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PTS system glucose-specific EIICBA component (EC 2.7.1.199) (EII-Glc/EIII-Glc) (EIICBA-Glc) (EIICBA-Glc 1) [Includes: Glucose permease IIC component (PTS system glucose-specific EIIC component); Glucose-specific phosphotransferase enzyme IIB component (PTS system glucose-specific EIIB component); Glucose-specific phosphotransferase enzyme IIA component (PTS system glucose-specific EIIA component)]

 PTG3C_BACSU             Reviewed;         699 AA.
P20166; P08875;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
01-DEC-1992, sequence version 2.
25-OCT-2017, entry version 155.
RecName: Full=PTS system glucose-specific EIICBA component {ECO:0000250|UniProtKB:Q57071};
EC=2.7.1.199 {ECO:0000250|UniProtKB:Q57071};
AltName: Full=EII-Glc/EIII-Glc {ECO:0000305|PubMed:1911744};
AltName: Full=EIICBA-Glc {ECO:0000250|UniProtKB:Q57071};
AltName: Full=EIICBA-Glc 1 {ECO:0000305};
Includes:
RecName: Full=Glucose permease IIC component {ECO:0000250|UniProtKB:Q57071};
AltName: Full=PTS system glucose-specific EIIC component {ECO:0000250|UniProtKB:Q57071};
Includes:
RecName: Full=Glucose-specific phosphotransferase enzyme IIB component {ECO:0000250|UniProtKB:Q57071};
AltName: Full=PTS system glucose-specific EIIB component {ECO:0000250|UniProtKB:Q57071};
Includes:
RecName: Full=Glucose-specific phosphotransferase enzyme IIA component {ECO:0000250|UniProtKB:Q57071};
AltName: Full=PTS system glucose-specific EIIA component {ECO:0000250|UniProtKB:Q57071};
Name=ptsG; Synonyms=crr, ptsX; OrderedLocusNames=BSU13890;
Bacillus subtilis (strain 168).
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
NCBI_TaxID=224308;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1508157; DOI=10.1007/BF00283853;
Zagorec M., Postma P.W.;
"Cloning and nucleotide sequence of the ptsG gene of Bacillus
subtilis.";
Mol. Gen. Genet. 234:325-328(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
PubMed=9384377; DOI=10.1038/36786;
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.;
"The complete genome sequence of the Gram-positive bacterium Bacillus
subtilis.";
Nature 390:249-256(1997).
[3]
PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 361-699.
STRAIN=168;
PubMed=2497294; DOI=10.1111/j.1365-2958.1989.tb00109.x;
Gonzy-Treboul G., Zagorec M., Rain-Guion M.-C., Steinmetz M.;
"Phosphoenolpyruvate:sugar phosphotransferase system of Bacillus
subtilis: nucleotide sequence of ptsX, ptsH and the 5'-end of ptsI and
evidence for a ptsHI operon.";
Mol. Microbiol. 3:103-112(1989).
[4]
SEQUENCE REVISION.
PubMed=1956301; DOI=10.1111/j.1365-2958.1991.tb01898.x;
Gonzy-Treboul G., de Waard J.H., Zagorec M., Postma P.W.;
"The glucose permease of the phosphotransferase system of Bacillus
subtilis: evidence for IIGlc and IIIGlc domains.";
Mol. Microbiol. 5:1241-1249(1991).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 483-558.
PubMed=2120236;
Sutrina S.L., Reddy P., Saier M.H. Jr., Reizer J.;
"The glucose permease of Bacillus subtilis is a single polypeptide
chain that functions to energize the sucrose permease.";
J. Biol. Chem. 265:18581-18589(1990).
[6]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF EIIA DOMAIN.
PubMed=1911744; DOI=10.1021/bi00104a004;
Liao D.-I., Kapadia G., Reddy P., Saier M.H. Jr., Reizer J.,
Herzberg O.;
"Structure of the IIA domain of the glucose permease of Bacillus
subtilis at 2.2-A resolution.";
Biochemistry 30:9583-9594(1991).
[7]
STRUCTURE BY NMR OF EIIA DOMAIN.
PubMed=1906345; DOI=10.1021/bi00242a013;
Fairbrother W.J., Cavanagh J., Dyson H.J., Plamer A.G. III,
Sutrina S.L., Reizer J., Saier M.H. Jr., Wright P.E.;
"Polypeptide backbone resonance assignments and secondary structure of
Bacillus subtilis enzyme IIIglc determined by two-dimensional and
three-dimensional heteronuclear NMR spectroscopy.";
Biochemistry 30:6896-6907(1991).
[8]
STRUCTURE BY NMR OF EIAA DOMAIN.
