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P23530 (PT1_ENTFA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Phosphoenolpyruvate-protein phosphotransferase
EC=2.7.3.9
Alternative name(s):
Phosphotransferase system, enzyme I
Gene names
Name:ptsI
Ordered Locus Names:EF_0710
OrganismEnterococcus faecalis (Streptococcus faecalis)
Taxonomic identifier1351 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Lactobacillales › Enterococcaceae › Enterococcus

Protein attributes

Sequence length575 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 575575Phosphoenolpyruvate-protein phosphotransferase
PRO_0000147068

Sites

Active site1911Tele-phosphohistidine intermediate Ref.2
Active site5061Proton donor By similarity
Metal binding4351Magnesium By similarity
Metal binding4591Magnesium By similarity
Binding site2981Substrate By similarity
Binding site3341Substrate By similarity
Binding site4351Substrate By similarity
Binding site4561Substrate; via carbonyl oxygen By similarity
Binding site4571Substrate; via amide nitrogen By similarity
Binding site4581Substrate By similarity
Binding site4591Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
P23530 [UniParc].

Last modified April 23, 2003. Version 2.
Checksum: 9A8E709FF128C5AE

FASTA57563,178
        10         20         30         40         50         60 
MSEMLKGIAA SDGVAVAKAY LLVQPDLSFN KTSVEDTDAE ATRLDDALAK STEELQAIRD 

        70         80         90        100        110        120 
KAAQSLGEAE AQVFDAHLMV LSDPEMVGQI KQNIQDNKVN AEAALKEVTD MYIGMFEAMD 

       130        140        150        160        170        180 
DNAYMQERAA DIRDVAKRIL AHLLGVTLPN PSMINEEVIV VAHDLTPSDT AQLDRTYVKA 

       190        200        210        220        230        240 
FVTDIGGRTS HSAIMARSLE IPAIVGTKEI TDKVKAGDIL AVNGIIGDVI IDPTDAEKSE 

       250        260        270        280        290        300 
FEAEAKAYAD QKAEWDKLKN AETVTADGKH VELAANIGTP KDLEGVHKNG GEAVGLYRTE 

       310        320        330        340        350        360 
FLYMDSSDFP TEEDQYQAYK AVLEGMEGKP VVVRTMDIGG DKELPYLTLP HEMNPFLGYR 

       370        380        390        400        410        420 
ALRISLSELG DGMFRTQMRA LLRASVHGNL RIMFPMVATL KEFRAAKAIF EDEKQKLVNE 

       430        440        450        460        470        480 
GVEVSNDIQV GIMIEIPAAA VLADKFAKEV DFFSVGTNDL IQYTMAADRM NERVSYLYQP 

       490        500        510        520        530        540 
YNPSILRLIK NVIDAAHAEG KWAGMCGEMA GDQTAVPLLL GMGLDEFSMS ATSILKTRSL 

       550        560        570 
MKRLDTTKMA ELADRALKEC DTMEEVFALV EEYTK

« Hide

References

« Hide 'large scale' references
[1]"Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus faecalis."
Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R., Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin S.A. expand/collapse author list , Kolonay J.F., Madupu R., Nelson W.C., Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M., Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.
Science 299:2071-2074(2003) [PubMed: 12663927] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700802 / V583.
[2]"Phosphoenolpyruvate-dependent protein kinase enzyme I of Streptococcus faecalis: purification and properties of the enzyme and characterization of its active center."
Alpert C.-A., Frank R., Stueber K., Deutscher J., Hengstenberg W.
Biochemistry 24:959-964(1985) [PubMed: 3922407] [Abstract]
Cited for: PROTEIN SEQUENCE OF 180-208, ACTIVE SITE HIS-191.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE016830 Genomic DNA. Translation: AAO80531.1.
PIRA22018.
RefSeqNP_814461.1. NC_004668.1.

3D structure databases

ProteinModelPortalP23530.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1199610.
GenomeReviewsGene locus EF_0710 in contig AE016830_GR.
KEGGefa:EF0710.
NMPDRfig|226185.1.peg.646.
PATRIC21851812. VBIEntFae7065_0656.
TIGREF_0710.

Phylogenomic databases

HOGENOMHBG456539.
OMASAKMAEY.
ProtClustDBCLSK876691.

Enzyme and pathway databases

BioCycEFAE226185:EF_0710-MONOMER.

Family and domain databases

InterProIPR008279. 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]
Gene3DG3DSA: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.
KOK08483.
PANTHERPTHR22931:SF10. PTHR22931:SF10. 1 hit.
PfamPF05524. PEP-utilisers_N. 1 hit.
PF00391. PEP-utilizers. 1 hit.
PF02896. PEP-utilizers_C. 1 hit.
[Graphical view]
PIRSFPIRSF000732. PTS_enzyme_I. 1 hit.
PRINTSPR01736. PHPHTRNFRASE.
SUPFAMSSF47831. PEP-utilisers_N. 1 hit.
SSF52009. PEP_mobile. 1 hit.
SSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
TIGRFAMsTIGR01417. PTS_I_fam. 1 hit.
PROSITEPS00742. PEP_ENZYMES_2. 1 hit.
PS00370. PEP_ENZYMES_PHOS_SITE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePT1_ENTFA
AccessionPrimary (citable) accession number: P23530
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: April 23, 2003
Last modified: January 25, 2012
This is version 81 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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