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Reviewed, UniProtKB/Swiss-Prot P69786 (PTGCB_ECOLI)

Last modified November 3, 2009. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    PTS system glucose-specific EIICB component
Alternative name(s):
    EIICB-Glc
      Short name=EII-Glc
Including the following 2 domains:
    1- Recommended name:
            Glucose permease IIC component
        Alternative name(s):
            PTS system glucose-specific EIIC component
    2- Recommended name:
            Glucose-specific phosphotransferase enzyme IIB component
              EC=2.7.1.69
        Alternative name(s):
            PTS system glucose-specific EIIB component
Gene names
Name: ptsG
Synonyms: glcA, umg
Ordered Locus Names: b1101, JW1087
OrganismEscherichia coli (strain K12) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length477 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

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. This system is involved in glucose transport. This enzyme is also a chemoreceptor monitoring the environment for changes in sugar concentration.

Catalytic activity

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

Enzyme regulation

Transporter activity may be inhibited by sgrT. Ref.8

Subcellular location

Cell inner membrane; Multi-pass membrane protein.

Induction

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 (Ref.8). The hybrid is subsequently degraded by RNase E. This reduces the quantity of transporter and relieves glucose phosphate stress. Ref.6

Domain

The EIIC domain forms the PTS system translocation channel and contains the specific substrate-binding site.

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.

Sequence similarities

Contains 1 PTS EIIB type-1 domain.

Contains 1 PTS EIIC type-1 domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

crrP697831EBI-903497,EBI-369856

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 477477PTS system glucose-specific EIICB component
PRO_0000186528

Regions

Topological domain1 – 1414Cytoplasmic Potential
Transmembrane15 – 3521 Potential
Topological domain36 – 5015Periplasmic Potential
Transmembrane51 – 7121 Potential
Topological domain72 – 798Cytoplasmic Potential
Transmembrane80 – 10021 Potential
Topological domain101 – 11111Periplasmic Potential
Transmembrane112 – 13221 Potential
Topological domain133 – 15119Cytoplasmic Potential
Transmembrane152 – 17221 Potential
Topological domain173 – 19018Periplasmic Potential
Transmembrane191 – 21121 Potential
Topological domain212 – 24938Cytoplasmic Potential
Transmembrane250 – 27021 Potential
Topological domain271 – 2799Periplasmic Potential
Transmembrane280 – 30021 Potential
Topological domain301 – 3099Cytoplasmic Potential
Transmembrane310 – 33021 Potential
Topological domain331 – 35525Periplasmic Potential
Transmembrane356 – 37621 Potential
Topological domain377 – 477101Cytoplasmic Potential
Domain1 – 388388PTS EIIC type-1
Domain399 – 47779PTS EIIB type-1

Sites

Active site4211Phosphocysteine intermediate; for EIIB activity

Secondary structure

.................. 477
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P69786-1 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: D97A80FD64B74F73

FASTA47750,677
        10         20         30         40         50         60 
MFKNAFANLQ KVGKSLMLPV SVLPIAGILL GVGSANFSWL PAVVSHVMAE AGGSVFANMP 

        70         80         90        100        110        120 
LIFAIGVALG FTNNDGVSAL AAVVAYGIMV KTMAVVAPLV LHLPAEEIAS KHLADTGVLG 

       130        140        150        160        170        180 
GIISGAIAAY MFNRFYRIKL PEYLGFFAGK RFVPIISGLA AIFTGVVLSF IWPPIGSAIQ 

       190        200        210        220        230        240 
TFSQWAAYQN PVVAFGIYGF IERCLVPFGL HHIWNVPFQM QIGEYTNAAG QVFHGDIPRY 

       250        260        270        280        290        300 
MAGDPTAGKL SGGFLFKMYG LPAAAIAIWH SAKPENRAKV GGIMISAALT SFLTGITEPI 

       310        320        330        340        350        360 
EFSFMFVAPI LYIIHAILAG LAFPICILLG MRDGTSFSHG LIDFIVLSGN SSKLWLFPIV 

       370        380        390        400        410        420 
GIGYAIVYYT IFRVLIKALD LKTPGREDAT EDAKATGTSE MAPALVAAFG GKENITNLDA 

       430        440        450        460        470 
CITRLRVSVA DVSKVDQAGL KKLGAAGVVV AGSGVQAIFG TKSDNLKTEM DEYIRNH 

« Hide

References

« Hide 'large scale' references
[1]"Glucose permease of the bacterial phosphotransferase system. Gene cloning, overproduction, and amino acid sequence of enzyme IIGlc."
Erni B., Zanolari B.
J. Biol. Chem. 261:16398-16403(1986) [PubMed: 3023349] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-16.
Strain: K12.
[2]"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map."
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. expand/collapse author list , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T.
DNA Res. 3:137-155(1996) [PubMed: 8905232] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"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.
[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]"Cysteine phosphorylation of the glucose transporter of Escherichia coli."
Meins M., Jenoe P., Mueller D., Richter W.J., Rosenbusch J.P., Erni B.
J. Biol. Chem. 268:11604-11609(1993) [PubMed: 8505292] [Abstract]
Cited for: PHOSPHORYLATION AT CYS-421.
[6]"Involvement of a novel transcriptional activator and small RNA in post-transcriptional regulation of the glucose phosphoenolpyruvate phosphotransferase system."
Vanderpool C.K., Gottesman S.
Mol. Microbiol. 54:1076-1089(2004) [PubMed: 15522088] [Abstract]
Cited for: INDUCTION BY POST-TRANSCRIPTIONAL RNA REGULATION.
Strain: K12 / MG1655 / ATCC 47076.
[7]"Global topology analysis of the Escherichia coli inner membrane proteome."
Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
Science 308:1321-1323(2005) [PubMed: 15919996] [Abstract]
Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
Strain: K12 / MG1655 / ATCC 47076.
[8]"Translational repression is sufficient for gene silencing by bacterial small noncoding RNAs in the absence of mRNA destruction."
Morita T., Mochizuki Y., Aiba H.
Proc. Natl. Acad. Sci. U.S.A. 103:4858-4863(2006) [PubMed: 16549791] [Abstract]
Cited for: ENZYME REGULATION.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[9]"The glucose transporter of Escherichia coli. Assignment of the 1H, 13C and 15N resonances and identification of the secondary structure of the soluble IIB domain."
Golic Grdadolnik S., Eberstadt M., Gemmecker G., Kessler H., Buhr A., Erni B.
Eur. J. Biochem. 219:945-952(1994) [PubMed: 8112346] [Abstract]
Cited for: STRUCTURE BY NMR OF 391-476.
[10]"Solution structure of the IIB domain of the glucose transporter of Escherichia coli."
Eberstadt M., Golic Grdadolnik S., Gemmecker G., Kessler H., Buhr A., Erni B.
Biochemistry 35:11286-11292(1996) [PubMed: 8784182] [Abstract]
Cited for: STRUCTURE BY NMR OF 386-477.
[11]"Glucose transporter of Escherichia coli: NMR characterization of the phosphocysteine form of the IIB(Glc) domain and its binding interface with the IIA(Glc) subunit."
Gemmecker G., Eberstadt M., Buhr A., Lanz R., Golic Grdadolnik S., Kessler H., Erni B.
Biochemistry 36:7408-7417(1997) [PubMed: 9200688] [Abstract]
Cited for: STRUCTURE BY NMR OF 386-477.
+Additional computationally mapped references.

Cross-references

Sequence databases

J02618 Genomic DNA. Translation: AAA24437.1.
U00096 Genomic DNA. Translation: AAC74185.1.
AP009048 Genomic DNA. Translation: BAA35908.1.
PIRWQEC2G. A25336.
RefSeqAP_001727.1.
NP_415619.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1IBANMR-A391-476[»]
1O2FNMR-B387-476[»]
3BP3X-ray1.65A/B396-477[»]
3BP8X-ray2.85C/D401-475[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP69786. 1 interaction.
STRINGP69786.

Protein family/group databases

TCDB4.A.1.1.1. PTS glucose-glucoside (Glc) family.

2-D gel databases

ECO2DBASEH042.6. 6TH EDITION.
H042.7. 6TH EDITION.

Proteomic databases

PRIDEP69786.

Genome annotation databases

GeneID945651.
GenomeReviewsGene locus JW1087 in contig AP009048_GR.
Gene locus b1101 in contig U00096_GR.
KEGGecj:JW1087.
eco:b1101.

Organism-specific databases

EchoBASEEB0780.
EcoGeneEG10787. ptsG.
CMRSearch...

Phylogenomic databases

HOGENOMP69786.
OMANNDGVAG.

Enzyme and pathway databases

BioCycEcoCyc:PTSG-MON.

Gene expression databases

GenevestigatorP69786.

Family and domain databases

InterProIPR018113. PTrfase_EIIB/Cys_phosph_CS.
IPR004719. PTrfase_sys_maltose/Glc-sp_IIC.
IPR001996. PTS_EIIB.
IPR003352. PTS_EIIC.
IPR013013. PTS_EIIC_1.
IPR011535. PTS_Glc-like_IIB_component.
IPR011299. PTS_IIBC_glc.
[Graphical view]
Gene3DG3DSA:3.30.1360.60. PTS_EIIB. 1 hit.
PfamPF00367. PTS_EIIB. 1 hit.
PF02378. PTS_EIIC. 1 hit.
[Graphical view]
TIGRFAMsTIGR00826. EIIB_glc. 1 hit.
TIGR00852. pts-Glc. 1 hit.
TIGR02002. PTS-II-BC-glcB. 1 hit.
PROSITEPS51098. PTS_EIIB_TYPE_1. 1 hit.
PS01035. PTS_EIIB_TYPE_1_CYS. 1 hit.
PS51103. PTS_EIIC_TYPE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePTGCB_ECOLI
AccessionPrimary (citable) accession number: P69786
Secondary accession number(s): P05053
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: November 3, 2009
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Escherichia coli

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents