 280 290 300 AVQEQVASEK AELAKLKDLP AITLDGHQVE VCANIGTVRD VEGAERNGAE GVGLYRTEFL 310 320 330 340 350 360 FMDRDALPTE EEQFAAYKAV AEACGSQAVI VRTMDIGGDK ELPYMNFPKE ENPFLGWRAI 370 380 390 400 410 420 RIAMDRREIL RDQLRAILRA SAFGKLRIMF PMIISVEEVR ALRKEIEIYK QELRDEGKAF 430 440 450 460 470 480 DESIEIGVMV ETPAAATIAR HLAKEVDFFS IGTNDLTQYT LAVDRGNDMI SHLYQPMSPS 490 500 510 520 530 540 VLNLIKQVID ASHAEGKWTG MCGELAGDER ATLLLLGMGL DEFSMSAISI PRIKKIIRNT 550 560 570 NFEDAKVLAE QALAQPTTDE LMTLVNKFIE EKTIC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The ptsH, ptsI, and crr genes of the Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system: a complex operon with several modes of transcription." de Reuse H., Danchin A. J. Bacteriol. 170:3827-3837(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Sugar transport by the bacterial phosphotransferase system. Molecular cloning and structural analysis of the Escherichia coli ptsH, ptsI, and crr genes." Saffen D.W., Presper K.A., Doering T.L., Roseman S. J. Biol. Chem. 262:16241-16253(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T. DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"Analysis of the ptsH-ptsI-crr region in Escherichia coli K-12: nucleotide sequence of the ptsH gene." de Reuse H., Roy A., Danchin A. Gene 35:199-207(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-56.
[7]	"DNA sequences of the cysK regions of Salmonella typhimurium and Escherichia coli and linkage of the cysK regions to ptsH." Byrne C.R., Monroe R.S., Ward K.A., Kredich N.M. J. Bacteriol. 170:3150-3157(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-54. Strain: K12.
[8]	"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Link A.J., Robison K., Church G.M. Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-11. Strain: K12 / EMG2.
[9]	"Novel proteins of the phosphotransferase system encoded within the rpoN operon of Escherichia coli. Enzyme IIANtr affects growth on organic nitrogen and the conditional lethality of an erats mutant." Powell B.S., Court D.L., Inada T., Nakamura Y., Michotey V., Cui X., Reizer A., Saier M.H. Jr., Reizer J. J. Biol. Chem. 270:4822-4839(1995) [PubMed] [Europe PMC] [Abstract] Cited for: PURIFICATION, FUNCTION IN NITROGEN-METABOLIC PTS.
[10]	"Escherichia coli proteome analysis using the gene-protein database." VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C. Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY 2D-GEL.
[11]	"The first step in sugar transport: crystal structure of the amino terminal domain of enzyme I of the E. coli PEP: sugar phosphotransferase system and a model of the phosphotransfer complex with HPr." Liao D.-I., Silverton E., Seok Y.-J., Lee B.R., Peterkofsky A., Davies D.R. Structure 4:861-872(1996) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-259.
[12]	"Solution structure of the 30 kDa N-terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system by multidimensional NMR." Garrett D.S., Seok Y.-J., Liao D.-I., Peterkofsky A., Gronenborn A.M., Clore G.M. Biochemistry 36:2517-2530(1997) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 1-259.
[13]	"Tautomeric state and pKa of the phosphorylated active site histidine in the N-terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system." Garrett D.S., Seok Y.-J., Peterkofsky A., Clore G.M., Gronenborn A.M. Protein Sci. 7:789-793(1998) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 1-259.
[14]	"Solution structure of the 40,000 Mr phosphoryl transfer complex between the N-terminal domain of enzyme I and HPr." Garrett D.S., Seok Y.-J., Peterkofsky A., Gronenborn A.M., Clore G.M. Nat. Struct. Biol. 6:166-173(1999) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 1-259.
[15]	"Structure of phosphorylated enzyme I, the phosphoenolpyruvate:sugar phosphotransferase system sugar translocation signal protein." Teplyakov A., Lim K., Zhu P.-P., Kapadia G., Chen C.C.H., Schwartz J., Howard A., Reddy P.T., Peterkofsky A., Herzberg O. Proc. Natl. Acad. Sci. U.S.A. 103:16218-16223(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, SUBUNIT, SUBSTRATE BINDING AT ARG-332; ASN-454 AND ASP-455, METAL BINDING AT GLU-431 AND ASP-455, ACTIVE SITE HIS-189 AND CYS-502.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J02796 Genomic DNA. Translation: AAA24441.1.
M10425 Genomic DNA. Translation: AAA24439.1.
U00096 Genomic DNA. Translation: AAC75469.1.
AP009048 Genomic DNA. Translation: BAA16290.1.
M21994 Genomic DNA. Translation: AAA24385.1.
M21451 Genomic DNA. Translation: AAA23656.1.

PIR

WQECPI. B29785.

RefSeq

NP_416911.1. NC_000913.2.
YP_490652.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EZA	NMR	-	A	1-258	[»]
1EZB	NMR	-	A	1-258	[»]
1EZC	NMR	-	A	1-258	[»]
1EZD	NMR	-	A	1-258	[»]
1ZYM	X-ray	2.50	A/B	1-258	[»]
2EZA	NMR	-	A	1-258	[»]
2EZB	NMR	-	A	1-258	[»]
2EZC	NMR	-	A	1-258	[»]
2HWG	X-ray	2.70	A/B	1-575	[»]
2KX9	Other	-	A/B	1-573	[»]
2L5H	Other	-	A/B	1-573	[»]
2XDF	Other	-	A/B	1-573	[»]
3EZA	NMR	-	A	1-249	[»]
3EZB	NMR	-	A	1-258	[»]
3EZE	NMR	-	A	1-258	[»]

ProteinModelPortal

P08839.

SMR

P08839. Positions 1-573.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-10603N.

IntAct

P08839. 11 interactions.

MINT

MINT-346878.

STRING

511145.b2416.

Protein family/group databases

TCDB

8.A.7.1.1. phosphotransferase system enzyme I (EI) family.

PTM databases

PhosSite

P0810428.

2D gel databases

SWISS-2DPAGE

P08839.

Proteomic databases

PaxDb

P08839.

PRIDE

P08839.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC75469; AAC75469; b2416.
BAA16290; BAA16290; BAA16290.

GeneID

12931576.
946879.

KEGG

ecj:Y75_p2377.
eco:b2416.

PATRIC

32120215. VBIEscCol129921_2510.

Organism-specific databases

EchoBASE

EB0782.

EcoGene

EG10789. ptsI.

Phylogenomic databases

eggNOG

COG1080.

HOGENOM

HOG000278513.

KO

K08483.

OMA

AAIFARS.

ProtClustDB

PRK11177.

Enzyme and pathway databases

BioCyc

EcoCyc:PTSI-MONOMER.
ECOL316407:JW2409-MONOMER.

BRENDA

2.7.3.9. 2026.

SABIO-RK

P08839.

Gene expression databases

Genevestigator

P08839.

Family and domain databases

Gene3D

1.10.274.10. 1 hit.
3.20.20.60. 1 hit.

InterPro

IPR008279. PEP-util_enz_mobile_dom.
IPR018274. PEP_util_AS.
IPR000121. PEP_util_C.
IPR023151. PEP_util_CS.
IPR006318. PEP_util_enz.
IPR024692. PTS_enz_I.
IPR008731. PTS_PEP_utilis_N.
IPR015813. Pyrv/PenolPyrv_Kinase.
[Graphical view]

PANTHER

PTHR22931:SF10. PTHR22931:SF10. 1 hit.

Pfam

PF05524. PEP-utilisers_N. 1 hit.
PF00391. PEP-utilizers. 1 hit.
PF02896. PEP-utilizers_C. 1 hit.
[Graphical view]

PIRSF

PIRSF000732. PTS_enzyme_I. 1 hit.

PRINTS

PR01736. PHPHTRNFRASE.

SUPFAM

SSF47831. PEP-utilisers_N. 1 hit.
SSF52009. PEP_mobile. 1 hit.
SSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit.

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...

Other

EvolutionaryTrace

P08839.

Entry information

Entry name

PT1_ECOLI

Accession

Primary (citable) accession number: P08839

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	November 1, 1988
Last modified:	May 1, 2013
This is version 146 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program