Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

PTS system glucose-specific EIICB component

Gene

ptsG

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

Functioni

The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II complex composed of PtsG and Crr is involved in glucose transport (PubMed:3129430, PubMed:10562420). Also functions as a chemoreceptor monitoring the environment for changes in sugar concentration and an effector modulating the activity of the transcriptional repressor Mlc (PubMed:18319344).3 Publications

Catalytic activityi

[Protein]-N(pi)-phospho-L-histidine + D-glucose(Side 1) = [protein]-L-histidine + D-glucose 6-phosphate(Side 2).1 Publication

Enzyme regulationi

Transporter activity may be inhibited by SgrT.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei421 – 4211Phosphocysteine intermediate; for EIIB activityPROSITE-ProRule annotation3 Publications

GO - Molecular functioni

GO - Biological processi

  • glucose transport Source: CACAO
  • phosphoenolpyruvate-dependent sugar phosphotransferase system Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Phosphotransferase system, Sugar transport, Transport

Enzyme and pathway databases

BioCyciEcoCyc:PTSG-MONOMER.
ECOL316407:JW1087-MONOMER.
MetaCyc:PTSG-MONOMER.

Protein family/group databases

MoonProtiP69786.
TCDBi4.A.1.1.1. the pts glucose-glucoside (glc) family.

Names & Taxonomyi

Protein namesi
Recommended name:
PTS system glucose-specific EIICB component1 Publication
Alternative name(s):
EIICB-Glc1 Publication
Short name:
EII-Glc1 Publication
Including the following 2 domains:
Glucose permease IIC component1 Publication
Alternative name(s):
PTS system glucose-specific EIIC component1 Publication
Glucose-specific phosphotransferase enzyme IIB component1 Publication (EC:2.7.1.1991 Publication)
Alternative name(s):
PTS system glucose-specific EIIB component1 Publication
Gene namesi
Name:ptsG
Synonyms:glcA, umg
Ordered Locus Names:b1101, JW1087
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10787. ptsG.

Subcellular locationi

  • Cell inner membrane PROSITE-ProRule annotation1 Publication; Multi-pass membrane protein PROSITE-ProRule annotation

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1414CytoplasmicSequence analysisAdd
BLAST
Transmembranei15 – 3521HelicalPROSITE-ProRule annotationAdd
BLAST
Topological domaini36 – 5015PeriplasmicSequence analysisAdd
BLAST
Transmembranei51 – 7121HelicalPROSITE-ProRule annotationAdd
BLAST
Topological domaini72 – 798CytoplasmicSequence analysis
Transmembranei80 – 10021HelicalPROSITE-ProRule annotationAdd
BLAST
Topological domaini101 – 11111PeriplasmicSequence analysisAdd
BLAST
Transmembranei112 – 13221HelicalPROSITE-ProRule annotationAdd
BLAST
Topological domaini133 – 15119CytoplasmicSequence analysisAdd
BLAST
Transmembranei152 – 17221HelicalPROSITE-ProRule annotationAdd
BLAST
Topological domaini173 – 19018PeriplasmicSequence analysisAdd
BLAST
Transmembranei191 – 21121HelicalPROSITE-ProRule annotationAdd
BLAST
Topological domaini212 – 24938CytoplasmicSequence analysisAdd
BLAST
Transmembranei250 – 27021HelicalPROSITE-ProRule annotationAdd
BLAST
Topological domaini271 – 2799PeriplasmicSequence analysis
Transmembranei280 – 30021HelicalPROSITE-ProRule annotationAdd
BLAST
Topological domaini301 – 3099CytoplasmicSequence analysis
Transmembranei310 – 33021HelicalPROSITE-ProRule annotationAdd
BLAST
Topological domaini331 – 35525PeriplasmicSequence analysisAdd
BLAST
Transmembranei356 – 37621HelicalPROSITE-ProRule annotationAdd
BLAST
Topological domaini377 – 477101CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cytosol Source: EcoCyc
  • integral component of plasma membrane Source: EcoCyc
  • plasma membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi204 – 2041C → S: Destabilizes the protein structure; when associated with S-326. 1 Publication
Mutagenesisi326 – 3261C → S: Destabilizes the protein structure; when associated with S-204. 1 Publication
Mutagenesisi421 – 4211C → S: Unable to be phosphorylated and to catalyze the phosphoryl exchange between glucose and glucose 6-phosphate at equilibrium. 1 Publication
Mutagenesisi449 – 4491V → Q: Interaction with Mlc is hardly detectable. 1 Publication
Mutagenesisi451 – 4511A → F: The complex with mlc shows much weaker association than the wild-type. 1 Publication
Mutagenesisi456 – 4561Q → A: Interaction with Mlc is hardly detectable. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 477477PTS system glucose-specific EIICB componentPRO_0000186528Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei421 – 4211Phosphocysteine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP69786.
PaxDbiP69786.
PRIDEiP69786.

