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Q89AG6 (PTGCB_BUCBP) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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. Glucose permease IIC component
    Alternative name(s):
    PTS system glucose-specific EIIC component
  2. Glucose-specific phosphotransferase enzyme IIB component
    EC=2.7.1.69
    Alternative name(s):
    PTS system glucose-specific EIIB component
Gene names
Name:ptsG
Ordered Locus Names:bbp_326
OrganismBuchnera aphidicola subsp. Baizongia pistaciae (strain Bp) [Complete proteome] [HAMAP]
Taxonomic identifier224915 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length479 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity.

Catalytic activity

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

Subcellular location

Cell membrane; Multi-pass membrane protein By similarity.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 479479PTS system glucose-specific EIICB component
PRO_0000186527

Regions

Transmembrane15 – 3521Helical; Potential
Transmembrane51 – 7121Helical; Potential
Transmembrane80 – 10021Helical; Potential
Transmembrane112 – 13221Helical; Potential
Transmembrane152 – 17221Helical; Potential
Transmembrane252 – 27221Helical; Potential
Transmembrane280 – 30021Helical; Potential
Transmembrane305 – 32521Helical; Potential
Transmembrane356 – 37621Helical; Potential
Domain1 – 388388PTS EIIC type-1
Domain399 – 47981PTS EIIB type-1

Sites

Active site4211Phosphocysteine intermediate; for EIIB activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q89AG6 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: FF1B60760B4D9ABD

FASTA47952,157
        10         20         30         40         50         60 
MFKNAFSNLQ KIGRSLMLPV SVLPIAGILL GIGSANFKII PHTISNIMTE AGSSVFSNMP 

        70         80         90        100        110        120 
LIFAIGIALG FTKNDGVSAL AAVVSYGIMT KTLSITIPIF SNLSDINVNQ KYLLDTGILG 

       130        140        150        160        170        180 
GIIAGSISAY IFNTFYRIQL PEYLGFFAGR RFVPIASGLI SIIFGCILSI IWPPIGNVIK 

       190        200        210        220        230        240 
TFSEWAAYQN PTLAFGIYGT VERALVPFGL HHIWNVPFQM QIGEYNNSIG QIFHGDIARY 

       250        260        270        280        290        300 
MAGDSTAGKL SGGFIFKMYG LPFAALAMWH CANKKNKAKI GGIMMSGALT AILTGITEPI 

       310        320        330        340        350        360 
EFSFILVAPI LYVIHAILAG LAFPICILLN MRSGTSFSHG LIDFIVLSGN SNNFWLFPIV 

       370        380        390        400        410        420 
GLFYGILYYG IFYFMIKKFN LKTPGREKSI TYINQKTIKE TALLVISILG GKTNIINLDA 

       430        440        450        460        470 
CITRLRITVL DISKVNQKKL KNLGASGVIV SGSGIQIVFG TQSDHIKTEI DNYMSNTNQ

« Hide

References

[1]"Reductive genome evolution in Buchnera aphidicola."
van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.
Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003) [PubMed: 12522265] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bp.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE016826 Genomic DNA. Translation: AAO27048.1.
RefSeqNP_777943.1. NC_004545.1.

3D structure databases

ProteinModelPortalQ89AG6.
SMRQ89AG6. Positions 405-476.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBUCT00000002366; EBBUCP00000002190; EBBUCG00000002366.
GeneID1058276.
GenomeReviewsGene locus bbp_326 in contig AE016826_GR.
KEGGbab:bbp326.
PATRIC21245441. VBIBucAph80364_0320.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000007830.
HOGENOMHBG571563.
OMAILSFIWP.
ProtClustDBPRK11089.

Enzyme and pathway databases

BioCycBAPH224915:BBP_326-MONOMER.

Family and domain databases

InterProIPR018113. PTrfase_EIIB/Cys_phosph_CS.
IPR001996. PTS_EIIB_1.
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.
KOK02778.
K02779.
PfamPF00367. PTS_EIIB. 1 hit.
PF02378. PTS_EIIC. 1 hit.
[Graphical view]
SUPFAMSSF55604. PTS_EIIB. 1 hit.
TIGRFAMsTIGR00826. EIIB_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_BUCBP
AccessionPrimary (citable) accession number: Q89AG6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 14, 2003
Last sequence update: June 1, 2003
Last modified: January 25, 2012
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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