Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P20166

- PTG3C_BACSU

UniProt

P20166 - PTG3C_BACSU

Protein

PTS system glucose-specific EIICBA component

Gene

ptsG

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 2 (01 Dec 1992)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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 activityi

    Protein EIIA N(pi)-phospho-L-histidine + protein EIIB = protein EIIA + protein EIIB N(pi)-phospho-L-histidine/cysteine.PROSITE-ProRule annotation
    Protein EIIB N(pi)-phospho-L-histidine/cysteine + sugar = protein EIIB + sugar phosphate.PROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei461 – 4611Phosphocysteine intermediate; for EIIB activityPROSITE-ProRule annotation
    Active sitei620 – 6201Tele-phosphohistidine intermediate; for EIIA activityPROSITE-ProRule annotation

    GO - Molecular functioni

    1. glucose transmembrane transporter activity Source: InterPro
    2. kinase activity Source: UniProtKB-KW
    3. protein-N(PI)-phosphohistidine-sugar phosphotransferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. phosphoenolpyruvate-dependent sugar phosphotransferase system Source: UniProtKB-KW

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Phosphotransferase system, Sugar transport, Transport

    Enzyme and pathway databases

    BioCyciBSUB:BSU13890-MONOMER.

    Protein family/group databases

    TCDBi4.A.1.1.9. the pts glucose-glucoside (glc) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    PTS system glucose-specific EIICBA component
    Alternative name(s):
    EII-Glc/EIII-Glc
    EIICBA-Glc
    Including the following 3 domains:
    Glucose permease IIC component
    Alternative name(s):
    PTS system glucose-specific EIIC component
    Glucose-specific phosphotransferase enzyme IIB component (EC:2.7.1.69)
    Alternative name(s):
    PTS system glucose-specific EIIB component
    Glucose-specific phosphotransferase enzyme IIA component (EC:2.7.1.-)
    Alternative name(s):
    PTS system glucose-specific EIIA component
    Gene namesi
    Name:ptsG
    Synonyms:crr, ptsX
    Ordered Locus Names:BSU13890
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU13890. [Micado]

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 699699PTS system glucose-specific EIICBA componentPRO_0000186557Add
    BLAST

    Proteomic databases

    PaxDbiP20166.

    Interactioni

    Protein-protein interaction databases

    STRINGi224308.BSU13890.

    Structurei

    Secondary structure

    1
    699
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi557 – 5626
    Helixi563 – 5653
    Beta strandi566 – 5683
    Helixi569 – 5724
    Beta strandi577 – 5848
    Beta strandi586 – 5927
    Beta strandi595 – 5995
    Beta strandi602 – 61413
    Beta strandi616 – 6205
    Beta strandi622 – 6243
    Turni625 – 6328
    Beta strandi633 – 6364
    Beta strandi641 – 6433
    Beta strandi645 – 6528
    Helixi654 – 6574
    Helixi658 – 6603
    Beta strandi666 – 6727
    Helixi673 – 6753
    Beta strandi678 – 6814
    Beta strandi685 – 6873
    Beta strandi692 – 6987

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AX3NMR-A539-699[»]
    1GPRX-ray1.90A539-699[»]
    ProteinModelPortaliP20166.
    SMRiP20166. Positions 438-516, 541-698.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP20166.

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei16 – 3621HelicalPROSITE-ProRule annotationAdd
    BLAST
    Transmembranei66 – 8621HelicalPROSITE-ProRule annotationAdd
    BLAST
    Transmembranei89 – 10921HelicalPROSITE-ProRule annotationAdd
    BLAST
    Transmembranei139 – 15921HelicalPROSITE-ProRule annotationAdd
    BLAST
    Transmembranei180 – 20021HelicalPROSITE-ProRule annotationAdd
    BLAST
    Transmembranei233 – 25321HelicalPROSITE-ProRule annotationAdd
    BLAST
    Transmembranei283 – 30321HelicalPROSITE-ProRule annotationAdd
    BLAST
    Transmembranei313 – 33321HelicalPROSITE-ProRule annotationAdd
    BLAST
    Transmembranei338 – 35821HelicalPROSITE-ProRule annotationAdd
    BLAST
    Transmembranei365 – 38521HelicalPROSITE-ProRule annotationAdd
    BLAST
    Transmembranei388 – 40821HelicalPROSITE-ProRule annotationAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 424424PTS EIIC type-1PROSITE-ProRule annotationAdd
    BLAST
    Domaini439 – 52082PTS EIIB type-1PROSITE-ProRule annotationAdd
    BLAST
    Domaini568 – 672105PTS EIIA type-1PROSITE-ProRule annotationAdd
    BLAST

    Domaini

    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 similaritiesi

    Contains 1 PTS EIIA type-1 domain.PROSITE-ProRule annotation
    Contains 1 PTS EIIB type-1 domain.PROSITE-ProRule annotation
    Contains 1 PTS EIIC type-1 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG1263.
    HOGENOMiHOG000250993.
    KOiK02763.
    K02764.
    K02765.
    OMAiLYYFSFR.
    OrthoDBiEOG6FFS9V.
    PhylomeDBiP20166.

    Family and domain databases

    Gene3Di3.30.1360.60. 1 hit.
    InterProiIPR011055. Dup_hybrid_motif.
    IPR018113. PTrfase_EIIB_Cys.
    IPR001127. PTS_EIIA_1_perm.
    IPR003352. PTS_EIIC.
    IPR013013. PTS_EIIC_1.
    IPR001996. PTS_IIB_1.
    IPR011299. PTS_IIBC_glc.
    IPR004719. PTS_maltose/Glc_sub_IIC.
    [Graphical view]
    PfamiPF00358. PTS_EIIA_1. 1 hit.
    PF00367. PTS_EIIB. 1 hit.
    PF02378. PTS_EIIC. 1 hit.
    [Graphical view]
    SUPFAMiSSF51261. SSF51261. 1 hit.
    SSF55604. SSF55604. 1 hit.
    TIGRFAMsiTIGR00826. EIIB_glc. 1 hit.
    TIGR00830. PTBA. 1 hit.
    TIGR00852. pts-Glc. 1 hit.
    TIGR02002. PTS-II-BC-glcB. 1 hit.
    PROSITEiPS51093. 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]

    Sequencei

    Sequence statusi: Complete.