PubMed=9593197;
DOI=10.1002/(SICI)1097-0134(19980515)31:3<258::AID-PROT3>3.3.CO;2-Q;
Chen Y., Case D.A., Reizer J., Saier M.H. Jr., Wright P.E.;
"High-resolution solution structure of Bacillus subtilis IIAglc.";
Proteins 31:258-270(1998).
-!- 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.
{ECO:0000250|UniProtKB:Q57071}.
-!- CATALYTIC ACTIVITY: [Protein]-N(pi)-phospho-L-histidine + D-
glucose(Side 1) = [protein]-L-histidine + D-glucose 6-
phosphate(Side 2). {ECO:0000250|UniProtKB:Q57071}.
-!- 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.
{ECO:0000255|PROSITE-ProRule:PRU00426}.
-!- 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.
{ECO:0000255|PROSITE-ProRule:PRU00421}.
-!- DOMAIN: The EIIA domain is phosphorylated by phospho-HPr on a
histidyl residue. Then, it transfers the phosphoryl group to the
EIIB domain. {ECO:0000255|PROSITE-ProRule:PRU00416}.
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EMBL; Z11744; CAA77803.1; -; Genomic_DNA.
EMBL; AL009126; CAB13262.1; -; Genomic_DNA.
EMBL; X12832; CAA31315.1; -; Genomic_DNA.
EMBL; M60344; AAA22498.1; -; Genomic_DNA.
PIR; S25083; WQBSGS.
RefSeq; NP_389272.1; NC_000964.3.
RefSeq; WP_003244661.1; NZ_JNCM01000035.1.
PDB; 1AX3; NMR; -; A=539-699.
PDB; 1GPR; X-ray; 1.90 A; A=539-699.
PDBsum; 1AX3; -.
PDBsum; 1GPR; -.
ProteinModelPortal; P20166; -.
SMR; P20166; -.
STRING; 224308.Bsubs1_010100007711; -.
TCDB; 4.A.1.1.9; the pts glucose-glucoside (glc) family.
PaxDb; P20166; -.
PRIDE; P20166; -.
EnsemblBacteria; CAB13262; CAB13262; BSU13890.
GeneID; 939255; -.
KEGG; bsu:BSU13890; -.
PATRIC; fig|224308.179.peg.1515; -.
eggNOG; COG1263; LUCA.
eggNOG; COG1264; LUCA.
eggNOG; COG2190; LUCA.
HOGENOM; HOG000250993; -.
InParanoid; P20166; -.
KO; K20116; -.
KO; K20117; -.
KO; K20118; -.
OMA; AWAFNRF; -.
PhylomeDB; P20166; -.
BioCyc; BSUB:BSU13890-MONOMER; -.
SABIO-RK; P20166; -.
EvolutionaryTrace; P20166; -.
Proteomes; UP000001570; Chromosome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005355; F:glucose transmembrane transporter activity; IEA:InterPro.
GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
GO; GO:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:InterPro.
GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
CDD; cd00212; PTS_IIB_glc; 1.
Gene3D; 3.30.1360.60; -; 1.
InterPro; IPR011055; Dup_hybrid_motif.
InterPro; IPR036878; Glu_permease_IIB.
InterPro; IPR018113; PTrfase_EIIB_Cys.
InterPro; IPR001127; PTS_EIIA_1_perm.
InterPro; IPR003352; PTS_EIIC.
InterPro; IPR013013; PTS_EIIC_1.
InterPro; IPR001996; PTS_IIB_1.
InterPro; IPR011299; PTS_IIBC_glc.
InterPro; IPR004719; PTS_maltose/Glc_sub_IIC.
Pfam; PF00358; PTS_EIIA_1; 1.
Pfam; PF00367; PTS_EIIB; 1.
Pfam; PF02378; PTS_EIIC; 1.
SUPFAM; SSF51261; SSF51261; 1.
SUPFAM; SSF55604; SSF55604; 1.
TIGRFAMs; TIGR00826; EIIB_glc; 1.
TIGRFAMs; TIGR00830; PTBA; 1.
TIGRFAMs; TIGR00852; pts-Glc; 1.
TIGRFAMs; TIGR02002; PTS-II-BC-glcB; 1.
PROSITE; PS51093; PTS_EIIA_TYPE_1; 1.
PROSITE; PS00371; PTS_EIIA_TYPE_1_HIS; 1.
PROSITE; PS51098; PTS_EIIB_TYPE_1; 1.
PROSITE; PS01035; PTS_EIIB_TYPE_1_CYS; 1.
PROSITE; PS51103; PTS_EIIC_TYPE_1; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome; Kinase; Membrane;
Phosphotransferase system; Reference proteome; Sugar transport;
Transferase; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 699 PTS system glucose-specific EIICBA
component.
