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Q7A3G4 (PTU3C_STAAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
PTS system glucoside-specific EIICBA component

Including the following 3 domains:

  1. Glucoside permease IIC component
    Alternative name(s):
    PTS system glucoside-specific EIIC component
  2. Glucoside-specific phosphotransferase enzyme IIB component
    EC=2.7.1.69
    Alternative name(s):
    PTS system glucoside-specific EIIB component
  3. Glucoside-specific phosphotransferase enzyme IIA component
    EC=2.7.1.-
    Alternative name(s):
    PTS system glucoside-specific EIIA component
Gene names
Name:glcB
Ordered Locus Names:SA2326
OrganismStaphylococcus aureus (strain N315) [Complete proteome] [HAMAP]
Taxonomic identifier158879 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length688 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 alpha- and beta-glucoside 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 – 688688PTS system glucoside-specific EIICBA component
PRO_0000351414

Regions

Transmembrane12 – 3221Helical; Potential
Transmembrane81 – 10121Helical; Potential
Transmembrane137 – 15721Helical; Potential
Transmembrane182 – 20221Helical; Potential
Transmembrane223 – 24321Helical; Potential
Transmembrane284 – 30421Helical; Potential
Transmembrane315 – 33521Helical; Potential
Transmembrane340 – 36021Helical; Potential
Transmembrane364 – 38421Helical; Potential
Transmembrane395 – 41521Helical; Potential
Domain3 – 427425PTS EIIC type-1
Domain438 – 51982PTS EIIB type-1
Domain560 – 664105PTS EIIA type-1

Sites

Active site4601Phosphocysteine intermediate; for EIIB activity By similarity
Active site6121Tele-phosphohistidine intermediate; for EIIA activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7A3G4 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 11D5C824835AFD21

FASTA68874,430
        10         20         30         40         50         60 
MFKKLFGQLQ RIGKALMLPV AILPAAGILL AFGNAMHNEQ LVEIAPWLKN DIIVMISSVM 

        70         80         90        100        110        120 
EAAGQVVFDN LPLLFAVGTA LGLAGGDGVA ALAALVGYLI MNATMGKVLH ITIDDIFSYA 

       130        140        150        160        170        180 
KGAKELSQAA KEPAHALVLG IPTLQTGVFG GIIMGALAAW CYNKFYNITL PPFLGFFAGK 

       190        200        210        220        230        240 
RFVPIVTSVV AIATGVLLSF AWPPIQDGLN SLSNFLLNKN LTLTTFIFGI IERSLIPFGL 

       250        260        270        280        290        300 
HHIFYSPFWF EFGSYTNHAG ELVRGDQRIW MAQLKDGVPF TAGAFTTGKY PFMMFGLPAA 

       310        320        330        340        350        360 
AFAIYKNARP ERKKVVGGLM LSAGLTAFLT GITEPLEFSF LFVAPVLYGI HVLLAGTSFL 

       370        380        390        400        410        420 
VMHLLGVKIG MTFSGGFIDY ILYGLLNWDR SHALLVIPVG IVYAIVYYFL FDFAIRKFKL 

       430        440        450        460        470        480 
KTPGREDEET EIRNSSVAKL PFDVLDAMGG KENIKHLDAC ITRLRVEVVD KSKVDVAGIK 

       490        500        510        520        530        540 
ALGASGVLEV GNNMQAIFGP KSDQIKHDMA KIMSGEITKP SETTVTEEMS DEPVHVEALG 

       550        560        570        580        590        600 
TTDIYAPGVG QIIPLSEVPD QVFAGKMMGD GIGFIPEKGE IVAPFDGTVK TIFPTKHAIG 

       610        620        630        640        650        660 
LESESGVEVL IHIGIDTVKL NGEGFESLIN VDEKVTQAQP LMKVNLAYLK AHAPSIVTPM 

       670        680 
IITNLENKEL VIEDVQDADP GKLIMTVK 

« Hide

References

[1]"Whole genome sequencing of meticillin-resistant Staphylococcus aureus."
Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y. expand/collapse author list , Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H., Hiramatsu K.
Lancet 357:1225-1240(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: N315.
[2]"Shotgun proteomic analysis of total and membrane protein extracts of S. aureus strain N315."
Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.
Submitted (OCT-2007) to UniProtKB
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: N315.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000018 Genomic DNA. Translation: BAB43629.1.
PIRC90058.
RefSeqNP_375650.1. NC_002745.2.

3D structure databases

ProteinModelPortalQ7A3G4.
SMRQ7A3G4. Positions 447-509, 532-671.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING158879.SA2326.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB43629; BAB43629; BAB43629.
GeneID1125253.
KEGGsau:SA2326.
PATRIC19577210. VBIStaAur116463_2523.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1263.
HOGENOMHOG000250993.
KOK02763.
K02764.
K02765.
OMARPENKKV.
OrthoDBEOG6FFS9V.
ProtClustDBCLSK872840.

Enzyme and pathway databases

BioCycSAUR158879:GJCB-2487-MONOMER.

Family and domain databases

Gene3D3.30.1360.60. 1 hit.
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]
PfamPF00358. PTS_EIIA_1. 1 hit.
PF00367. PTS_EIIB. 1 hit.
PF02378. PTS_EIIC. 1 hit.
[Graphical view]
SUPFAMSSF51261. SSF51261. 1 hit.
SSF55604. SSF55604. 1 hit.
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 namePTU3C_STAAN
AccessionPrimary (citable) accession number: Q7A3G4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 14, 2008
Last sequence update: July 5, 2004
Last modified: April 16, 2014
This is version 76 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