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P20166 (PTG3C_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 glucose-specific EIICBA component
Alternative name(s):
EII-Glc/EIII-Glc
EIICBA-Glc

Including the following 3 domains:

  1. Glucose permease IIC component
    Alternative name(s):
    PTS system glucose-specific EIIC component
  2. Glucose-specific phosphotransferase enzyme IIB component
    EC=2.7.1.69
    Alternative name(s):
    PTS system glucose-specific EIIB component
  3. Glucose-specific phosphotransferase enzyme IIA component
    EC=2.7.1.-
    Alternative name(s):
    PTS system glucose-specific EIIA component
Gene names
Name:ptsG
Synonyms:crr, ptsX
Ordered Locus Names:BSU13890
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length699 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 glucose transport.

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.

Domain

The EIIC domain forms the PTS system translocation channel and contains the specific substrate-binding site. Ref.6 Ref.7 Ref.8

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. Ref.6 Ref.7 Ref.8

The EIIA domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the EIIB domain. Ref.6 Ref.7 Ref.8

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 – 699699PTS system glucose-specific EIICBA component
PRO_0000186557

Regions

Transmembrane16 – 3621Helical; Potential
Transmembrane66 – 8621Helical; Potential
Transmembrane89 – 10921Helical; Potential
Transmembrane139 – 15921Helical; Potential
Transmembrane180 – 20021Helical; Potential
Transmembrane233 – 25321Helical; Potential
Transmembrane283 – 30321Helical; Potential
Transmembrane313 – 33321Helical; Potential
Transmembrane338 – 35821Helical; Potential
Transmembrane365 – 38521Helical; Potential
Transmembrane388 – 40821Helical; Potential
Domain1 – 424424PTS EIIC type-1
Domain439 – 52082PTS EIIB type-1
Domain568 – 672105PTS EIIA type-1

Sites

Active site4611Phosphocysteine intermediate; for EIIB activity By similarity
Active site6201Tele-phosphohistidine intermediate; for EIIA activity By similarity

Secondary structure

.................................... 699
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P20166 [UniParc].

Last modified December 1, 1992. Version 2.
Checksum: 2A14D3C32EE0A9C5

FASTA69975,525
        10         20         30         40         50         60 
MFKALFGVLQ KIGRALMLPV AILPAAGILL AIGNAMQNKD MIQVLHFLSN DNVQLVAGVM 

        70         80         90        100        110        120 
ESAGQIVFDN LPLLFAVGVA IGLANGDGVA GIAAIIGYLV MNVSMSAVLL ANGTIPSDSV 

       130        140        150        160        170        180 
ERAKFFTENH PAYVNMLGIP TLATGVFGGI IVGVLAALLF NRFYTIELPQ YLGFFAGKRF 

       190        200        210        220        230        240 
VPIVTSISAL ILGLIMLVIW PPIQHGLNAF STGLVEANPT LAAFIFGVIE RSLIPFGLHH 

       250        260        270        280        290        300 
IFYSPFWYEF FSYKSAAGEI IRGDQRIFMA QIKDGVQLTA GTFMTGKYPF MMFGLPAAAL 

       310        320        330        340        350        360 
AIYHEAKPQN KKLVAGIMGS AALTSFLTGI TEPLEFSFLF VAPVLFAIHC LFAGLSFMVM 

       370        380        390        400        410        420 
QLLNVKIGMT FSGGLIDYFL FGILPNRTAW WLVIPVGLGL AVIYYFGFRF AIRKFNLKTP 

       430        440        450        460        470        480 
GREDAAEETA APGKTGEAGD LPYEILQAMG DQENIKHLDA CITRLRVTVN DQKKVDKDRL 

       490        500        510        520        530        540 
KQLGASGVLE VGNNIQAIFG PRSDGLKTQM QDIIAGRKPR PEPKTSAQEE VGQQVEEVIA 

       550        560        570        580        590        600 
EPLQNEIGEE VFVSPITGEI HPITDVPDQV FSGKMMGDGF AILPSEGIVV SPVRGKILNV 

