Q9WXK9 (PT1_STREI) Reviewed, UniProtKB/Swiss-Prot

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 equinus (Streptococcus bovis)

Taxonomic identifier

1335 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Streptococcaceae › Streptococcus

Protein attributes

Sequence length	577 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript 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.
Induction	Transcription of ptsI appears to be regulated in response to sugars supplied, i.e. is four-fold lower when cells were grown on lactose than when grown on glucose.
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
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	kinase activity Inferred from electronic annotation. Source: UniProtKB-KW metal 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_0000147090
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)
	Q9WXK9 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 989FF58D1B6DDD12	FASTA	577	63,219
	10 20 30 40 50 60 MTEMLKGIAA SDGVAVAKAY LLVQPDLSFE TVTVEDTSAE EARLDAALKA SQDELSIIRE 70 80 90 100 110 120 KAVETLGEEA AAVFDAHLMV LADPEMISQI KETIRAKQTN AEAGLKEVTD MFITIFEGME 130 140 150 160 170 180 DNPYMQERAA DIRDVAKRVL AHLLGAKLPN PATIDEESIV IAHDLTPSDT AQLNKQFVKA 190 200 210 220 230 240 FVTNIGGRTS HSAIMARTLE IAAVLGTNDI TSRVKDGDIV AVNGITGEVI INPTDEQVAE 250 260 270 280 290 300 FKAAGEAYAK QKAEWALLKD AKTVTADGKH FELAANIGTP KDVEGVNANG AEAVGLYRTE 310 320 330 340 350 360 FLYMDSQDFP TEDEQYEAYK AVLEGMNGKP VVVRTMDIGG DKELPYLDLP KEMNPFLGFR 370 380 390 400 410 420 ALRISISETG NAMFRTQIRA LLRASVHGQL RIMFPMVALL KEFRAAKAIF DEEKANLKAE 430 440 450 460 470 480 GVAVSDDIQV GIMIEIPAAA MLADQFAKEV DFFSIGTNDL IQYTMAADRM NEQVSYLYQP 490 500 510 520 530 540 YNPSILRLIN NVIKAAHAEG KWVGMCGEMA GDQKAVPLLV EMGLDEFSMS ATSILRTRSL 550 560 570 MKKLDTAKMQ EYANRALTEC STMEEVLELS KEYVNVD

References

[1]	"Molecular characterization of HPr and related enzymes, and regulation of HPr phosphorylation in the ruminal bacterium Streptococcus bovis." Asanuma N., Hino T. Arch. Microbiol. 179:205-213(2003) [PubMed: 12610726] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 700410 / JB1.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB027569 Genomic DNA. Translation: BAA78049.1.
3D structure databases
ProteinModelPortal	Q9WXK9.
SMR	Q9WXK9. Positions 5-573.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR008279. PEP-util_enz_mobile_dom. IPR018274. PEP_util_AS. IPR000121. PEP_util_C. IPR023151. PEP_util_CS. IPR006318. PEP_util_enz. IPR024692. PTS_enz_I. IPR008731. PTS_PEP_utilis_N. IPR015813. Pyrv/PenolPyrv_Kinase. [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.
PANTHER	PTHR22931:SF10. PTHR22931:SF10. 1 hit.
Pfam	PF05524. PEP-utilisers_N. 1 hit. PF00391. PEP-utilizers. 1 hit. PF02896. PEP-utilizers_C. 1 hit. [Graphical view]
PIRSF	PIRSF000732. PTS_enzyme_I. 1 hit.
PRINTS	PR01736. PHPHTRNFRASE.
SUPFAM	SSF47831. PEP-utilisers_N. 1 hit. SSF52009. PEP_mobile. 1 hit. SSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
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_STREI

Accession

Primary (citable) accession number: Q9WXK9

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 2, 2002
Last sequence update:	November 1, 1999
Last modified:	October 19, 2011
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program