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Protein

Multiphosphoryl transfer protein 2

Gene

ptsA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

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).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 activityi

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.PROSITE-ProRule annotation

Cofactori

Mg2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei16 – 161Tele-phosphohistidine intermediate; for HPr activityPROSITE-ProRule annotation
Active sitei301 – 3011Tele-phosphohistidine intermediate; for PTS EI activityPROSITE-ProRule annotation
Binding sitei408 – 4081SubstrateBy similarity
Binding sitei444 – 4441SubstrateBy similarity
Metal bindingi543 – 5431MagnesiumBy similarity
Binding sitei543 – 5431SubstrateBy similarity
Binding sitei564 – 5641Substrate; via carbonyl oxygenBy similarity
Binding sitei565 – 5651Substrate; via amide nitrogenBy similarity
Binding sitei566 – 5661SubstrateBy similarity
Metal bindingi567 – 5671MagnesiumBy similarity
Binding sitei567 – 5671Substrate; via amide nitrogenBy similarity
Active sitei614 – 6141Proton donor; for EI activityBy similarity
Active sitei750 – 7501Tele-phosphohistidine intermediate; for PTS EIIA activityPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Phosphotransferase system, Sugar transport, Transport

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG11906-MONOMER.
ECOL316407:JW5555-MONOMER.

Protein family/group databases

TCDBi4.A.2.1.10. the pts fructose-mannitol (fru) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Multiphosphoryl transfer protein 2
Short name:
MTP 2
Including the following 3 domains:
Phosphoenolpyruvate-protein phosphotransferase (EC:2.7.3.9)
Alternative name(s):
Enzyme I-Ani
Phosphotransferase system enzyme I
Phosphocarrier protein HPr
Short name:
Protein H
Fructose-like phosphotransferase enzyme IIA component (EC:2.7.1.-)
Alternative name(s):
PTS system fructose-like EIIA component
Gene namesi
Name:ptsA
Synonyms:frwA, yijH
Ordered Locus Names:b3947, JW5555
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11906. ptsA.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 833833Multiphosphoryl transfer protein 2PRO_0000147094Add
BLAST

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP32670.
PRIDEiP32670.

Interactioni

Protein-protein interaction databases

BioGridi4262062. 11 interactions.
DIPiDIP-10601N.
STRINGi511145.b3947.

Structurei

3D structure databases

ProteinModelPortaliP32670.
SMRiP32670. Positions 3-90, 118-684, 731-827.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 9190HPrPROSITE-ProRule annotationAdd
BLAST
Domaini688 – 830143PTS EIIA type-2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni269 – 616348PTS EIAdd
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the PEP-utilizing enzyme family.Curated
Contains 1 HPr domain.PROSITE-ProRule annotation
Contains 1 PTS EIIA type-2 domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105BZ3. Bacteria.
COG1080. LUCA.
COG1762. LUCA.
COG1925. LUCA.
HOGENOMiHOG000122933.
InParanoidiP32670.
KOiK08483.
K11189.
K11201.
OMAiHIYGEQR.
OrthoDBiEOG657JBQ.
PhylomeDBiP32670.

Family and domain databases

Gene3Di1.10.274.10. 1 hit.
3.20.20.60. 1 hit.
3.30.1340.10. 1 hit.
3.40.930.10. 1 hit.
3.50.30.10. 1 hit.
InterProiIPR000032. HPr_prot-like.
IPR008279. PEP-util_enz_mobile_dom.
IPR018274. PEP_util_AS.
IPR000121. PEP_util_C.
IPR023151. PEP_util_CS.
IPR016152. PTrfase/Anion_transptr.
IPR006318. PTS_EI-like.
IPR002178. PTS_EIIA_type-2_dom.
IPR008731. PTS_EIN.
IPR001020. PTS_HPr_His_P_site.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
PfamiPF05524. 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]
SUPFAMiSSF47831. SSF47831. 1 hit.
SSF51621. SSF51621. 1 hit.
SSF52009. SSF52009. 1 hit.
SSF55594. SSF55594. 1 hit.
SSF55804. SSF55804. 1 hit.
TIGRFAMsiTIGR01417. PTS_I_fam. 1 hit.
PROSITEiPS00742. 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.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P32670-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALIVEFICE LPNGVHARPA SHVETLCNTF SSQIEWHNLR TDRKGNAKSA
60 70 80 90 100
LALIGTDTLA GDNCQLLISG ADEQEAHQRL SQWLRDEFPH CDAPLAEVKS
110 120 130 140 150
DELEPLPVSL TNLNPQIIRA RTVCSGSAGG ILTPISSLDL NALGNLPAAK
160 170 180 190 200
GVDAEQSALE NGLTLVLKNI EFRLLDSDGA TSAILEAHRS LAGDTSLREH
210 220 230 240 250
LLAGVSAGLS CAEAIVASAN HFCEEFSRSS SSYLQERALD VRDVCFQLLQ
260 270 280 290 300
QIYGEQRFPA PGKLTQPAIC MADELTPSQF LELDKNHLKG LLLKSGGTTS
310 320 330 340 350
HTVILARSFN IPTLVGVDID ALTPWQQQTI YIDGNAGAIV VEPGEAVARY
360 370 380 390 400
YQQEARVQDA LREQQRVWLT QQARTADGIR IEIAANIAHS VEAQAAFGNG
410 420 430 440 450
AEGVGLFRTE MLYMDRTSAP GESELYNIFC QALESANGRS IIVRTMDIGG
460 470 480 490 500
DKPVDYLNIP AEANPFLGYR AVRIYEEYAS LFTTQLRSIL RASAHGSLKI
510 520 530 540 550
MIPMISSMEE ILWVKEKLAE AKQQLRNEHI PFDEKIQLGI MLEVPSVMFI
560 570 580 590 600
IDQCCEEIDF FSIGSNDLTQ YLLAVDRDNA KVTRHYNSLN PAFLRALDYA
610 620 630 640 650
VQAVHRQGKW IGLCGELGAK GSVLPLLVGL GLDELSMSAP SIPAAKARMA
660 670 680 690 700
QLDSRECRKL LNQAMACRTS LEVEHLLAQF RMTQQDAPLV TAECITLESD
710 720 730 740 750
WRSKEEVLKG MTDNLLLAGR CRYPRKLEAD LWAREAVFST GLGFSFAIPH
760 770 780 790 800
SKSEHIEQST ISVARLQAPV RWGDDEAQFI IMLTLNKHAA GDQHMRIFSR
810 820 830
LARRIMHEEF RNALVNAASA DAIASLLQHE LEL
Length:833
Mass (Da):91,774
Last modified:April 27, 2001 - v2
Checksum:i8E667F44D29CC732
GO

