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P45595 (PT1_STRMU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 89. 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:SMU_675
OrganismStreptococcus mutans [Complete proteome] [HAMAP]
Taxonomic identifier1309 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Lactobacillales › Streptococcaceae › Streptococcus

Protein attributes

Sequence length577 AA.
Sequence statusComplete.
Protein existenceInferred 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 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 – 577577Phosphoenolpyruvate-protein phosphotransferase
PRO_0000147092

Sites

Active site1911Tele-phosphohistidine intermediate By similarity
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

Experimental info

Sequence conflict5471D → A in AAA91093. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P45595 [UniParc].

Last modified November 28, 2002. Version 2.
Checksum: EE20E49B60FF8FE2

FASTA57763,398
        10         20         30         40         50         60 
MTEMLKGIAA SDGVAVAKAY LLVQPDLTFE TVSVTDTQAE EARLDAALEA SQNELSLIRQ 

        70         80         90        100        110        120 
KAVDTLGEEA AAVFDAHLMV LADPEMIGQI KETIRTKEVN AESALKEVTD MFVTLFENME 

       130        140        150        160        170        180 
DNPYMQERAA DIRDVAKRVL AHLLGVELPN PATISEESIV IAHDLTPSDT AQLDANYVKA 

       190        200        210        220        230        240 
FVTNIGGRTS HSAIMARTLE IAAVLGTNDI TERVKNGDIV AVNGITGQVI INPTEDQIAE 

       250        260        270        280        290        300 
FKAAGETYAK QKAEWALLKD AETVTADGKH FELAANIGTP KDVEGVNNNG AEAVGLYRTE 

       310        320        330        340        350        360 
FLYMDSQDFP TEDEQYEAYK AVLEGMNGKP VVVRTMDIGG DKELPYFDLP KEMNPFLGFR 

       370        380        390        400        410        420 
ALRISISETG NQMFRTQLRA LLRASVHGQL RIMFPMVALL NEFRKAKGIL EEEKANLKAE 

       430        440        450        460        470        480 
GVAVSDDIQV GIMIEIPAAA MLADQFAKEV DFFSIGTNDL IQYTMAADRM NEQVSYLYQP 

       490        500        510        520        530        540 
YNPSILRLVD HVVKAAHAEG KWAGMCGEMA GDQTAVPLLV GIGLDEFSMS ATSVLRTRSL 

       550        560        570 
MKKLDTDKMQ ELAQRALTEC ATMEEVLELE KEYIDFD

« Hide

References

« Hide 'large scale' references
[1]"Sequence and expression of the genes for HPr (ptsH) and enzyme I (ptsI) of the phosphoenolpyruvate-dependent phosphotransferase transport system from Streptococcus mutans."
Boyd D.A., Cvitkovitch D.G., Hamilton I.R.
Infect. Immun. 62:1156-1165(1994) [PubMed: 8132321] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: NG5 / Serotype c.
[2]"Genome sequence of Streptococcus mutans UA159, a cariogenic dental pathogen."
Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B., Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S., Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.
Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002) [PubMed: 12397186] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700610 / UA159 / Serotype c.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L15191 Genomic DNA. Translation: AAA91093.1.
AE014133 Genomic DNA. Translation: AAN58409.1.
RefSeqNP_721103.1. NC_004350.2.

3D structure databases

ProteinModelPortalP45595.
SMRP45595. Positions 5-573.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBSTRT00000012916; EBSTRP00000012398; EBSTRG00000012916.
GeneID1028092.
GenomeReviewsGene locus SMU_675 in contig AE014133_GR.
KEGGsmu:SMU_675.
NMPDRfig|210007.1.peg.616.
PATRIC19663535. VBIStrMut61772_0600.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000026845.
HOGENOMHBG456539.
OMAIFSAHLL.
ProtClustDBCLSK876691.

Enzyme and pathway databases

BioCycSMUT210007:SMU_675-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_STRMU
AccessionPrimary (citable) accession number: P45595
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 28, 2002
Last modified: January 25, 2012
This is version 89 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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