       610        620        630        640        650        660 
FPTKHAIGLQ SDGGREILIH FGIDTVSLKG EGFTSFVSEG DRVEPGQKLL EVDLDAVKPN 

       670        680        690 
VPSLMTPIVF TNLAEGETVS IKASGSVNRE QEDIVKIEK 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and nucleotide sequence of the ptsG gene of Bacillus subtilis."
Zagorec M., Postma P.W.
Mol. Gen. Genet. 234:325-328(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[3]"Phosphoenolpyruvate:sugar phosphotransferase system of Bacillus subtilis: nucleotide sequence of ptsX, ptsH and the 5'-end of ptsI and evidence for a ptsHI operon."
Gonzy-Treboul G., Zagorec M., Rain-Guion M.-C., Steinmetz M.
Mol. Microbiol. 3:103-112(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 361-699.
Strain: 168.
[4]"The glucose permease of the phosphotransferase system of Bacillus subtilis: evidence for IIGlc and IIIGlc domains."
Gonzy-Treboul G., de Waard J.H., Zagorec M., Postma P.W.
Mol. Microbiol. 5:1241-1249(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[5]"The glucose permease of Bacillus subtilis is a single polypeptide chain that functions to energize the sucrose permease."
Sutrina S.L., Reddy P., Saier M.H. Jr., Reizer J.
J. Biol. Chem. 265:18581-18589(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 483-558.
[6]"Structure of the IIA domain of the glucose permease of Bacillus subtilis at 2.2-A resolution."
Liao D.-I., Kapadia G., Reddy P., Saier M.H. Jr., Reizer J., Herzberg O.
Biochemistry 30:9583-9594(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF EIII-GLC DOMAIN.
[7]"Polypeptide backbone resonance assignments and secondary structure of Bacillus subtilis enzyme IIIglc determined by two-dimensional and three-dimensional heteronuclear NMR spectroscopy."
Fairbrother W.J., Cavanagh J., Dyson H.J., Plamer A.G. III, Sutrina S.L., Reizer J., Saier M.H. Jr., Wright P.E.
Biochemistry 30:6896-6907(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF EIIA DOMAIN.
[8]"High-resolution solution structure of Bacillus subtilis IIAglc."
Chen Y., Case D.A., Reizer J., Saier M.H. Jr., Wright P.E.
Proteins 31:258-270(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF EIAA DOMAIN.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z11744 Genomic DNA. Translation: CAA77803.1.
AL009126 Genomic DNA. Translation: CAB13262.1.
X12832 Genomic DNA. Translation: CAA31315.1.
M60344 Genomic DNA. Translation: AAA22498.1.
PIRWQBSGS. S25083.
RefSeqNP_389272.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AX3NMR-A539-699[»]
1GPRX-ray1.90A539-699[»]
ProteinModelPortalP20166.
SMRP20166. Positions 438-516, 541-698.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224308.BSU13890.

Protein family/group databases

TCDB4.A.1.1.9. the pts glucose-glucoside (glc) family.

Proteomic databases

PaxDbP20166.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB13262; CAB13262; BSU13890.
GeneID939255.
KEGGbsu:BSU13890.
PATRIC18974561. VBIBacSub10457_1472.

Organism-specific databases

GenoListBSU13890. [Micado]

Phylogenomic databases

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

Enzyme and pathway databases

BioCycBSUB:BSU13890-MONOMER.

Family and domain databases

Gene3D3.30.1360.60. 1 hit.
InterProIPR011055. Dup_hybrid_motif.
IPR018113. PTrfase_EIIB/Cys_phosph_CS.
IPR004719. PTrfase_sys_maltose/Glc-sp_IIC.
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.
TIGR00852. pts-Glc. 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...

Other

EvolutionaryTraceP20166.

Entry information

Entry namePTG3C_BACSU
AccessionPrimary (citable) accession number: P20166
Secondary accession number(s): P08875
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: December 1, 1992
Last modified: April 16, 2014
This is version 132 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList