Reviewed, UniProtKB/Swiss-Prot Q99V14 (PT1_STAAN)

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:	SA0935

Organism

Staphylococcus aureus (strain N315) [Complete proteome] [HAMAP]

Taxonomic identifier

158879 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	572 AA.
Sequence status	Complete.
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 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
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 – 572	572	Phosphoenolpyruvate-protein phosphotransferase		PRO_0000147082
Sites
	Active site	191	1	Tele-phosphohistidine intermediate By similarity
	Active site	504	1	Proton donor By similarity
	Metal binding	433	1	Magnesium By similarity
	Metal binding	457	1	Magnesium By similarity
	Binding site	298	1	Substrate By similarity
	Binding site	334	1	Substrate By similarity
	Binding site	433	1	Substrate By similarity
	Binding site	454	1	Substrate; via carbonyl oxygen By similarity
	Binding site	455	1	Substrate; via amide nitrogen By similarity
	Binding site	456	1	Substrate By similarity
	Binding site	457	1	Substrate; via amide nitrogen By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q99V14-1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 88D6B3F829BCC926	FASTA	572	63,224
	10 20 30 40 50 60 MSKLIKGIAA SDGVAIAKAY LLVEPDLTFD KNEKVTDVEG EVAKFNSAIE ASKVELTKIR 70 80 90 100 110 120 NNAEVQLGAD KAAIFDAHLL VLDDPELIQP IQDKIKNENA NAATALTDVT TQFVTIFESM 130 140 150 160 170 180 DNEYMKERAA DIRDVSKRVL SHILGVELPN PSMIDESVVI VGNDLTPSDT AQLNKEFVQG 190 200 210 220 230 240 FATNIGGRTS HSAIMSRSLE IPAIVGTKSI TQEVKQGDMI IVDGLNGDVI VNPTEDELIA 250 260 270 280 290 300 YQDKRECYFA DKKELQKLRD ADTVTVDGVH AELAANIGTP NDLPGVIENG AQGIGLYRTE 310 320 330 340 350 360 FLYMGRDQMP TEEEQFEAYK EVLEAMDGKR VVVRTLDIGG DKELSYLNLP EEMNPFLGYR 370 380 390 400 410 420 AIRLCLAQQD IFRPQLRALL RASVYGKLNI MFPMVATINE FREAKAILLE EKENLKNEGH 430 440 450 460 470 480 DISDDIELGI MVEIPATAAL ADVFAKEVDF FSIGTNDLIQ YTLAADRMSE RVSYLYQPYN 490 500 510 520 530 540 PSILRLVKQV IEASHKEGKW TGMCGEMAGD ETAIPLLLGL GLDEFSMSAT SILKARRQIN 550 560 570 GLSKNEMTEL ANRAVDCATQ EEVIELVNNY VK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Whole genome sequencing of meticillin-resistant Staphylococcus aureus." Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y. , Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H., Hiramatsu K. Lancet 357:1225-1240(2001) [PubMed: 11418146] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"Correlation of proteomic and transcriptomic profiles of Staphylococcus aureus during the post-exponential phase of growth." Scherl A., Francois P., Bento M., Deshusses J.M., Charbonnier Y., Converset V., Huyghe A., Walter N., Hoogland C., Appel R.D., Sanchez J.-C., Zimmermann-Ivol C.G., Corthals G.L., Hochstrasser D.F., Schrenzel J. J. Microbiol. Methods 60:247-257(2005) [PubMed: 15590099] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
[3]	"Shotgun proteomic analysis of total and membrane protein extracts of S. aureus strain N315." Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F. Submitted (OCT-2007) to UniProtKB Cited for: IDENTIFICATION BY MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000018 Genomic DNA. Translation: BAB42181.1.
PIR	B89878.
RefSeq	NP_374203.1.
3D structure databases
SMR	Q99V14. Positions 5-572.
ModBase	Search...
Protein-protein interaction databases
STRING	Q99V14.
2-D gel databases
SWISS-2DPAGE	Q99V14.
Genome annotation databases
GeneID	1123759.
GenomeReviews	Gene locus SA0935 in contig BA000018_GR.
KEGG	sau:SA0935.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1080.
HOGENOM	HBG456539.
OMA	EKVSYLY.
Enzyme and pathway databases
BioCyc	SAUR158879:SA0935-MONOMER.
Family and domain databases
InterPro	IPR008279. PEP-utiliz_enz_mobile_dom. IPR018274. PEP_mobile_CS. IPR006318. PEP_P_trans. IPR000121. PEP_utilisers. 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.
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_STAAN

Accession

Primary (citable) accession number: Q99V14

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 2, 2002
Last sequence update:	June 1, 2001
Last modified:	February 9, 2010
This is version 58 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)