Sequence cautioni

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00006 Genomic DNA. Translation: AAC43053.1. Frameshift.
U00096 Genomic DNA. Translation: AAT48236.1.
AP009048 Genomic DNA. Translation: BAE77363.1.
RefSeqiWP_001174077.1. NZ_LN832404.1.
YP_026278.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAT48236; AAT48236; b3947.
BAE77363; BAE77363; BAE77363.
GeneIDi948437.
KEGGiecj:JW5555.
eco:b3947.
PATRICi32123417. VBIEscCol129921_4069.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00006 Genomic DNA. Translation: AAC43053.1. Frameshift.
U00096 Genomic DNA. Translation: AAT48236.1.
AP009048 Genomic DNA. Translation: BAE77363.1.
RefSeqiWP_001174077.1. NZ_LN832404.1.
YP_026278.1. NC_000913.3.

3D structure databases

ProteinModelPortaliP32670.
SMRiP32670. Positions 3-90, 118-684, 731-827.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262062. 11 interactions.
DIPiDIP-10601N.
STRINGi511145.b3947.

Protein family/group databases

TCDBi4.A.2.1.10. the pts fructose-mannitol (fru) family.

Proteomic databases

PaxDbiP32670.
PRIDEiP32670.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAT48236; AAT48236; b3947.
BAE77363; BAE77363; BAE77363.
GeneIDi948437.
KEGGiecj:JW5555.
eco:b3947.
PATRICi32123417. VBIEscCol129921_4069.

Organism-specific databases

EchoBASEiEB1851.
EcoGeneiEG11906. ptsA.

Phylogenomic databases

eggNOGiENOG4105BZ3. Bacteria.
COG1080. LUCA.
COG1762. LUCA.
COG1925. LUCA.
HOGENOMiHOG000122933.
InParanoidiP32670.
KOiK08483.
K11189.
K11201.
OMAiHIYGEQR.
OrthoDBiEOG657JBQ.
PhylomeDBiP32670.

Enzyme and pathway databases

BioCyciEcoCyc:EG11906-MONOMER.
ECOL316407:JW5555-MONOMER.

Miscellaneous databases

PROiP32670.

Family and domain databases

Gene3Di1.10.274.10. 1 hit.
3.20.20.60. 1 hit.
3.30.1340.10. 1 hit.
3.40.930.10. 1 hit.
3.50.30.10. 1 hit.
InterProiIPR000032. HPr_prot-like.
IPR008279. PEP-util_enz_mobile_dom.
IPR018274. PEP_util_AS.
IPR000121. PEP_util_C.
IPR023151. PEP_util_CS.
IPR016152. PTrfase/Anion_transptr.
IPR006318. PTS_EI-like.
IPR002178. PTS_EIIA_type-2_dom.
IPR008731. PTS_EIN.
IPR001020. PTS_HPr_His_P_site.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
PfamiPF05524. 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]
SUPFAMiSSF47831. SSF47831. 1 hit.
SSF51621. SSF51621. 1 hit.
SSF52009. SSF52009. 1 hit.
SSF55594. SSF55594. 1 hit.
SSF55804. SSF55804. 1 hit.
TIGRFAMsiTIGR01417. PTS_I_fam. 1 hit.
PROSITEiPS00742. 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.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. 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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: DISCUSSION OF SEQUENCE.

Entry informationi

Entry nameiPTFX2_ECOLI
AccessioniPrimary (citable) accession number: P32670
Secondary accession number(s): Q2M8P3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: April 27, 2001
Last modified: January 20, 2016
This is version 150 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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).By similarity

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.