Reviewed, UniProtKB/Swiss-Prot P08839 (PT1_ECOLI)

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) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	575 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.14
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
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	cytosol Inferred from direct assay. Source: UniProtKB
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 protein binding Inferred from physical interaction. Source: IntAct 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.14

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

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

186 – 188

3

Helix

189 – 197

9

Helix

208 – 211

4

Beta strand

217 – 220

4

Beta strand

227 – 230

4

Helix

233 – 239

7

Turn

240 – 243

4

Helix

244 – 247

4

Helix

250 – 253

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)
	P08839-1 [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: 2457575] [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: 2960675] [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: 9205837] [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: 9278503] [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: 16738553] [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: 2411636] [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: 3290198] [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: 9298646] [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: 7876255] [Abstract] Cited for: PURIFICATION, FUNCTION IN NITROGEN-METABOLIC PTS.
[10]	"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: 8805571] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-259.
[11]	"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: 9054557] [Abstract] Cited for: STRUCTURE BY NMR OF 1-259.
[12]	"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: 9541412] [Abstract] Cited for: STRUCTURE BY NMR OF 1-259.
[13]	"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: 10048929] [Abstract] Cited for: STRUCTURE BY NMR OF 1-259.
[14]	"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: 17053069] [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

EMBLGenBankDDBJ

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

AP_003010.1.
NP_416911.1.

3D structure databases

PDBPDBe

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	[»]
3EZA	NMR	-	A	1-249	[»]
3EZB	NMR	-	A	1-258	[»]
3EZE	NMR	-	A	1-258	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:10603N.

IntAct

P08839. 11 interactions.

STRING

P08839.

Protein family/group databases

TCDB

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

PTM databases

PhosSite

P08839.

2-D gel databases

SWISS-2DPAGE

P08839.

ECO2DBASE

B058.3. 6TH EDITION.

Genome annotation databases

GeneID

946879.

GenomeReviews

Gene locus JW2409 in contig AP009048_GR.
Gene locus b2416 in contig U00096_GR.

KEGG

ecj:JW2409.
eco:b2416.

Organism-specific databases

EchoBASE

EB0782.

EcoGene

EG10789. ptsI.

CMR

Search...

Phylogenomic databases

HOGENOM

P08839.

OMA

VILVAYD.

Enzyme and pathway databases

BioCyc

EcoCyc:PTSI-MON.

BRENDA

2.7.3.9. 246.

Gene expression databases

Genevestigator

P08839.

Family and domain databases

InterPro

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:1.10.274.10. PTS_PEP_utilis_N. 1 hit.
G3DSA:3.20.20.60. Pyrv/PenolPyrv_Kinase_cat. 1 hit.

Pfam

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]

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

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:	November 3, 2009
This is version 113 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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