Expressioni

Inductioni

The ptsG transcript is degraded under conditions of glucose-phosphate stress (due to intracellular accumulation of glucose-6-phosphate caused by disruption of glycolytic flux), or in the presence of (toxic) non-metabolizable glucose phosphate analogs due to hybridization with the small RNA sgrS (originally known as ryaA). This hybridization is sufficient to repress mRNA translation (PubMed:16549791). The hybrid is subsequently degraded by RNase E. This reduces the quantity of transporter and relieves glucose phosphate stress.2 Publications

Interactioni

Subunit structurei

Homodimer.1 Publication3 Publications

Protein-protein interaction databases

BioGridi4260940. 8 interactions.
DIPiDIP-29833N.
IntActiP69786. 3 interactions.
STRINGi511145.b1101.

Structurei

Secondary structure

1
477
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi401 – 4088Combined sources
Helixi412 – 4143Combined sources
Beta strandi415 – 4206Combined sources
Beta strandi422 – 4309Combined sources
Helixi432 – 4343Combined sources
Helixi437 – 4426Combined sources
Beta strandi446 – 4516Combined sources
Beta strandi454 – 4585Combined sources
Helixi460 – 4623Combined sources
Helixi463 – 47513Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IBANMR-A391-476[»]
1O2FNMR-B387-476[»]
3BP3X-ray1.65A/B396-477[»]
3BP8X-ray2.85C/D401-475[»]
ProteinModelPortaliP69786.
SMRiP69786. Positions 396-476.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP69786.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 388388PTS EIIC type-1PROSITE-ProRule annotationAdd
BLAST
Domaini399 – 47779PTS EIIB type-1PROSITE-ProRule annotationAdd
BLAST

Domaini

The EIIB domain is phosphorylated by phospho-EIIA on a cysteinyl or histidyl residue, depending on the transported sugar. Then, it transfers the phosphoryl group to the sugar substrate concomitantly with the sugar uptake processed by the EIIC domain.PROSITE-ProRule annotation
The EIIC domain forms the PTS system translocation channel and contains the specific substrate-binding site.PROSITE-ProRule annotation

Sequence similaritiesi

Contains 1 PTS EIIB type-1 domain.PROSITE-ProRule annotation
Contains 1 PTS EIIC type-1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105CI1. Bacteria.
COG1263. LUCA.
COG1264. LUCA.
HOGENOMiHOG000250993.
KOiK02778.
K02779.
OMAiMQIGEFT.
PhylomeDBiP69786.

Family and domain databases

CDDicd00212. PTS_IIB_glc. 1 hit.
Gene3Di3.30.1360.60. 1 hit.
InterProiIPR018113. PTrfase_EIIB_Cys.
IPR003352. PTS_EIIC.
IPR013013. PTS_EIIC_1.
IPR001996. PTS_IIB_1.
IPR011299. PTS_IIBC_glc.
IPR004719. PTS_maltose/Glc_sub_IIC.
[Graphical view]
PfamiPF00367. PTS_EIIB. 1 hit.
PF02378. PTS_EIIC. 1 hit.
[Graphical view]
SUPFAMiSSF55604. SSF55604. 1 hit.
TIGRFAMsiTIGR00826. EIIB_glc. 1 hit.
TIGR00852. pts-Glc. 1 hit.
TIGR02002. PTS-II-BC-glcB. 1 hit.
PROSITEiPS51098. PTS_EIIB_TYPE_1. 1 hit.
PS01035. PTS_EIIB_TYPE_1_CYS. 1 hit.
PS51103. PTS_EIIC_TYPE_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P69786-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFKNAFANLQ KVGKSLMLPV SVLPIAGILL GVGSANFSWL PAVVSHVMAE
60 70 80 90 100
AGGSVFANMP LIFAIGVALG FTNNDGVSAL AAVVAYGIMV KTMAVVAPLV
110 120 130 140 150
LHLPAEEIAS KHLADTGVLG GIISGAIAAY MFNRFYRIKL PEYLGFFAGK
160 170 180 190 200
RFVPIISGLA AIFTGVVLSF IWPPIGSAIQ TFSQWAAYQN PVVAFGIYGF
210 220 230 240 250
IERCLVPFGL HHIWNVPFQM QIGEYTNAAG QVFHGDIPRY MAGDPTAGKL
260 270 280 290 300
SGGFLFKMYG LPAAAIAIWH SAKPENRAKV GGIMISAALT SFLTGITEPI
310 320 330 340 350
EFSFMFVAPI LYIIHAILAG LAFPICILLG MRDGTSFSHG LIDFIVLSGN
360 370 380 390 400
SSKLWLFPIV GIGYAIVYYT IFRVLIKALD LKTPGREDAT EDAKATGTSE
410 420 430 440 450
MAPALVAAFG GKENITNLDA CITRLRVSVA DVSKVDQAGL KKLGAAGVVV
460 470
AGSGVQAIFG TKSDNLKTEM DEYIRNH
Length:477
Mass (Da):50,677
Last modified:August 13, 1987 - v1
Checksum:iD97A80FD64B74F73
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02618 Genomic DNA. Translation: AAA24437.1.
U00096 Genomic DNA. Translation: AAC74185.1.
AP009048 Genomic DNA. Translation: BAA35908.1.
PIRiA25336. WQEC2G.
RefSeqiNP_415619.1. NC_000913.3.
WP_000475719.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74185; AAC74185; b1101.
BAA35908; BAA35908; BAA35908.
GeneIDi945651.
KEGGiecj:JW1087.
eco:b1101.
PATRICi32117443. VBIEscCol129921_1144.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02618 Genomic DNA. Translation: AAA24437.1.
U00096 Genomic DNA. Translation: AAC74185.1.
AP009048 Genomic DNA. Translation: BAA35908.1.
PIRiA25336. WQEC2G.
RefSeqiNP_415619.1. NC_000913.3.
WP_000475719.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IBANMR-A391-476[»]
1O2FNMR-B387-476[»]
3BP3X-ray1.65A/B396-477[»]
3BP8X-ray2.85C/D401-475[»]
ProteinModelPortaliP69786.
SMRiP69786. Positions 396-476.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260940. 8 interactions.
DIPiDIP-29833N.
IntActiP69786. 3 interactions.
STRINGi511145.b1101.

Protein family/group databases

MoonProtiP69786.
TCDBi4.A.1.1.1. the pts glucose-glucoside (glc) family.

Proteomic databases

EPDiP69786.
PaxDbiP69786.
PRIDEiP69786.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74185; AAC74185; b1101.
BAA35908; BAA35908; BAA35908.
GeneIDi945651.
KEGGiecj:JW1087.
eco:b1101.
PATRICi32117443. VBIEscCol129921_1144.

Organism-specific databases

EchoBASEiEB0780.
EcoGeneiEG10787. ptsG.

Phylogenomic databases

eggNOGiENOG4105CI1. Bacteria.
COG1263. LUCA.
COG1264. LUCA.
HOGENOMiHOG000250993.
KOiK02778.
K02779.
OMAiMQIGEFT.
PhylomeDBiP69786.

Enzyme and pathway databases

BioCyciEcoCyc:PTSG-MONOMER.
ECOL316407:JW1087-MONOMER.
MetaCyc:PTSG-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP69786.
PROiP69786.

Family and domain databases

CDDicd00212. PTS_IIB_glc. 1 hit.
Gene3Di3.30.1360.60. 1 hit.
InterProiIPR018113. PTrfase_EIIB_Cys.
IPR003352. PTS_EIIC.
IPR013013. PTS_EIIC_1.
IPR001996. PTS_IIB_1.
IPR011299. PTS_IIBC_glc.
IPR004719. PTS_maltose/Glc_sub_IIC.
[Graphical view]
PfamiPF00367. PTS_EIIB. 1 hit.
PF02378. PTS_EIIC. 1 hit.
[Graphical view]
SUPFAMiSSF55604. SSF55604. 1 hit.
TIGRFAMsiTIGR00826. EIIB_glc. 1 hit.
TIGR00852. pts-Glc. 1 hit.
TIGR02002. PTS-II-BC-glcB. 1 hit.
PROSITEiPS51098. PTS_EIIB_TYPE_1. 1 hit.
PS01035. PTS_EIIB_TYPE_1_CYS. 1 hit.
PS51103. PTS_EIIC_TYPE_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPTGCB_ECOLI
AccessioniPrimary (citable) accession number: P69786
Secondary accession number(s): P05053
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: September 7, 2016
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.