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Reviewed, UniProtKB/Swiss-Prot Q45298 (PTG3B_CORGL)

Last modified June 16, 2009. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    PTS system glucose-specific EIIBCA component
Alternative name(s):
    EIIBCA-Glc
    EII-Glc/EIII-Glc
Including the following 3 domains:
    1- Recommended name:
            Glucose-specific phosphotransferase enzyme IIB component
              EC=2.7.1.69
        Alternative name(s):
            PTS system glucose-specific EIIB component
    2- Recommended name:
            Glucose permease IIC component
        Alternative name(s):
            PTS system glucose-specific EIIC component
    3- Recommended name:
            Glucose-specific phosphotransferase enzyme IIA component
              EC=2.7.1.-
        Alternative name(s):
            PTS system glucose-specific EIIA component
Gene names
Name: ptsG
Encoded onPlasmid pBSBG2
OrganismCorynebacterium glutamicum (Brevibacterium flavum)
Taxonomic identifier1718 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length674 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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 EIIA N(pi)-phospho-L-histidine + protein EIIB = protein EIIA + protein EIIB N(pi)-phospho-L-histidine/cysteine.

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

Subcellular location

Cell membrane; Multi-pass membrane protein Potential.

Domain

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.

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

The EIIA domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the EIIB domain.

Sequence similarities

Contains 1 PTS EIIA type-1 domain.

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 – 674674PTS system glucose-specific EIIBCA component
PRO_0000186558

Regions

Transmembrane126 – 14621 Potential
Transmembrane162 – 18221 Potential
Transmembrane193 – 21321 Potential
Transmembrane225 – 24521 Potential
Transmembrane260 – 28021 Potential
Transmembrane303 – 32321 Potential
Transmembrane344 – 36421 Potential
Transmembrane376 – 39621 Potential
Transmembrane409 – 42921 Potential
Transmembrane442 – 46221 Potential
Domain1 – 8989PTS EIIB type-1
Domain117 – 476360PTS EIIC type-1
Domain542 – 646105PTS EIIA type-1

Sites

Active site281Phosphocysteine intermediate; for EIIB activity By similarity
Active site5941Tele-phosphohistidine intermediate; for EIIA activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q45298-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 67A75AAF76E42FA2

FASTA67471,626
        10         20         30         40         50         60 
MASKLTTTSQ HILENLGGPD NITSMTHCAT RLRFQVKDQS IVDQQEIDSD PSVLGVVPQG 

        70         80         90        100        110        120 
STGMQVVMGG SVANYYQEIL KLDGMKHFAD GEATESSSKK EYGGVRGKYS GIDYAFEFLS 

       130        140        150        160        170        180 
DTFRPILWAL LGASLIITLL VLADTFGLQD FRAPMDEQPD TYVFLHSMWR SVFYFLPIMV 

       190        200        210        220        230        240 
GATAARKLGA NEWIGAAIPA ALLTPEFLAL GSAGDTVTVF GLPMVLNDYS GQVFPPLIAA 

       250        260        270        280        290        300 
IGLYWVEKAL KKIIPEAVQM VFVPFFSLLI MIPATAFLLG PFGIGVGNGI SSLLEAVNNF 

       310        320        330        340        350        360 
SPFILSIVIP LLYPFLVPLG LHWPLNAIMI QNLNTLGYDF IQGPMGAWNF ACFGLVTGVF 

       370        380        390        400        410        420 
LIALKEKNRA MRQVSLGGML AGLLGGISEP SLYGVLLRFK KTYFRLLPGC LVGGIVMGIF 

       430        440        450        460        470        480 
DIKAYAFVFT SLLTIPAMDP WLGYTVGIAA AFFTSMLLVL FFDYRSDAER DEAKAQMAAA 

       490        500        510        520        530        540 
EQTNNTPAAP AAPVAPAAGA AAAGGAAGAT AVATKPRLAA GQLVEITSPL EGHAVPLSEV 

       550        560        570        580        590        600 
PDPIFAAGKL GPGIAIEPTG NTVVAPADAT VILVQKSGHA VALRLESGVE LLIHIGLDTV 

       610        620        630        640        650        660 
QLGGEGFKVH VERKQQVKAG DPLITFDPEF IRSKNLPLIT PVVVSNANKF GEIVGIEAAQ 

       670 
ADATTTVIKV NGAE 

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References

[1]"Cloning and nucleotide sequence of enzyme II of Brevibacterium lactofermentum phosphotransferase system."
Yoon K.-H.
Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 13869 / DSMZ 1412 / NCIMB 9567.

Cross-references

Sequence databases

L18875 Genomic DNA. Translation: AAA22992.1.

3D structure databases

HSSPHSSP built from PDB template 1GLC based on UniProtKB P08837.
ModBaseSearch...

Enzyme and pathway databases

BRENDA2.7.1.69. 812.

Family and domain databases

InterProIPR018113. PTrfase_EIIB/Cys_phospho_site.
IPR001127. PTS_EIIA_1_perm.
IPR001996. PTS_EIIB.
IPR003352. PTS_EIIC.
IPR013013. PTS_EIIC_1.
[Graphical view]
Gene3DG3DSA:3.30.1360.60. PTS_EIIB. 1 hit.
PfamPF00358. PTS_EIIA_1. 1 hit.
PF00367. PTS_EIIB. 1 hit.
PF02378. PTS_EIIC. 1 hit.
[Graphical view]
ProDomPD001476. Ptrans_EIIB. 1 hit.
PD002243. PTS_EIIA. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00830. PTBA. 1 hit.
PROSITEPS51093. PTS_EIIA_TYPE_1. 1 hit.
PS00371. PTS_EIIA_TYPE_1_HIS. 1 hit.
PS51098. 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 namePTG3B_CORGL
AccessionPrimary (citable) accession number: Q45298
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: June 16, 2009
This is version 67 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

SIMILARITY comments

Index of protein domains and families

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