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Reviewed, UniProtKB/Swiss-Prot Q5HJI3 (PTG3C_STAAC)

Last modified November 3, 2009. Version 43. 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 EIICBA component
Alternative name(s):
    EIICBA-Glc
      Short name=EII-Glc
Including the following 3 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
    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
Synonyms: glcA
Ordered Locus Names: SACOL0175
OrganismStaphylococcus aureus (strain COL) [Complete proteome] [HAMAP]
Taxonomic identifier93062 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesStaphylococcus

Protein attributes

Sequence length681 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 EIIB N(pi)-phospho-L-histidine/cysteine + sugar = protein EIIB + sugar phosphate.

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

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 – 681681PTS system glucose-specific EIICBA component
PRO_0000351393

Regions

Transmembrane16 – 3621 Potential
Transmembrane73 – 9321 Potential
Transmembrane126 – 14621 Potential
Transmembrane170 – 19021 Potential
Transmembrane199 – 21921 Potential
Transmembrane273 – 29321 Potential
Transmembrane303 – 32321 Potential
Transmembrane328 – 34821 Potential
Transmembrane355 – 37521 Potential
Transmembrane383 – 40321 Potential
Domain3 – 414412PTS EIIC type-1
Domain425 – 50682PTS EIIB type-1
Domain551 – 655105PTS EIIA type-1

Sites

Active site4471Phosphocysteine intermediate; for EIIB activity By similarity
Active site6031Tele-phosphohistidine intermediate; for EIIA activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5HJI3-1 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: 7F1F4A2D4FEBD377

FASTA68173,925
        10         20         30         40         50         60 
MRKKLFGQLQ RIGKALMLPV AILPAAGLLL AIGTAMQGES LQHYLPFIQN GGVQTVAKLM 

        70         80         90        100        110        120 
TGAGGIIFDN LPMIFALGVA IGLAGGDGVA AIAAFVGYII MNKTMGDFLQ VTPKNIGDPA 

       130        140        150        160        170        180 
SGYASILGIP TLQTGVFGGI IIGALAAWCY NKFYNINLPS YLGFFAGKRF VPIMMATTSF 

       190        200        210        220        230        240 
ILAFPMALIW PTIQSGLNAF STGLLDSNTG VAVFLFGFIK RLLIPFGLHH IFHAPFWFEF 

       250        260        270        280        290        300 
GSWKNAAGEI IHGDQRIFIE QIREGAHLTA GKFMQGEFPV MMFGLPAAAL AIYHTAKPEN 

       310        320        330        340        350        360 
KKVVAGLMGS AALTSFLTGI TEPLEFSFLF VAPLLFFIHA VLDGLSFLTL YLLDLHLGYT 

       370        380        390        400        410        420 
FSGGFIDYFL LGILPNKTQW WLVIPVGLVY AVIYYFVFRF LIVKLKYKTP GREDKQSQAA 

       430        440        450        460        470        480 
TASATELPYA VLEAMGGKAN IKHLDACITR LRVEVNDKSK VDVPGLKDLG ASGVLEVGNN 

       490        500        510        520        530        540 
MQAIFGPKSD QIKHEMQQIM NGQVVENPTT MEDDKDETVV VAEDKSATSE LSHIVHAPLT 

       550        560        570        580        590        600 
GEVTPLSEVP DQVFSEKMMG DGIAIKPSQG EVRAPFNGKV QMIFPTKHAI GLVSDSGLEL 

       610        620        630        640        650        660 
LIHIGLDTVK LNGEGFTLHV EEGQEVKQGD LLINFDLDYI RNHAKSDITP IIVTQGNITN 

       670        680 
LDFKQGEHGN ISFGDQLFEA K 

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References

[1]"Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain."
Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H. expand/collapse author list , Utterback T.R., Lee C., Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E., Fraser C.M.
J. Bacteriol. 187:2426-2438(2005) [PubMed: 15774886] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000046 Genomic DNA. Translation: AAW37471.1.
RefSeqYP_185074.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ5HJI3.

Genome annotation databases

GeneID3236177.
GenomeReviewsGene locus SACOL0175 in contig CP000046_GR.
KEGGsac:SACOL0175.
TIGRSACOL0175.

Phylogenomic databases

HOGENOMQ5HJI3.
OMARCASPEN.

Family and domain databases

InterProIPR018113. PTrfase_EIIB/Cys_phosph_CS.
IPR001127. PTS_EIIA_1_perm.
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.
PfamPF00358. PTS_EIIA_1. 1 hit.
PF00367. PTS_EIIB. 1 hit.
PF02378. PTS_EIIC. 1 hit.
[Graphical view]
ProDomPD002243. PTS_EIIA. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00826. EIIB_glc. 1 hit.
TIGR00830. PTBA. 1 hit.
TIGR02002. PTS-II-BC-glcB. 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 namePTG3C_STAAC
AccessionPrimary (citable) accession number: Q5HJI3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 14, 2008
Last sequence update: February 15, 2005
Last modified: November 3, 2009
This is version 43 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