/FTId=PRO_0000186557.
TRANSMEM 16 36 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00426}.
TRANSMEM 66 86 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00426}.
TRANSMEM 89 109 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00426}.
TRANSMEM 139 159 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00426}.
TRANSMEM 180 200 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00426}.
TRANSMEM 233 253 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00426}.
TRANSMEM 283 303 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00426}.
TRANSMEM 313 333 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00426}.
TRANSMEM 338 358 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00426}.
TRANSMEM 365 385 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00426}.
TRANSMEM 388 408 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00426}.
DOMAIN 1 424 PTS EIIC type-1. {ECO:0000255|PROSITE-
ProRule:PRU00426}.
DOMAIN 439 520 PTS EIIB type-1. {ECO:0000255|PROSITE-
ProRule:PRU00421}.
DOMAIN 568 672 PTS EIIA type-1. {ECO:0000255|PROSITE-
ProRule:PRU00416}.
ACT_SITE 461 461 Phosphocysteine intermediate; for EIIB
activity. {ECO:0000255|PROSITE-
ProRule:PRU00421}.
ACT_SITE 620 620 Tele-phosphohistidine intermediate; for
EIIA activity. {ECO:0000255|PROSITE-
ProRule:PRU00416}.
STRAND 557 562 {ECO:0000244|PDB:1AX3}.
HELIX 563 565 {ECO:0000244|PDB:1AX3}.
STRAND 566 568 {ECO:0000244|PDB:1AX3}.
HELIX 569 572 {ECO:0000244|PDB:1AX3}.
STRAND 577 584 {ECO:0000244|PDB:1AX3}.
STRAND 586 592 {ECO:0000244|PDB:1AX3}.
STRAND 595 599 {ECO:0000244|PDB:1AX3}.
STRAND 602 614 {ECO:0000244|PDB:1AX3}.
STRAND 616 620 {ECO:0000244|PDB:1AX3}.
STRAND 622 624 {ECO:0000244|PDB:1AX3}.
TURN 625 632 {ECO:0000244|PDB:1AX3}.
STRAND 633 636 {ECO:0000244|PDB:1AX3}.
STRAND 641 643 {ECO:0000244|PDB:1AX3}.
STRAND 645 652 {ECO:0000244|PDB:1AX3}.
HELIX 654 657 {ECO:0000244|PDB:1AX3}.
HELIX 658 660 {ECO:0000244|PDB:1AX3}.
STRAND 666 672 {ECO:0000244|PDB:1AX3}.
HELIX 673 675 {ECO:0000244|PDB:1AX3}.
STRAND 678 681 {ECO:0000244|PDB:1AX3}.
STRAND 685 687 {ECO:0000244|PDB:1AX3}.
STRAND 692 698 {ECO:0000244|PDB:1AX3}.
SEQUENCE 699 AA; 75525 MW; 2A14D3C32EE0A9C5 CRC64;
MFKALFGVLQ KIGRALMLPV AILPAAGILL AIGNAMQNKD MIQVLHFLSN DNVQLVAGVM
ESAGQIVFDN LPLLFAVGVA IGLANGDGVA GIAAIIGYLV MNVSMSAVLL ANGTIPSDSV
ERAKFFTENH PAYVNMLGIP TLATGVFGGI IVGVLAALLF NRFYTIELPQ YLGFFAGKRF
VPIVTSISAL ILGLIMLVIW PPIQHGLNAF STGLVEANPT LAAFIFGVIE RSLIPFGLHH
IFYSPFWYEF FSYKSAAGEI IRGDQRIFMA QIKDGVQLTA GTFMTGKYPF MMFGLPAAAL
AIYHEAKPQN KKLVAGIMGS AALTSFLTGI TEPLEFSFLF VAPVLFAIHC LFAGLSFMVM
QLLNVKIGMT FSGGLIDYFL FGILPNRTAW WLVIPVGLGL AVIYYFGFRF AIRKFNLKTP
GREDAAEETA APGKTGEAGD LPYEILQAMG DQENIKHLDA CITRLRVTVN DQKKVDKDRL
KQLGASGVLE VGNNIQAIFG PRSDGLKTQM QDIIAGRKPR PEPKTSAQEE VGQQVEEVIA
EPLQNEIGEE VFVSPITGEI HPITDVPDQV FSGKMMGDGF AILPSEGIVV SPVRGKILNV
FPTKHAIGLQ SDGGREILIH FGIDTVSLKG EGFTSFVSEG DRVEPGQKLL EVDLDAVKPN
VPSLMTPIVF TNLAEGETVS IKASGSVNRE QEDIVKIEK


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