Reviewed, UniProtKB/Swiss-Prot Q84F83 (PT1_BACSH)

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

Bacillus sphaericus

Taxonomic identifier

1421 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Planococcaceae › Lysinibacillus

Protein attributes

Sequence length	570 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). It seems that in B.sphaericus, the sugar PTS is mainly implicated in N-acetylglucosamine (GlcNAc) transport and utilization. Ref.1
Catalytic activity	Phosphoenolpyruvate + protein L-histidine = pyruvate + protein N(pi)-phospho-L-histidine.
Cofactor	Magnesium 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.

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 – 570	570	Phosphoenolpyruvate-protein phosphotransferase		PRO_0000147057
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

Sequences

	Sequence		Length	Mass (Da)
	Q84F83-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: B29CB05A4694876C	FASTA	570	62,600
	10 20 30 40 50 60 MTHLACIAAS DGIAIAKAYR FVQPNLTFSQ TTVQDVQAEQ QRLAAALAKT EQELRPSKQQ 70 80 90 100 110 120 TLKKFSAEEA AIFEAHLLVV KDSELIGPIN QKTADEGVNA EFALHEVSSM FVALFESMDD 130 140 150 160 170 180 EYMSARASDI KDVTNRILAH LLGAHIPNPS SISEQVIIVA NDLTPSETAQ LDRNFVLGFI 190 200 210 220 230 240 TDIGGRTSHS AIMGRSLEIP AVVGTGVATT TIQDGDILIV DGLSGQVFVN PTADVIVSYQ 250 260 270 280 290 300 EKAQSYHTQQ AEWSTLVNEQ TVSKDGVHVE LAANIGSPGD LEGVLRHGAE GIGLYRTEFL 310 320 330 340 350 360 YMGRENLPSE DEQFTAYQTV LEGMQGKPVV IRTLDLGGDK HLPYLPLQEE MNPFLGHRAI 370 380 390 400 410 420 RLCLEQQELF RTPLRALLRA SVYGNLKIMF PIIATIQEFR DAKAILLEEQ EKLKAAGEEV 430 440 450 460 470 480 SADIEIGMMV EIPATAVMAD VFAKEVDFFS IGTNDLIQYT MAADRMNEKV SYLYQPYNPA 490 500 510 520 530 540 FLRLIQMVIH AAHQEQKWVG MCGEMAGDEL AVPLLLGLGL DEFSMSATSI LKTRSLLKRL 550 560 570 SVKDMQALAT EALQVATAEE VMEKVKQAVK

References

[1]	"Phosphoenolpyruvate phosphotransferase system and N-acetylglucosamine metabolism in Bacillus sphaericus." Alice A.F., Perez-Martinez G., Sanchez-Rivas C. Microbiology 149:1687-1698(2003) [PubMed: 12855720] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION. Strain: 2362.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY211495 Genomic DNA. Translation: AAO43400.1.
3D structure databases
ModBase	Search...
Enzyme and pathway databases
BRENDA	2.7.3.9. 327.
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. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PT1_BACSH

Accession

Primary (citable) accession number: Q84F83

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	June 1, 2003
Last modified:	September 22, 2009
This is version 33 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)