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Reviewed, UniProtKB/Swiss-Prot Q5HL73 (PTG3C_STAEQ)

Last modified February 9, 2010. Version 47. 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
Ordered Locus Names: SERP2114
OrganismStaphylococcus epidermidis (strain ATCC 35984 / RP62A) [Complete proteome] [HAMAP]
Taxonomic identifier176279 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesStaphylococcus

Protein attributes

Sequence length675 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.

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 – 675675PTS system glucose-specific EIICBA component
PRO_0000351403

Regions

Transmembrane16 – 3621 Potential
Transmembrane59 – 7921 Potential
Transmembrane81 – 10121 Potential
Transmembrane126 – 14621 Potential
Transmembrane170 – 19021 Potential
Transmembrane211 – 23121 Potential
Transmembrane273 – 29321 Potential
Transmembrane303 – 32321 Potential
Transmembrane328 – 34821 Potential
Transmembrane355 – 37521 Potential
Transmembrane378 – 39821 Potential
Domain3 – 414412PTS EIIC type-1
Domain425 – 50682PTS EIIB type-1
Domain547 – 651105PTS EIIA type-1

Sites

Active site4471Phosphocysteine intermediate; for EIIB activity By similarity
Active site5991Tele-phosphohistidine intermediate; for EIIA activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5HL73-1 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: AD6EC55F6C15C4C2

FASTA67573,359
        10         20         30         40         50         60 
MFKKLFGQMQ RIGKALMLPV AILPAAGLLL AIGTAFQGEA LQHYLPFIKN DIVQQIANML 

        70         80         90        100        110        120 
TGAGGIIFDN LPIIFALGVA IGLAGGDGVA AIAAFVGFII LNKTMGAFLH VTPDKLSDPT 

       130        140        150        160        170        180 
NGYANVLGIP TLQTGVFGGI IIGALAAWCY NKFYNITLPS YLGFFAGKRF VPIMMATTSF 

       190        200        210        220        230        240 
ILAFPMAIIW PTIQNGLNAF SEGLLDSNTG LAVFLFGFIK RLLIPFGLHH IFHAPFWFEF 

       250        260        270        280        290        300 
GSWKNAAGEI IRGDQRIFIE QIREGAHLTS GKFMQGEFPV MMFGLPAAAL AIYQTAKPEN 

       310        320        330        340        350        360 
KKVVAGLMIS AALTSFLTGI TEPLEFSFLF VAPFLFVIHA VLDGLSFLTL YLLNVHLGYT 

       370        380        390        400        410        420 
FSGGFIDYVL LGILPNKTAW WLVIPVGIIY AVIYYFVFRF LIVKFNYKTP GREDKKSSVT 

       430        440        450        460        470        480 
TTSASQLPFD VLKAMGGKEN IKHLDACITR LRVEVNEKSK VDVAGLKSLG ASGVLEVGNN 

       490        500        510        520        530        540 
MQAIFGPKSD QIKHDMAKII SGEITKPSET TIDEEVSDDP VHVEDIVETE IYAPGHGEII 

       550        560        570        580        590        600 
PLSEVPDKVF SEKMMGDGIG FVPDSGEIVA PFDGTVKTIF PTKHAIGLES DSGVEVLIHI 

       610        620        630        640        650        660 
GIDTVKLNGE GFESLVNTDE PVTQGQPLMK IDLEYLKEHA PSIITPVIIT NQEDKTLTIE 

       670 
DVKQVDPGKA IMTIK 

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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

EMBL
GenBank
DDBJ
CP000029 Genomic DNA. Translation: AAW52991.1.
RefSeqYP_189670.1.

3D structure databases

HSSPHSSP built from PDB template 1O2F based on UniProtKB P69786.
SMRQ5HL73. Positions 431-500, 529-675.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5HL73.

Genome annotation databases

GeneID3242483.
GenomeReviewsGene locus SERP2114 in contig CP000029_GR.
KEGGser:SERP2114.
TIGRSERP2114.

Phylogenomic databases

eggNOGCOG1263.
HOGENOMHBG571563.
OMACIPAIAL.

Enzyme and pathway databases

BioCycSEPI176279:SERP2114-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.
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]
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_STAEQ
AccessionPrimary (citable) accession number: Q5HL73
Entry history
Integrated into UniProtKB/Swiss-Prot: October 14, 2008
Last sequence update: February 15, 2005
Last modified: February 9, 2010
This is version 47 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