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Q9KF90 (PTV3B_BACHD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 72. 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 beta-glucoside-specific EIIBCA component
Alternative name(s):
EIIBCA-Bgl
Short name=EII-Bgl

Including the following 3 domains:

  1. Beta-glucoside-specific phosphotransferase enzyme IIB component
    EC=2.7.1.69
    Alternative name(s):
    PTS system beta-glucoside-specific EIIB component
  2. Beta-glucoside permease IIC component
    Alternative name(s):
    PTS system beta-glucoside-specific EIIC component
  3. Beta-glucoside-specific phosphotransferase enzyme IIA component
    EC=2.7.1.-
    Alternative name(s):
    PTS system beta-glucoside-specific EIIA component
Gene names
Name:bglP
Ordered Locus Names:BH0595
OrganismBacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) [Complete proteome] [HAMAP]
Taxonomic identifier272558 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length636 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 beta-glucoside 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 Potential.

Domain

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 EIIC domain forms the PTS system translocation channel and contains the specific substrate-binding site.

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 – 636636PTS system beta-glucoside-specific EIIBCA component
PRO_0000186479

Regions

Transmembrane104 – 12421Helical; Potential
Transmembrane146 – 16621Helical; Potential
Transmembrane172 – 19221Helical; Potential
Transmembrane215 – 23521Helical; Potential
Transmembrane258 – 27821Helical; Potential
Transmembrane299 – 31921Helical; Potential
Transmembrane337 – 35721Helical; Potential
Transmembrane369 – 38921Helical; Potential
Transmembrane407 – 42721Helical; Potential
Transmembrane444 – 46421Helical; Potential
Domain1 – 8686PTS EIIB type-1
Domain105 – 476372PTS EIIC type-1
Domain506 – 610105PTS EIIA type-1

Sites

Active site261Phosphocysteine intermediate; for EIIB activity By similarity
Active site5581Tele-phosphohistidine intermediate; for EIIA activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9KF90 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 434C0B12311716F2

FASTA63668,438
        10         20         30         40         50         60 
MKYEQLAKDI IQHVGGKENV ISVVHCITRL RFKLKDEGKA NTDVLKNMDG IVTVMKSGGQ 

        70         80         90        100        110        120 
YQVVIGNHVP DVYKDVVEIG GFQNQAETET EDEKKYQGLF NKFIDIIASI FTPVLGVLAA 

       130        140        150        160        170        180 
TGMIKGLNAL FLSTGVLEEA NGTYQLLHAI GDSLFYFFPI FLGYTAAKKF GATPFIGMAI 

       190        200        210        220        230        240 
GASLVYPTLV VLTEGEPLYT LFTGTIFESP VHITFLGIPV ILMSYATSVI PIILAAYFAS 

       250        260        270        280        290        300 
KVEARLRKII PDVVKTFLVP FFTLLIVVPL TFIVIGPIAT WAGQLLGQFT LWVYNLSPII 

       310        320        330        340        350        360 
AGAFLGGFWQ VFVIFGLHWG LIPIAINNLV VQGSDPVLAM VFAASFAQIG AVAAVWLKIK 

       370        380        390        400        410        420 
QQKVKTLSVP AFISGIFGVT EPAIYGVTLP LKRPFIISCI AAAVGGAIIG LFRSQGYIIG 

       430        440        450        460        470        480 
GLGIFGIPSF LHPADGMDAG FWGIVIAVVV AFVLGFILTY LFGLKSGNAS DEQTETKAHT 

       490        500        510        520        530        540 
STGTGEKEEI SSPFNGSVIT LSEIKDEAFS SGALGEGIAI EPSEGKLFSP VSGMVTALYP 

       550        560        570        580        590        600 
THHALGITTD RGAELLIHIG LDTVQLDGKF FTAHTIQGAQ VEKGDLLIEF DIKEIKAAGY 

       610        620        630 
AVTTPVIVTN HKQYGQLFLT DKQQVNAGDR LLELTR

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References

[1]"Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis."
Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.
Nucleic Acids Res. 28:4317-4331(2000) [PubMed: 11058132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000004 Genomic DNA. Translation: BAB04314.1.
PIRC83724.
RefSeqNP_241461.1. NC_002570.2.

3D structure databases

ProteinModelPortalQ9KF90.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000053669; EBBACP00000052308; EBBACG00000053660.
GeneID893200.
GenomeReviewsGene locus BH0595 in contig BA000004_GR.
KEGGbha:BH0595.
NMPDRfig|272558.1.peg.595.
PATRIC18938166. VBIBacHal18977_0626.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000000033.
HOGENOMHBG673521.
OMADYTELAK.
PhylomeDBQ9KF90.
ProtClustDBCLSK872762.

Enzyme and pathway databases

BioCycBHAL272558:BH0595-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.
IPR011297. PTS_IIABC_b_glu.
[Graphical view]
Gene3DG3DSA:3.30.1360.60. PTS_EIIB. 1 hit.
KOK02755.
K02756.
K02757.
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.
TIGRFAMsTIGR00830. PTBA. 1 hit.
TIGR01995. PTS-II-ABC-beta. 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 namePTV3B_BACHD
AccessionPrimary (citable) accession number: Q9KF90
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: October 1, 2000
Last modified: January 25, 2012
This is version 72 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents