Reviewed, UniProtKB/Swiss-Prot P0A250 (PT1_SALTI)

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:	STY2668, t0425

Organism

Salmonella typhi [Complete proteome] [HAMAP]

Taxonomic identifier

90370 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella

Protein attributes

Sequence length	575 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) By similarity.
Catalytic activity	Phosphoenolpyruvate + protein L-histidine = pyruvate + protein N(pi)-phospho-L-histidine.
Cofactor	Magnesium By similarity.
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
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.
Caution	In strain CT18 it seems to be a pseudogene. It is interrupted by a frameshift in position 353. The sequence has been verified by the authors and is believed to be correct.

Ontologies

Keywords
Biological process	Phosphotransferase system Sugar transport Transport
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding
Molecular function	Kinase Transferase
Technical term	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 – 575	575	Phosphoenolpyruvate-protein phosphotransferase		PRO_0000147078
Sites
	Active site	189	1	Tele-phosphohistidine intermediate By similarity
	Active site	502	1	Proton donor By similarity
	Metal binding	431	1	Magnesium By similarity
	Metal binding	455	1	Magnesium By similarity
	Binding site	296	1	Substrate By similarity
	Binding site	332	1	Substrate By similarity
	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 By similarity
	Binding site	455	1	Substrate; via amide nitrogen By similarity
Experimental info
	Sequence conflict	346	1	N → H Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P0A250-1 [UniParc]. Last modified March 15, 2005. Version 1. Checksum: 5A87EEE702D823F0	FASTA	575	63,369
	10 20 30 40 50 60 MISGILASPG IAFGKALLLK EDEIVIDRKK ISADKVDQEV ERFLSGRAKA SAQLEAIKTK 70 80 90 100 110 120 AGETFGEEKE AIFEGHIMLL EDEELEQEII ALIKDKHMTA DAAAHEVIEG QATALEELDD 130 140 150 160 170 180 EYLKERAADV RDIGKRLLRN ILGLAIIDLS AIQEEVILVA ADLTPSETAQ LNLQKVLGFI 190 200 210 220 230 240 TDAGGRTSHT SIMARSLELP AIVGTGSVTA QVKNGDYLIL DAVNNQVYVN PTNDVIEQLR 250 260 270 280 290 300 AVQEQVATEK AELAKLKDLP AITLDGHQVE VCANIGTVRD VEGAERNGAE GVGLYRTEFL 310 320 330 340 350 360 FMDRDALPTE EEQFAAYKAV AEACGSQAVI VRTMDIGGDK ELPYMNFPKE ENPFLGWRAV 370 380 390 400 410 420 RIAMDRKEIL RDQVRAILRA 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

[1]

"Complete genome sequence of a multiple drug resistant Salmonella enterica serovar Typhi CT18." Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J., Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M., Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A., Davis P. , Davies R.M., Dowd L., White N., Farrar J., Feltwell T., Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A., Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S., Barrell B.G. Nature 413:848-852(2001) [PubMed: 11677608] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CT18.

[2]

"Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and CT18." Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V., Kodoyianni V., Schwartz D.C., Blattner F.R. J. Bacteriol. 185:2330-2337(2003) [PubMed: 12644504] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700931 / Ty2.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AL627274 Genomic DNA. No translation available. AE014613 Genomic DNA. Translation: AAO68143.1.
RefSeq	NP_804294.1.
3D structure databases
HSSP	HSSP built from PDB template 1EZC based on UniProtKB P08839.
SMR	P0A250. Positions 2-573.
ModBase	Search...
Proteomic databases
PRIDE	P0A250.
Genome annotation databases
GeneID	1068461.
GenomeReviews	Gene locus t0425 in contig AE014613_GR. Gene locus STY2668 in contig AL513382_GR.
KEGG	stt:t0425. sty:STY2668.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P0A250.
Enzyme and pathway databases
BioCyc	SENT209261:T0425-MON.
BRENDA	2.7.3.9. 3716.
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_SALTI

Accession

Primary (citable) accession number: P0A250
Secondary accession number(s): P12654

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	March 15, 2005
Last modified:	September 22, 2009
This is version 32 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)