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P75569 (PTG3C_MYCPN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
PTS system glucose-specific EIICBA component
Alternative name(s):
EII-Glc/EIII-Glc
EIICBA-Glc

Including the following 3 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
  3. Glucose-specific phosphotransferase enzyme IIA component
    EC=2.7.1.-
    Alternative name(s):
    PTS system glucose-specific EIIA component
Gene names
Name:ptsG
Ordered Locus Names:MPN_207
ORF Names:MP624
OrganismMycoplasma pneumoniae (strain ATCC 29342 / M129)
Taxonomic identifier272634 [NCBI]
Taxonomic lineageBacteriaTenericutesMollicutesMycoplasmataceaeMycoplasma

Protein attributes

Sequence length940 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 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 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.

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 – 940940PTS system glucose-specific EIICBA component
PRO_0000186560

Regions

Transmembrane43 – 6321Helical; Potential
Transmembrane83 – 10321Helical; Potential
Transmembrane112 – 13221Helical; Potential
Transmembrane175 – 19521Helical; Potential
Transmembrane209 – 22921Helical; Potential
Transmembrane487 – 50721Helical; Potential
Transmembrane515 – 53521Helical; Potential
Transmembrane537 – 55721Helical; Potential
Transmembrane564 – 58421Helical; Potential
Transmembrane598 – 61821Helical; Potential
Domain1 – 284284PTS EIIC type-1; first part
Domain479 – 630152PTS EIIC type-1; second part
Domain661 – 74383PTS EIIB type-1
Domain794 – 907114PTS EIIA type-1
Region285 – 478194Unknown

Sites

Active site6831Phosphocysteine intermediate; for EIIB activity By similarity
Active site8471Tele-phosphohistidine intermediate; for EIIA activity By similarity

Sequences

Sequence LengthMass (Da)Tools
P75569 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 44B836307FDA36EF

FASTA940101,619
        10         20         30         40         50         60 
MQIKAQDTGQ QKKSCLLSNI RNKWKNRNRG SFRQWVGKLS NGLMIPIAVL PIAGIFLGVG 

        70         80         90        100        110        120 
DAIAGNAGDL TGLRYFGLFI KNGGDVVFAN LPILFAIAIA ITFSQDAGVA GFSAFVFWAA 

       130        140        150        160        170        180 
MNGFMSSLIL PFDKAGKIIT DTSTPIAGFK VLYNKSVPVH AIATTLGLRT LSTSVFGGII 

       190        200        210        220        230        240 
VGALTSVLYK KFYAIRLPDV IGFFSGTRFV PIICFVVAIP VALILLMIWP AVSIGLNAIG 

       250        260        270        280        290        300 
TGLGFLGGKG YGANSLIFGY IERSLIPFGV HHAFYAPLWY TSAGGSLQEI VNQQVWIRPD 

       310        320        330        340        350        360 
FHLSDNYVAR VIGWVDPNNS SMYIIPGALN GQNGSSTGNT MSKDLNGALS AYMSKESTAF 

       370        380        390        400        410        420 
LTWKDLVDGL TFKGNFDKMA ENGLLDGSNK IWLGLNGSGI LGKKLLLSDG NVYTITFKTF 

       430        440        450        460        470        480 
ANTTPIAWSK GAQAVLPLNA SSTIVNNPTA LAAATQSNNN TNNIKLYPVN SFRVAVESLN 

       490        500        510        520        530        540 
PAQYSQGKFP FMLFGIPAAG VAMILAAPKD RRKEAASIVG SAAFTSFLTG ITEPFEFTFL 

       550        560        570        580        590        600 
FLAPWLFYGV HAVLAAVSFW LMNILGANVG QTFSGSFIDF ILYGALPDGR RWLANSYLVP 

       610        620        630        640        650        660 
IIGLFLAAIY FPTFYFLIKH FNLATPGRGG KLITKKEYLA SKAAAKAEGV SGVAENFTQT 

       670        680        690        700        710        720 
QIEAGILLQA YGGKENIVEL GACITKLRVT VKNPELVKEE PIKELGAAGV MRTTPTFFVA 

       730        740        750        760        770        780 
VFGTRAAVYK SAMQDIIQGK VNWEALQKVI NTDQLAVEPK ETTPPKEVMP VVQDEIVILS 

       790        800        810        820        830        840 
PVNGTLKSLN QVPDETFKQK LVGEGVAIVP SDGHFKAPGE AGVKTELAFP GGHAYIFDID 

       850        860        870        880        890        900 
GIKVMLHIGI DTVQINAKKQ PGEPLEVFDI KTKQGEYTKE KSESVVEVDL KKLSKKYNPI 

       910        920        930        940 
TPFVVMKESL ENFKLVPIRQ RGEIKVGQPI FKLVYKKSQA 

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References

[1]"Complete sequence analysis of the genome of the bacterium Mycoplasma pneumoniae."
Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.
Nucleic Acids Res. 24:4420-4449(1996) [PubMed: 8948633] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29342 / M129.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U00089 Genomic DNA. Translation: AAB96272.1.
PIRS73950.
RefSeqNP_109895.1. NC_000912.1.

3D structure databases

ProteinModelPortalP75569.
ModBaseSearch...

Protein-protein interaction databases

IntActP75569. 4 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID876972.
GenomeReviewsGene locus MPN_207 in contig U00089_GR.
KEGGmpn:MPN207.
PATRIC20021739. VBIMycPne110_0226.

Phylogenomic databases

HOGENOMHBG571563.
OMAIFGYIER.
PhylomeDBP75569.
ProtClustDBCLSK542132.

Enzyme and pathway databases

BioCycMPNE272634:MPN207-MONOMER.

Family and domain databases

InterProIPR011055. Dup_hybrid_motif.
IPR018113. PTrfase_EIIB/Cys_phosph_CS.
IPR001127. PTS_EIIA_1_perm.
IPR001996. PTS_EIIB_1.
IPR003352. PTS_EIIC.
IPR013013. PTS_EIIC_1.
IPR011535. PTS_Glc-like_IIB_component.
[Graphical view]
Gene3DG3DSA:3.30.1360.60. PTS_EIIB. 1 hit.
KOK02777.
K02778.
K02779.
PfamPF00358. PTS_EIIA_1. 1 hit.
PF00367. PTS_EIIB. 1 hit.
PF02378. PTS_EIIC. 2 hits.
[Graphical view]
SUPFAMSSF51261. Dup_hybrid_motif. 1 hit.
SSF55604. PTS_EIIB. 1 hit.
TIGRFAMsTIGR00826. EIIB_glc. 1 hit.
TIGR00830. 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.
PS51103. PTS_EIIC_TYPE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePTG3C_MYCPN
AccessionPrimary (citable) accession number: P75569
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: January 25, 2012
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Mycoplasma pneumoniae

Mycoplasma pneumoniae (strain M129): entries and gene names

SIMILARITY comments

Index of protein domains and families