Phosphoenolpyruvate-protein phosphotransferase

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P0A249 (PT1_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 49. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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:	STM2432

Organism

Salmonella typhimurium

Taxonomic identifier

90371 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella

Protein attributes

Sequence length	575 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).
Catalytic activity	Phosphoenolpyruvate + protein L-histidine = pyruvate + protein N(pi)-phospho-L-histidine.
Cofactor	Magnesium By similarity.
Subunit structure	Homodimer.
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 Reference proteome
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 – 575

575

Phosphoenolpyruvate-protein phosphotransferase

PRO_0000147079

Sites

Active site

189

Tele-phosphohistidine intermediate By similarity

Active site

502

Proton donor By similarity

Metal binding

431

Magnesium By similarity

Metal binding

455

Magnesium By similarity

Binding site

296

Substrate By similarity

Binding site

332

Substrate By similarity

Binding site

431

Substrate By similarity

Binding site

452

Substrate; via carbonyl oxygen By similarity

Binding site

453

Substrate; via amide nitrogen By similarity

Binding site

454

Substrate By similarity

Binding site

455

Substrate; via amide nitrogen By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P0A249 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: 5A87EEE702D823F0
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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

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sugar transport by the bacterial phosphotransferase system. Structural and thermodynamic domains of enzyme I of Salmonella typhimurium." Licalsi C., Crocenzi T.S., Freire E., Roseman S. J. Biol. Chem. 266:19519-19527(1991) [PubMed: 1655788] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2." McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. Wilson R.K. Nature 413:852-856(2001) [PubMed: 11677609] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: LT2 / SGSC1412 / ATCC 700720.
[3]	"DNA sequences of the cysK regions of Salmonella typhimurium and Escherichia coli and linkage of the cysK regions to ptsH." Byrne C.R., Monroe R.S., Ward K.A., Kredich N.M. J. Bacteriol. 170:3150-3157(1988) [PubMed: 3290198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-299. Strain: LT2.
[4]	"Partial nucleotide sequence of the pts operon in Salmonella typhimurium: comparative analyses in five bacterial genera." Schnierow B.J., Yamada M., Saier M.H. Jr. Mol. Microbiol. 3:113-118(1989) [PubMed: 2497295] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9. Strain: LT2.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M76176 Genomic DNA. Translation: AAA27060.1. AE006468 Genomic DNA. Translation: AAL21326.1. M21450 Genomic DNA. Translation: AAA27053.1. X14737 Genomic DNA. Translation: CAA32867.1.
PIR	WQEBPI. A41027.
RefSeq	NP_461367.1. NC_003197.1.
3D structure databases
ProteinModelPortal	P0A249.
SMR	P0A249. Positions 2-573.
ModBase	Search...
Proteomic databases
PRIDE	P0A249.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1253954.
GenomeReviews	Gene locus STM2432 in contig AE006468_GR.
KEGG	stm:STM2432.
PATRIC	32383495. VBISalEnt20916_2570.
Phylogenomic databases
HOGENOM	HBG456539.
OMA	HINIVND.
ProtClustDB	PRK11177.
Enzyme and pathway databases
BioCyc	STYP99287:STM2432-MONOMER.
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.
KO	K08483.
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_SALTY

Accession

Primary (citable) accession number: P0A249
Secondary accession number(s): P12654

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	March 15, 2005
Last modified:	January 25, 2012
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents