Reviewed, UniProtKB/Swiss-Prot P30299 (PT1_STRSL)

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

Organism

Streptococcus salivarius

Taxonomic identifier

1304 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Streptococcaceae › Streptococcus

Protein attributes

Sequence length	577 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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.
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
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 – 577	577	Phosphoenolpyruvate-protein phosphotransferase		PRO_0000147093
Sites
	Active site	191	1	Tele-phosphohistidine intermediate By similarity
	Active site	506	1	Proton donor By similarity
	Metal binding	435	1	Magnesium By similarity
	Metal binding	459	1	Magnesium By similarity
	Binding site	298	1	Substrate By similarity
	Binding site	334	1	Substrate By similarity
	Binding site	435	1	Substrate By similarity
	Binding site	456	1	Substrate; via carbonyl oxygen By similarity
	Binding site	457	1	Substrate; via amide nitrogen By similarity
	Binding site	458	1	Substrate By similarity
	Binding site	459	1	Substrate; via amide nitrogen By similarity

Sequences

	Sequence		Length	Mass (Da)
	P30299-1 [UniParc]. Last modified April 1, 1993. Version 1. Checksum: EDADDF90B85E72D2	FASTA	577	63,047
	10 20 30 40 50 60 MTEMLKGIAA SDGVAVAKAY LLVQPDLSFE TVTVEDTSAE EARLDAALAA SQDELSVIRE 70 80 90 100 110 120 KAVESLGEEA AAVFDAHLMV LADPEMTGQI KETIRAKQVN AEAALTEVTD MFIAIFEGME 130 140 150 160 170 180 DNPYMQERAA DIRDVTKRVL ANLLGKKLPN PATINEESIV VAHDLTPSDT AQLNKKYVKA 190 200 210 220 230 240 FVTNIGGRTS HSAIMARTLE IAAVLGTNNI TELVKDGDIL AVSGITGEVV INPTEEQIAE 250 260 270 280 290 300 FKAAGEAYAK QKAEWALLKD AQTVTADGKH FELAANIGTP KDVEGVNDNG AEAVGLYRTE 310 320 330 340 350 360 FLYMDSQDFP TEDDQYEAYK AVLEGMNGKP VVVRTMDIGG DKELPYFDLP KEMNPFLGYR 370 380 390 400 410 420 ALRISISETG NQMFRTQLRA LLRASVHGKL RIMFPMVALL TEFRTAKGIL EEEKAKLVAE 430 440 450 460 470 480 GVAVADDIEV GIMIEIPAAA MLADQFAKEV DFFSIGTNDL IQYTMAADRM NEQVSYLYQP 490 500 510 520 530 540 YNPSILRLIN NVIKAAHAEG KWAGMCGEMA GDQTAVPLLV GMGLDEFSMS ATSVLRTRSL 550 560 570 MKKLDTAKME EYANRALTEC STMEEVLELS KEYVNVD

References

[1]	"Cloning, sequencing and expression in Escherichia coli of the ptsI gene encoding enzyme I of the phosphoenolpyruvate:sugar phosphotransferase transport system from Streptococcus salivarius." Gagnon G., Vadeboncoeur C., Levesque R.C., Frenette M. Gene 121:71-78(1992) [PubMed: 1427100] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 25975.
[2]	"Phosphotransferase system of Streptococcus salivarius: characterization of the ptsH gene and its product." Gagnon G., Vadeboncoeur C., Frenette M. Gene 136:27-34(1993) [PubMed: 8294015] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10. Strain: ATCC 25975.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M81756 Genomic DNA. Translation: AAA26873.1. Z17217 Genomic DNA. Translation: CAA78924.1.
PIR	JC1375.
3D structure databases
HSSP	HSSP built from PDB template 1EZC based on UniProtKB P08839.
ModBase	Search...
Enzyme and pathway databases
BRENDA	2.7.3.9. 39093.
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_STRSL

Accession

Primary (citable) accession number: P30299

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	September 22, 2009
This is version 59 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)