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Q53922 (PTU3C_STACT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
PTS system glucoside-specific EIICBA component
Alternative name(s):
EIICBA-Glc 2

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:Sca_1000
OrganismStaphylococcus carnosus (strain TM300) [Complete proteome] [HAMAP]
Taxonomic identifier396513 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Staphylococcus ›

Protein attributes

Sequence length692 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. Can also transport glucose, but not galactose, fructose, mannose, cellobiose, sucrose, maltose, lactose, melibiose and trehalose, as well as N-acetylglucosamine. Ref.3

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.

Enzyme regulation

Inhibited by methyl alpha-D-glucoside, methyl beta-D-glucoside, p-nitrophenyl alpha-D-glucoside, o-nitrophenyl beta-D-glucoside and salicin, but not by 2-deoxyglucose. Ref.3

Subcellular location

Cell membrane; Multi-pass membrane protein Ref.3.

Induction

Up-regulated by the antiterminator protein GlcT. Ref.3 Ref.4

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.

Biophysicochemical properties

Kinetic parameters:

KM=19 µM for glucose Ref.3

KM=37.2 µM for glucose (in the presence of Triton X-100)

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 692692PTS system glucoside-specific EIICBA component
PRO_0000351419

Regions

Transmembrane15 – 3521Helical; Potential
Transmembrane84 – 10421Helical; Potential
Transmembrane140 – 16021Helical; Potential
Transmembrane185 – 20521Helical; Potential
Transmembrane215 – 23521Helical; Potential
Transmembrane287 – 30721Helical; Potential
Transmembrane318 – 33821Helical; Potential
Transmembrane344 – 36421Helical; Potential
Transmembrane370 – 39021Helical; Potential
Transmembrane398 – 41821Helical; Potential
Domain6 – 430425PTS EIIC type-1
Domain441 – 52282PTS EIIB type-1
Domain563 – 667105PTS EIIA type-1

Sites

Active site4631Phosphocysteine intermediate; for EIIB activity By similarity
Active site6151Tele-phosphohistidine intermediate; for EIIA activity By similarity

Experimental info

Sequence conflict3091R → P in CAA63743. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q53922 [UniParc].

Last modified May 5, 2009. Version 2.
Checksum: 0BF5E8208F6227A0

FASTA69275,403
        10         20         30         40         50         60 
MKNLLKKFFG QLQRIGKALM LPVAILPAAG ILLTFGNAMH NEQILHFAPW MQHHYIQLIS 

        70         80         90        100        110        120 
QIMEASGQVI FDNLPLLFAM GTALGLAGGD GVAGIAALVG YLIMSATMGK IAGITIDDIF 

       130        140        150        160        170        180 
SYADGAKTLG QSAKDPAHAL VLGIPTLQTG VFGGIIIGAL AAWCYNKFYN IQLPQFLGFF 

       190        200        210        220        230        240 
AGKRFVPIIT SLVAIVTGIV LSFVWPPVQD GLNNLSNFLL GKNLALTTFI FGIIERSLIP 

       250        260        270        280        290        300 
FGLHHIFYAP FWFEFGHYVN ESGNLVRGDQ RIWMAQYQDG VPFTAGAFTT GKYPFMMFGL 

       310        320        330        340        350        360 
PAAAFAIYRQ AKPERRKVVG GLMLSAALTS FLTGITEPLE FSFLFVAPIL YVAHVILAGT 

       370        380        390        400        410        420 
SFLIMHLLHV QIGMTFSGGF IDYILYGLLS WDRSNALLVI PVGIAYALIY YFLFTFLIKK 

       430        440        450        460        470        480 
LNLKTPGRED KEVESKDVSV SELPFEVLEA MGNKDNIKHL DACITRLRVE VRDKGLVDVE 

       490        500        510        520        530        540 
KLKQLGASGV LEVGNNMQAI FGPKSDQIKH DMQQIMDGKI TSPAETTVTE DGDVETAEIV 

       550        560        570        580        590        600 
AEGGAVIYAP ITGEAVDLSE VPDKVFSAKM MGDGIAIKPE TGEVVAPFDG KVKMIFPTKH 

       610        620        630        640        650        660 
AIGLESKDGI ELLIHFGLET VKLDGEGFEI LVKENDNIVL GQPLMKVDLN YIKEHADDTI 

       670        680        690 
TPIIITNAGS ANIEVLHTGK VEQGEKLLLV NN

« Hide

References

« Hide 'large scale' references
[1]"Cloning and sequencing of two genes from Staphylococcus carnosus coding for glucose-specific PTS and their expression in Escherichia coli K-12."
Christiansen I., Hengstenberg W.
Mol. Gen. Genet. 250:375-379(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Genome analysis of the meat starter culture bacterium Staphylococcus carnosus TM300."
Rosenstein R., Nerz C., Biswas L., Resch A., Raddatz G., Schuster S.C., Goetz F.
Appl. Environ. Microbiol. 75:811-822(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TM300.
[3]"Staphylococcal phosphoenolpyruvate-dependent phosphotransferase system -- two highly similar glucose permeases in Staphylococcus carnosus with different glucoside specificity: protein engineering in vivo?"
Christiansen I., Hengstenberg W.
Microbiology 145:2881-2889(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, SUBSTRATE SPECIFICITY, ENZYME REGULATION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES.
[4]"Regulation of the glucose-specific phosphotransferase system (PTS) of Staphylococcus carnosus by the antiterminator protein GlcT."
Knezevic I., Bachem S., Sickmann A., Meyer H.E., Stuelke J., Hengstenberg W.
Microbiology 146:2333-2342(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY GLCT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X93360 Genomic DNA. Translation: CAA63743.1.
AM295250 Genomic DNA. Translation: CAL27908.1.
PIRS46953. S63606.
RefSeqYP_002634093.1. NC_012121.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRING396513.Sca_1000.

Protein family/group databases

TCDB4.A.1.1.14. PTS glucose-glucoside (Glc) family.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID7551629.
KEGGsca:Sca_1000.
PATRIC19602770. VBIStaCar105558_0999.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1263.
HOGENOMHOG000250993.
KOK02763.
K02764.
K02765.
OMAFSDWAAH.
ProtClustDBCLSK872840.

Enzyme and pathway databases

BioCycSCAR396513:GJ9G-1013-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. Dup_hybrid_motif. 1 hit.
SSF55604. PTS_EIIB. 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_STACT
AccessionPrimary (citable) accession number: Q53922
Secondary accession number(s): B9DP63, Q53948
Entry history
Integrated into UniProtKB/Swiss-Prot: October 14, 2008
Last sequence update: May 5, 2009
Last modified: May 29, 2013
This is version 85 of the entry and version 2 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

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