Reviewed, UniProtKB/Swiss-Prot P23533 (PT1_STACT)

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:	Sca_0705

Organism

Staphylococcus carnosus (strain TM300) [Complete proteome] [HAMAP]

Taxonomic identifier

396513 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	573 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).
Catalytic activity	Phosphoenolpyruvate + protein L-histidine = pyruvate + protein N(pi)-phospho-L-histidine.
Cofactor	Magnesium By similarity.
Subunit structure	Homodimer. Ref.4
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 By similarity.
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.

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
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 – 573

573

Phosphoenolpyruvate-protein phosphotransferase

PRO_0000147087

Sites

Active site

190

1

Tele-phosphohistidine intermediate By similarity

Active site

503

1

Proton donor Probable

Metal binding

432

1

Magnesium By similarity

Metal binding

456

1

Magnesium By similarity

Binding site

297

1

Substrate

Binding site

333

1

Substrate

Binding site

432

1

Substrate By similarity

Binding site

453

1

Substrate; via carbonyl oxygen By similarity

Binding site

454

1

Substrate; via amide nitrogen By similarity

Binding site

455

1

Substrate

Binding site

456

1

Substrate; via amide nitrogen By similarity

Binding site

466

1

Substrate

Experimental info

Sequence conflict

124

1

M → I in AAA26664. Ref.1

Sequence conflict

128

1

A → AK in AAA26664. Ref.1

Sequence conflict

406 – 420

15

LLEEE…NEGYE → FLKKNVLTLKMKAMK in AAA26664. Ref.1

Sequence conflict

479 – 484

6

NPAILR → ISNFSF in AAA26664. Ref.1

Sequence conflict

536

1

R → V in AAA26664. Ref.1

Secondary structure

1

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573

Helix Strand Turn

Details...

Beta strand

10 – 12

3

Helix

37 – 66

30

Beta strand

68 – 70

3

Helix

73 – 81

9

Helix

84 – 97

14

Helix

101 – 117

17

Helix

124 – 143

20

Turn

166 – 170

5

Turn

174 – 176

3

Helix

190 – 197

8

Helix

209 – 211

3

Turn

236 – 238

3

Helix

239 – 244

6

Helix

247 – 255

9

Helix

256 – 258

3

Beta strand

271 – 278

8

Helix

279 – 281

3

Helix

282 – 286

5

Turn

287 – 289

3

Beta strand

291 – 297

7

Helix

299 – 301

3

Helix

311 – 324

14

Turn

325 – 327

3

Beta strand

329 – 333

5

Beta strand

344 – 346

3

Helix

354 – 356

3

Beta strand

357 – 359

3

Helix

361 – 366

6

Helix

368 – 381

14

Helix

382 – 384

3

Beta strand

385 – 393

9

Helix

397 – 415

19

Turn

416 – 418

3

Beta strand

426 – 431

6

Helix

434 – 438

5

Helix

440 – 446

7

Beta strand

448 – 452

5

Helix

454 – 462

9

Helix

472 – 474

3

Helix

480 – 495

16

Beta strand

499 – 502

4

Helix

505 – 508

4

Turn

510 – 512

3

Helix

513 – 519

7

Beta strand

522 – 526

5

Helix

528 – 530

3

Helix

531 – 539

9

Helix

543 – 553

11

Helix

559 – 569

11

Sequences

	Sequence		Length	Mass (Da)
	P23533-1 [UniParc]. Last modified May 5, 2009. Version 2. Checksum: EB31B4DB01D0611D	FASTA	573	63,299
	10 20 30 40 50 60 MAKQIKGIAA SDGVAIAKAY LLVEPDLSFD NESVTDTDAE VAKFNGALNK SKVELTKIRN 70 80 90 100 110 120 NAEKQLGADK AAIFDAHLLV LEDPELIQPI EDKIKNESVN AAQALTDVSN QFITIFESMD 130 140 150 160 170 180 NEYMAERAAD IRDVSKRVLA HILGVELPNP SIVDESVVII GNDLTPSDTA QLNKEYVQGF 190 200 210 220 230 240 VTNIGGRTSH SAIMSRSLEI PAVVGTKSIT EEVEAGDTIV VDGMTGDVLI NPSDEVIAEY 250 260 270 280 290 300 QEKRENFFKD KQELQKLRDA ESVTADGHHV ELAANIGTPN DLPGVIENGA EGIGLYRTEF 310 320 330 340 350 360 LYMGRDQMPT EEEQFEAYKA VLEAMKGKRV VVRTLDIGGD KELPYLDLPE EMNPFLGYRA 370 380 390 400 410 420 IRLCLDQPEI FRPQLRALLR ASVFGKLNIM FPMVATIQEF RDAKALLEEE RANLKNEGYE 430 440 450 460 470 480 VADDIELGIM VEIPSTAALA DIFAKEVDFF SIGTNDLIQY TMAADRMSER VSYLYQPYNP 490 500 510 520 530 540 AILRLVKQVI EASHAEGKWT GMCGEMAGDQ TAIPLLLGLG LDEFSMSATS ILKARRLIRS 550 560 570 LNESEMKELS ERAVQCATSE EVVDLVEEYT KNA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Staphylococcal phosphoenolpyruvate-dependent phosphotransferase system: molecular cloning and nucleotide sequence of the Staphylococcus carnosus ptsI gene and expression and complementation studies of the gene product." Kohlbrecher D., Eisermann R., Hengstenberg W. J. Bacteriol. 174:2208-2214(1992) [PubMed: 1551842] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Genome analysis of the meat starter culture bacterium Staphylococcus carnosus TM300." Rosenstein R., Nerz C., Biswas L., Resch A., Raddatz G., Schuster S.C., Goetz F. Appl. Environ. Microbiol. 75:811-822(2009) [PubMed: 19060169] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"Staphylococcal phosphoenolpyruvate-dependent phosphotransferase system. Purification and protein sequencing of the Staphylococcus carnosus histidine-containing protein, and cloning and DNA sequencing of the ptsH gene." Eisermann R., Fischer R., Kessler U., Neubauer A., Hengstenberg W. Eur. J. Biochem. 197:9-14(1991) [PubMed: 1901791] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-90.
[4]	"Structure of the full-length enzyme I of the phosphoenolpyruvate-dependent sugar phosphotransferase system." Marquez J., Reinelt S., Koch B., Engelmann R., Hengstenberg W., Scheffzek K. J. Biol. Chem. 281:32508-32515(2006) [PubMed: 16867985] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), SUBUNIT, SUBSTRATE BINDING AT ARG-297; ARG-333; ASN-455 AND ARG-466, ACTIVE SITE CYS-503.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M69050 Genomic DNA. Translation: AAA26664.1.
AM295250 Genomic DNA. Translation: CAL27616.1.
X60766 Genomic DNA. Translation: CAA43176.1.

PIR

B42374.

RefSeq

YP_002633801.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2HRO	X-ray	2.50	A	1-573	[»]

ModBase

Search...

Genome annotation databases

GeneID

7551969.

GenomeReviews

Gene locus Sca_0705 in contig AM295250_GR.

KEGG

sca:Sca_0705.

Organism-specific databases

CMR

Search...

Enzyme and pathway databases

BRENDA

2.7.3.9. 3303.

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:3.50.30.10. PEP_mobile. 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]

PROSITE

PS00742. PEP_ENZYMES_2. 1 hit.
PS00370. PEP_ENZYMES_PHOS_SITE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

PT1_STACT

Accession

Primary (citable) accession number: P23533
Secondary accession number(s): B9DQ26

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	May 5, 2009
Last modified:	September 22, 2009
This is version 65 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)