    P20166-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFKALFGVLQ KIGRALMLPV AILPAAGILL AIGNAMQNKD MIQVLHFLSN    50
    DNVQLVAGVM ESAGQIVFDN LPLLFAVGVA IGLANGDGVA GIAAIIGYLV 100
    MNVSMSAVLL ANGTIPSDSV ERAKFFTENH PAYVNMLGIP TLATGVFGGI 150
    IVGVLAALLF NRFYTIELPQ YLGFFAGKRF VPIVTSISAL ILGLIMLVIW 200
    PPIQHGLNAF STGLVEANPT LAAFIFGVIE RSLIPFGLHH IFYSPFWYEF 250
    FSYKSAAGEI IRGDQRIFMA QIKDGVQLTA GTFMTGKYPF MMFGLPAAAL 300
    AIYHEAKPQN KKLVAGIMGS AALTSFLTGI TEPLEFSFLF VAPVLFAIHC 350
    LFAGLSFMVM QLLNVKIGMT FSGGLIDYFL FGILPNRTAW WLVIPVGLGL 400
    AVIYYFGFRF AIRKFNLKTP GREDAAEETA APGKTGEAGD LPYEILQAMG 450
    DQENIKHLDA CITRLRVTVN DQKKVDKDRL KQLGASGVLE VGNNIQAIFG 500
    PRSDGLKTQM QDIIAGRKPR PEPKTSAQEE VGQQVEEVIA EPLQNEIGEE 550
    VFVSPITGEI HPITDVPDQV FSGKMMGDGF AILPSEGIVV SPVRGKILNV 600
    FPTKHAIGLQ SDGGREILIH FGIDTVSLKG EGFTSFVSEG DRVEPGQKLL 650
    EVDLDAVKPN VPSLMTPIVF TNLAEGETVS IKASGSVNRE QEDIVKIEK 699
    Length:699
    Mass (Da):75,525
    Last modified:December 1, 1992 - v2
    Checksum:i2A14D3C32EE0A9C5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z11744 Genomic DNA. Translation: CAA77803.1.
    AL009126 Genomic DNA. Translation: CAB13262.1.
    X12832 Genomic DNA. Translation: CAA31315.1.
    M60344 Genomic DNA. Translation: AAA22498.1.
    PIRiS25083. WQBSGS.
    RefSeqiNP_389272.1. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB13262; CAB13262; BSU13890.
    GeneIDi939255.
    KEGGibsu:BSU13890.
    PATRICi18974561. VBIBacSub10457_1472.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z11744 Genomic DNA. Translation: CAA77803.1 .
    AL009126 Genomic DNA. Translation: CAB13262.1 .
    X12832 Genomic DNA. Translation: CAA31315.1 .
    M60344 Genomic DNA. Translation: AAA22498.1 .
    PIRi S25083. WQBSGS.
    RefSeqi NP_389272.1. NC_000964.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AX3 NMR - A 539-699 [» ]
    1GPR X-ray 1.90 A 539-699 [» ]
    ProteinModelPortali P20166.
    SMRi P20166. Positions 438-516, 541-698.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU13890.

    Protein family/group databases

    TCDBi 4.A.1.1.9. the pts glucose-glucoside (glc) family.

    Proteomic databases

    PaxDbi P20166.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB13262 ; CAB13262 ; BSU13890 .
    GeneIDi 939255.
    KEGGi bsu:BSU13890.
    PATRICi 18974561. VBIBacSub10457_1472.

    Organism-specific databases

    GenoListi BSU13890. [Micado ]

    Phylogenomic databases

    eggNOGi COG1263.
    HOGENOMi HOG000250993.
    KOi K02763.
    K02764.
    K02765.
    OMAi LYYFSFR.
    OrthoDBi EOG6FFS9V.
    PhylomeDBi P20166.

    Enzyme and pathway databases

    BioCyci BSUB:BSU13890-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P20166.

    Family and domain databases

    Gene3Di 3.30.1360.60. 1 hit.
    InterProi IPR011055. Dup_hybrid_motif.
    IPR018113. PTrfase_EIIB_Cys.
    IPR001127. PTS_EIIA_1_perm.
    IPR003352. PTS_EIIC.
    IPR013013. PTS_EIIC_1.
    IPR001996. PTS_IIB_1.
    IPR011299. PTS_IIBC_glc.
    IPR004719. PTS_maltose/Glc_sub_IIC.
    [Graphical view ]
    Pfami PF00358. PTS_EIIA_1. 1 hit.
    PF00367. PTS_EIIB. 1 hit.
    PF02378. PTS_EIIC. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51261. SSF51261. 1 hit.
    SSF55604. SSF55604. 1 hit.
    TIGRFAMsi TIGR00826. EIIB_glc. 1 hit.
    TIGR00830. PTBA. 1 hit.
    TIGR00852. pts-Glc. 1 hit.
    TIGR02002. PTS-II-BC-glcB. 1 hit.
    PROSITEi PS51093. 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 ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.

    Entry informationi

    Entry nameiPTG3C_BACSU
    AccessioniPrimary (citable) accession number: P20166
    Secondary accession number(s): P08875
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: December 1, 1992
    Last modified: October 1, 2014
    This is version 136 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3