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P32670 (PTFX2_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Multiphosphoryl transfer protein 2
Short name=MTP 2

Including the following 3 domains:

  1. Phosphoenolpyruvate-protein phosphotransferase
    EC=2.7.3.9
    Alternative name(s):
    Enzyme I-Ani
    Phosphotransferase system enzyme I
  2. Phosphocarrier protein HPr
    Short name=Protein H
  3. Fructose-like phosphotransferase enzyme IIA component
    EC=2.7.1.-
    Alternative name(s):
    PTS system fructose-like EIIA component
Gene names
Name:ptsA
Synonyms:frwA, yijH
Ordered Locus Names:b3947, JW5555
OrganismEscherichia coli (strain K12)
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length833 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Multifunctional protein that includes general (non sugar-specific) and sugar-specific components 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). HPr transfers the phosphoryl group to the phosphoryl carrier EIIA, which then transfers it to EIIB By similarity.

The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane By similarity.

Catalytic activity

Phosphoenolpyruvate + protein L-histidine = pyruvate + protein N(pi)-phospho-L-histidine.

Protein EIIA N(pi)-phospho-L-histidine + protein EIIB = protein EIIA + protein EIIB N(pi)-phospho-L-histidine/cysteine.

Cofactor

Magnesium By similarity.

Subcellular location

Cytoplasm Potential.

Domain

The EIIA domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the EIIB domain.

The Enzyme I (EI) 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 Enzyme I (EI) 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.

Contains 1 HPr domain.

Contains 1 PTS EIIA type-2 domain.

Sequence caution

The sequence AAC43053.1 differs from that shown. Reason: Frameshift at position 45.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 833833Multiphosphoryl transfer protein 2
PRO_0000147094

Regions

Domain2 – 9190HPr
Domain688 – 830143PTS EIIA type-2
Region269 – 616348PTS EI

Sites

Active site161Tele-phosphohistidine intermediate; for HPr activity By similarity
Active site3011Tele-phosphohistidine intermediate; for PTS EI activity By similarity
Active site6141Proton donor; for EI activity By similarity
Active site7501Tele-phosphohistidine intermediate; for PTS EIIA activity By similarity
Metal binding5431Magnesium By similarity
Metal binding5671Magnesium By similarity
Binding site4081Substrate By similarity
Binding site4441Substrate By similarity
Binding site5431Substrate By similarity
Binding site5641Substrate; via carbonyl oxygen By similarity
Binding site5651Substrate; via amide nitrogen By similarity
Binding site5661Substrate By similarity
Binding site5671Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
P32670 [UniParc].

Last modified April 27, 2001. Version 2.
Checksum: 8E667F44D29CC732

FASTA83391,774
        10         20         30         40         50         60 
MALIVEFICE LPNGVHARPA SHVETLCNTF SSQIEWHNLR TDRKGNAKSA LALIGTDTLA 

        70         80         90        100        110        120 
GDNCQLLISG ADEQEAHQRL SQWLRDEFPH CDAPLAEVKS DELEPLPVSL TNLNPQIIRA 

       130        140        150        160        170        180 
RTVCSGSAGG ILTPISSLDL NALGNLPAAK GVDAEQSALE NGLTLVLKNI EFRLLDSDGA 

       190        200        210        220        230        240 
TSAILEAHRS LAGDTSLREH LLAGVSAGLS CAEAIVASAN HFCEEFSRSS SSYLQERALD 

       250        260        270        280        290        300 
VRDVCFQLLQ QIYGEQRFPA PGKLTQPAIC MADELTPSQF LELDKNHLKG LLLKSGGTTS 

       310        320        330        340        350        360 
HTVILARSFN IPTLVGVDID ALTPWQQQTI YIDGNAGAIV VEPGEAVARY YQQEARVQDA 

       370        380        390        400        410        420 
LREQQRVWLT QQARTADGIR IEIAANIAHS VEAQAAFGNG AEGVGLFRTE MLYMDRTSAP 

       430        440        450        460        470        480 
GESELYNIFC QALESANGRS IIVRTMDIGG DKPVDYLNIP AEANPFLGYR AVRIYEEYAS 

       490        500        510        520        530        540 
LFTTQLRSIL RASAHGSLKI MIPMISSMEE ILWVKEKLAE AKQQLRNEHI PFDEKIQLGI 

       550        560        570        580        590        600 
MLEVPSVMFI IDQCCEEIDF FSIGSNDLTQ YLLAVDRDNA KVTRHYNSLN PAFLRALDYA 

       610        620        630        640        650        660 
VQAVHRQGKW IGLCGELGAK GSVLPLLVGL GLDELSMSAP SIPAAKARMA QLDSRECRKL 

       670        680        690        700        710        720 
LNQAMACRTS LEVEHLLAQF RMTQQDAPLV TAECITLESD WRSKEEVLKG MTDNLLLAGR 

       730        740        750        760        770        780 
CRYPRKLEAD LWAREAVFST GLGFSFAIPH SKSEHIEQST ISVARLQAPV RWGDDEAQFI 

       790        800        810        820        830 
IMLTLNKHAA GDQHMRIFSR LARRIMHEEF RNALVNAASA DAIASLLQHE LEL

« Hide

References

« Hide 'large scale' references
[1]"Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes."
Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.
Nucleic Acids Res. 21:5408-5417(1993) [PubMed: 8265357] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[2]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"Escherichia coli K-12: a cooperatively developed annotation snapshot -- 2005."
Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R., Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T., Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H., Thomson N.R., Wishart D., Wanner B.L.
Nucleic Acids Res. 34:1-9(2006) [PubMed: 16397293] [Abstract]
Cited for: SEQUENCE REVISION.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Novel phosphotransferase system genes revealed by bacterial genome analysis -- a gene cluster encoding a unique Enzyme I and the proteins of a fructose-like permease system."
Reizer J., Reizer A., Saier M.H. Jr.
Microbiology 141:961-971(1995) [PubMed: 7773398] [Abstract]
Cited for: DISCUSSION OF SEQUENCE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U00006 Genomic DNA. Translation: AAC43053.1. Frameshift.
U00096 Genomic DNA. Translation: AAT48236.1.
AP009048 Genomic DNA. Translation: BAE77363.1.
RefSeqYP_026278.1. NC_000913.2.

3D structure databases

ProteinModelPortalP32670.
SMRP32670. Positions 3-91, 116-682, 687-827.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-10601N.

Protein family/group databases

TCDB4.A.2.1.10. PTS fructose-mannitol (Fru) family.

PTM databases

PhosSiteP32670.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000004971; EBESCP00000004971; EBESCG00000004059.
EBESCT00000018053; EBESCP00000017344; EBESCG00000017109.
GeneID948437.
GenomeReviewsGene locus JW5555 in contig AP009048_GR.
Gene locus b3947 in contig U00096_GR.
KEGGecj:JW5555.
eco:b3947.
PATRIC32123417. VBIEscCol129921_4069.

Organism-specific databases

EchoBASEEB1851.
EcoGeneEG11906. ptsA.

Phylogenomic databases

eggNOGCOG1080.
GeneTreeEBGT00050000009028.
HOGENOMHBG456539.
OMAMLYMDRA.
PhylomeDBP32670.
ProtClustDBCLSK880377.

Enzyme and pathway databases

BioCycEcoCyc:EG11906-MONOMER.

Gene expression databases

GenevestigatorP32670.

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.
IPR016152. PTrfase/Anion_transptr.
IPR002178. PTS_EIIA_2.
IPR001020. PTS_HPr_His_P_site.
IPR005698. PTS_HPr_prot.
IPR000032. PTS_HPr_prot-like.
IPR008731. PTS_PEP_utilis_N.
IPR015813. Pyrv/PenolPyrv_Kinase.
[Graphical view]
Gene3DG3DSA:3.50.30.10. PEP_mobile. 1 hit.
G3DSA:3.40.930.10. PTS_EIIA_2. 1 hit.
G3DSA:3.30.1340.10. PTS_HPr_protein. 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.
K11189.
K11201.
PANTHERPTHR22931:SF10. PTHR22931:SF10. 1 hit.
PfamPF05524. PEP-utilisers_N. 1 hit.
PF00391. PEP-utilizers. 1 hit.
PF02896. PEP-utilizers_C. 1 hit.
PF00381. PTS-HPr. 1 hit.
PF00359. PTS_EIIA_2. 1 hit.
[Graphical view]
PRINTSPR01736. PHPHTRNFRASE.
SUPFAMSSF55594. HPr_protein. 1 hit.
SSF47831. PEP-utilisers_N. 1 hit.
SSF52009. PEP_mobile. 1 hit.
SSF55804. PTrfase/Anion_transptr. 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.
PS51094. PTS_EIIA_TYPE_2. 1 hit.
PS51350. PTS_HPR_DOM. 1 hit.
PS00369. PTS_HPR_HIS. 1 hit.
PS00589. PTS_HPR_SER. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePTFX2_ECOLI
AccessionPrimary (citable) accession number: P32670
Secondary accession number(s): Q2M8P3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: April 27, 2001
Last modified: January 25, 2012
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents