O83018 (PT1_BACSI) 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

Bacillus sp. (strain S)

Taxonomic identifier

126783 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	578 AA.
Sequence status	Complete.
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.
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
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 – 578	578	Phosphoenolpyruvate-protein phosphotransferase		PRO_0000147056
Sites
	Active site	195	1	Tele-phosphohistidine intermediate By similarity
	Active site	508	1	Proton donor By similarity
	Metal binding	437	1	Magnesium By similarity
	Metal binding	461	1	Magnesium By similarity
	Binding site	302	1	Substrate By similarity
	Binding site	338	1	Substrate By similarity
	Binding site	437	1	Substrate By similarity
	Binding site	458	1	Substrate; via carbonyl oxygen By similarity
	Binding site	459	1	Substrate; via amide nitrogen By similarity
	Binding site	460	1	Substrate By similarity
	Binding site	461	1	Substrate; via amide nitrogen By similarity

Sequences

	Sequence		Length	Mass (Da)
	O83018 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: 82F7EEB1D901CBEE	FASTA	578	63,451
	10 20 30 40 50 60 MGNAIREKTI HGIAASSGIA IAKAYRLETP DLAAEKRAVA DVEAEVARFE AAVAKAKEEL 70 80 90 100 110 120 EAIKQHALEK LGEDKAAIFA AHLLVLDDPE LLNPIKEKIQ TERVNAEYSL DETASFFISM 130 140 150 160 170 180 FEAMDNEYMK ERAADIRDVT KRVLAHLLGV TISNPSLISE EVVIIAEDLT PSDTAQLNRQ 190 200 210 220 230 240 YVKGFATDIG GRTSHSAIMA RSLEIPAVVG TKTVTAEVKN GDIVIVDGLD GQVIINPSPE 250 260 270 280 290 300 LLAQYEQKRA RYEAQKAEWA KLVHEATVTA DGIHVELAAN IGTPDDVKGA LANGAEGIGL 310 320 330 340 350 360 YRTEFLYMGR SELPTEDEQF VAYKTVLEQM NGKPVVVRTL DIGGDKELPY LQLPKEMNPF 370 380 390 400 410 420 LGFRAIRLCL EMQDMFRTQL RALLRASVYG NLKIMFPMIA TLDEFRQAKA ILLEEKEALL 430 440 450 460 470 480 RQGVAVADGI EVGMMVEIPA AAVMADQFAK EVDFFSIGTN DLIQYTMAAD RMNERVAYLY 490 500 510 520 530 540 QPYNPAILRL ISHVIDAAHR EGKWVGMCGE MAGDPIAIPI LLALGLDEFS MSATSILPAR 550 560 570 AQLKQLAKEE AARIKETVLS LGTAEEVVSF VKRTFSLA

References

[1]	"Bacillus sp. strain S phosphotransferase system enzyme I (ptsI) gene." Ohno M., Beppu T., Ueda K. Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB016285 Genomic DNA. Translation: BAA31955.1.
3D structure databases
ProteinModelPortal	O83018.
SMR	O83018. Positions 10-572.
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_BACSI

Accession

Primary (citable) accession number: O83018

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1998
Last modified:	October 19, 2011
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program