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Protein

Phosphoenolpyruvate-dependent phosphotransferase system

Gene

ptsP

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the phosphoenolpyruvate-dependent nitrogen-metabolic phosphotransferase system (nitrogen-metabolic PTS), that seems to be involved in regulating nitrogen metabolism. Enzyme I-Ntr transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (NPr) (PubMed:10473571). Could function in the transcriptional regulation of sigma-54 dependent operons in conjunction with the NPr (PtsO) and EIIA-Ntr (PtsN) proteins (PubMed:8973315). Enzyme I-Ntr is specific for NPr (PubMed:10473571).2 Publications

Catalytic activityi

Phosphoenolpyruvate + protein L-histidine = pyruvate + protein N(pi)-phospho-L-histidine.1 Publication

Cofactori

Mg2+1 PublicationNote: Mn2+ allows activity only at low concentrations. In the presence of low concentrations of Co2+ or Ni2+, activity could be measured, but at concentrations above 0.2 mM, strong inhibition is observed.1 Publication

Enzyme regulationi

Inhibited by GDP and FAD.1 Publication

Kineticsi

Enzyme I-Ntr activity requires high ionic strength.1 Publication

Manual assertion based on experiment ini

  1. KM=10 µM for mannitol phosphate1 Publication
  1. Vmax=1 µmol/min/mg enzyme1 Publication

pH dependencei

Optimum pH is 8.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei356Tele-phosphohistidine intermediateBy similarity1
Binding sitei462PEPBy similarity1
Binding sitei498PEPBy similarity1
Metal bindingi597MagnesiumBy similarity1
Metal bindingi621MagnesiumBy similarity1
Binding sitei631PEPBy similarity1
Active sitei668Proton donorBy similarity1

GO - Molecular functioni

GO - Biological processi

  • phosphoenolpyruvate-dependent sugar phosphotransferase system Source: UniProtKB-KW
  • protein phosphorylation Source: EcoCyc
  • response to organonitrogen compound Source: EcoCyc
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:EG12188-MONOMER.
ECOL316407:JW2797-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoenolpyruvate-dependent phosphotransferase system1 Publication (EC:2.7.3.91 Publication)
Alternative name(s):
Enzyme I-Ntr1 Publication
Short name:
EINtr1 Publication
Phosphotransferase system, enzyme I1 Publication
Gene namesi
Name:ptsP
Synonyms:ygdF, ygdO
Ordered Locus Names:b2829, JW2797
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12188. ptsP.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001470951 – 748Phosphoenolpyruvate-dependent phosphotransferase systemAdd BLAST748

Proteomic databases

EPDiP37177.
PaxDbiP37177.
PRIDEiP37177.

Interactioni

Protein-protein interaction databases

BioGridi4263274. 24 interactors.
IntActiP37177. 10 interactors.
STRINGi511145.b2829.

Structurei

3D structure databases

ProteinModelPortaliP37177.
SMRiP37177.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 127GAF1 PublicationAdd BLAST127

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni128 – 170Linker1 PublicationAdd BLAST43
Regioni171 – 748PTS EI1 PublicationAdd BLAST578
Regioni620 – 621PEP bindingBy similarity2

Domaini

The 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
The GAF domain is an important site of signal perception in prokaryotes and eukaryotes.Curated

Sequence similaritiesi

Belongs to the PEP-utilizing enzyme family.Curated
Contains 1 GAF domain.1 Publication

Phylogenomic databases

eggNOGiENOG4108HRM. Bacteria.
COG3605. LUCA.
HOGENOMiHOG000278514.
InParanoidiP37177.
KOiK08484.
OMAiMFPMISE.
PhylomeDBiP37177.

