Reviewed, UniProtKB/Swiss-Prot P23530 (PT1_ENTFA)

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:	EF_0710

Organism

Enterococcus faecalis (Streptococcus faecalis) [Complete proteome] [HAMAP]

Taxonomic identifier

1351 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Enterococcaceae › Enterococcus

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).
Catalytic activity	Phosphoenolpyruvate + protein L-histidine = pyruvate + protein N(pi)-phospho-L-histidine.
Cofactor	Magnesium By similarity.
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	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	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 – 575	575	Phosphoenolpyruvate-protein phosphotransferase		PRO_0000147068
Sites
	Active site	191	1	Tele-phosphohistidine intermediate Ref.2
	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)
	P23530-1 [UniParc]. Last modified April 23, 2003. Version 2. Checksum: 9A8E709FF128C5AE	FASTA	575	63,178
	10 20 30 40 50 60 MSEMLKGIAA SDGVAVAKAY LLVQPDLSFN KTSVEDTDAE ATRLDDALAK STEELQAIRD 70 80 90 100 110 120 KAAQSLGEAE AQVFDAHLMV LSDPEMVGQI KQNIQDNKVN AEAALKEVTD MYIGMFEAMD 130 140 150 160 170 180 DNAYMQERAA DIRDVAKRIL AHLLGVTLPN PSMINEEVIV VAHDLTPSDT AQLDRTYVKA 190 200 210 220 230 240 FVTDIGGRTS HSAIMARSLE IPAIVGTKEI TDKVKAGDIL AVNGIIGDVI IDPTDAEKSE 250 260 270 280 290 300 FEAEAKAYAD QKAEWDKLKN AETVTADGKH VELAANIGTP KDLEGVHKNG GEAVGLYRTE 310 320 330 340 350 360 FLYMDSSDFP TEEDQYQAYK AVLEGMEGKP VVVRTMDIGG DKELPYLTLP HEMNPFLGYR 370 380 390 400 410 420 ALRISLSELG DGMFRTQMRA LLRASVHGNL RIMFPMVATL KEFRAAKAIF EDEKQKLVNE 430 440 450 460 470 480 GVEVSNDIQV GIMIEIPAAA VLADKFAKEV DFFSVGTNDL IQYTMAADRM NERVSYLYQP 490 500 510 520 530 540 YNPSILRLIK NVIDAAHAEG KWAGMCGEMA GDQTAVPLLL GMGLDEFSMS ATSILKTRSL 550 560 570 MKRLDTTKMA ELADRALKEC DTMEEVFALV EEYTK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus faecalis." Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R., Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin S.A. , Kolonay J.F., Madupu R., Nelson W.C., Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M., Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M. Science 299:2071-2074(2003) [PubMed: 12663927] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: V583 / ATCC 700802.
[2]	"Phosphoenolpyruvate-dependent protein kinase enzyme I of Streptococcus faecalis: purification and properties of the enzyme and characterization of its active center." Alpert C.-A., Frank R., Stueber K., Deutscher J., Hengstenberg W. Biochemistry 24:959-964(1985) [PubMed: 3922407] [Abstract] Cited for: PROTEIN SEQUENCE OF 180-208, ACTIVE SITE HIS-191.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE016830 Genomic DNA. Translation: AAO80531.1.
PIR	A22018.
RefSeq	NP_814461.1.
3D structure databases
HSSP	HSSP built from PDB template 1EZC based on UniProtKB P08839.
ModBase	Search...
Genome annotation databases
GeneID	1199610.
GenomeReviews	Gene locus EF_0710 in contig AE016830_GR.
KEGG	efa:EF0710.
NMPDR	fig|226185.1.peg.646.
TIGR	EF_0710.
Phylogenomic databases
HOGENOM	P23530.
OMA	IFRASHY.
Enzyme and pathway databases
BioCyc	EFAE226185:EF_0710-MON.
BRENDA	2.7.3.9. 704.
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: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_ENTFA

Accession

Primary (citable) accession number: P23530

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	April 23, 2003
Last modified:	November 3, 2009
This is version 66 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)