Family and domain databases

Gene3Di1.10.274.10. 1 hit.
3.20.20.60. 1 hit.
3.30.450.40. 1 hit.
3.50.30.10. 1 hit.
InterProiIPR003018. GAF.
IPR029016. GAF_dom-like.
IPR008279. PEP-util_enz_mobile_dom.
IPR018274. PEP_util_AS.
IPR000121. PEP_util_C.
IPR023151. PEP_util_CS.
IPR006318. PTS_EI-like.
IPR008731. PTS_EIN.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
PfamiPF01590. GAF. 1 hit.
PF05524. PEP-utilisers_N. 1 hit.
PF00391. PEP-utilizers. 1 hit.
PF02896. PEP-utilizers_C. 1 hit.
[Graphical view]
SMARTiSM00065. GAF. 1 hit.
[Graphical view]
SUPFAMiSSF47831. SSF47831. 1 hit.
SSF51621. SSF51621. 1 hit.
SSF52009. SSF52009. 1 hit.
SSF55781. SSF55781. 1 hit.
TIGRFAMsiTIGR01417. PTS_I_fam. 1 hit.
PROSITEiPS00742. PEP_ENZYMES_2. 1 hit.
PS00370. PEP_ENZYMES_PHOS_SITE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P37177-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLTRLREIVE KVASAPRLNE ALNILVTDIC LAMDTEVCSV YLADHDRRCY
60 70 80 90 100
YLMATRGLKK PRGRTVTLAF DEGIVGLVGR LAEPINLADA QKHPSFKYIP
110 120 130 140 150
SVKEERFRAF LGVPIIQRRQ LLGVLVVQQR ELRQYDESEE SFLVTLATQM
160 170 180 190 200
AAILSQSQLT ALFGQYRQTR IRALPAAPGV AIAEGWQDAT LPLMEQVYQA
210 220 230 240 250
STLDPALERE RLTGALEEAA NEFRRYSKRF AAGAQKETAA IFDLYSHLLS
260 270 280 290 300
DTRLRRELFA EVDKGSVAEW AVKTVIEKFA EQFAALSDNY LKERAGDLRA
310 320 330 340 350
LGQRLLFHLD DANQGPNAWP ERFILVADEL SATTLAELPQ DRLVGVVVRD
360 370 380 390 400
GAANSHAAIM VRALGIPTVM GADIQPSVLH RRTLIVDGYR GELLVDPEPV
410 420 430 440 450
LLQEYQRLIS EEIELSRLAE DDVNLPAQLK SGERIKVMLN AGLSPEHEEK
460 470 480 490 500
LGSRIDGIGL YRTEIPFMLQ SGFPSEEEQV AQYQGMLQMF NDKPVTLRTL
510 520 530 540 550
DVGADKQLPY MPISEENPCL GWRGIRITLD QPEIFLIQVR AMLRANAATG
560 570 580 590 600
NLNILLPMVT SLDEVDEARR LIERAGREVE EMIGYEIPKP RIGIMLEVPS
610 620 630 640 650
MVFMLPHLAK RVDFISVGTN DLTQYILAVD RNNTRVANIY DSLHPAMLRA
660 670 680 690 700
LAMIAREAEI HGIDLRLCGE MAGDPMCVAI LIGLGYRHLS MNGRSVARAK
710 720 730 740
YLLRRIDYAE AENLAQRSLE AQLATEVRHQ VAAFMERRGM GGLIRGGL
Length:748
Mass (Da):83,716
Last modified:November 1, 1995 - v2
Checksum:iAC7137BD0AEBBF01
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U29581 Genomic DNA. Translation: AAB40476.1.
U00096 Genomic DNA. Translation: AAC75868.1.
AP009048 Genomic DNA. Translation: BAE76898.1.
U12289 Genomic DNA. Translation: AAA69023.1.
PIRiF65065.
RefSeqiNP_417306.1. NC_000913.3.
WP_000957910.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75868; AAC75868; b2829.
BAE76898; BAE76898; BAE76898.
GeneIDi947301.
KEGGiecj:JW2797.
eco:b2829.
PATRICi32121076. VBIEscCol129921_2927.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U29581 Genomic DNA. Translation: AAB40476.1.
U00096 Genomic DNA. Translation: AAC75868.1.
AP009048 Genomic DNA. Translation: BAE76898.1.
U12289 Genomic DNA. Translation: AAA69023.1.
PIRiF65065.
RefSeqiNP_417306.1. NC_000913.3.
WP_000957910.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP37177.
SMRiP37177.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263274. 24 interactors.
IntActiP37177. 10 interactors.
STRINGi511145.b2829.

Proteomic databases

EPDiP37177.
PaxDbiP37177.
PRIDEiP37177.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75868; AAC75868; b2829.
BAE76898; BAE76898; BAE76898.
GeneIDi947301.
KEGGiecj:JW2797.
eco:b2829.
PATRICi32121076. VBIEscCol129921_2927.

Organism-specific databases

EchoBASEiEB2105.
EcoGeneiEG12188. ptsP.

Phylogenomic databases

eggNOGiENOG4108HRM. Bacteria.
COG3605. LUCA.
HOGENOMiHOG000278514.
InParanoidiP37177.
KOiK08484.
OMAiMFPMISE.
PhylomeDBiP37177.

Enzyme and pathway databases

BioCyciEcoCyc:EG12188-MONOMER.
ECOL316407:JW2797-MONOMER.

Miscellaneous databases

PROiP37177.

Family and domain databases

Gene3Di1.10.274.10. 1 hit.
3.20.20.60. 1 hit.
3.30.450.40. 1 hit.
3.50.30.10. 1 hit.
InterProiIPR003018. GAF.
IPR029016. GAF_dom-like.
IPR008279. PEP-util_enz_mobile_dom.
IPR018274. PEP_util_AS.
IPR000121. PEP_util_C.
IPR023151. PEP_util_CS.
IPR006318. PTS_EI-like.
IPR008731. PTS_EIN.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
PfamiPF01590. GAF. 1 hit.
PF05524. PEP-utilisers_N. 1 hit.
PF00391. PEP-utilizers. 1 hit.
PF02896. PEP-utilizers_C. 1 hit.
[Graphical view]
SMARTiSM00065. GAF. 1 hit.
[Graphical view]
SUPFAMiSSF47831. SSF47831. 1 hit.
SSF51621. SSF51621. 1 hit.
SSF52009. SSF52009. 1 hit.
SSF55781. SSF55781. 1 hit.
TIGRFAMsiTIGR01417. PTS_I_fam. 1 hit.
PROSITEiPS00742. PEP_ENZYMES_2. 1 hit.
PS00370. PEP_ENZYMES_PHOS_SITE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPT1P_ECOLI
AccessioniPrimary (citable) accession number: P37177
Secondary accession number(s): Q2MA08
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: November 1, 1995
Last modified: November 2, 2016
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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

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.