PTG3C_BACSU
ID PTG3C_BACSU Reviewed; 699 AA.
AC P20166; P08875;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=PTS system glucose-specific EIICBA component {ECO:0000250|UniProtKB:Q57071};
DE EC=2.7.1.199 {ECO:0000250|UniProtKB:Q57071};
DE AltName: Full=EII-Glc/EIII-Glc {ECO:0000305|PubMed:1911744};
DE AltName: Full=EIICBA-Glc {ECO:0000250|UniProtKB:Q57071};
DE AltName: Full=EIICBA-Glc 1 {ECO:0000305};
DE Includes:
DE RecName: Full=Glucose permease IIC component {ECO:0000250|UniProtKB:Q57071};
DE AltName: Full=PTS system glucose-specific EIIC component {ECO:0000250|UniProtKB:Q57071};
DE Includes:
DE RecName: Full=Glucose-specific phosphotransferase enzyme IIB component {ECO:0000250|UniProtKB:Q57071};
DE AltName: Full=PTS system glucose-specific EIIB component {ECO:0000250|UniProtKB:Q57071};
DE Includes:
DE RecName: Full=Glucose-specific phosphotransferase enzyme IIA component {ECO:0000250|UniProtKB:Q57071};
DE AltName: Full=PTS system glucose-specific EIIA component {ECO:0000250|UniProtKB:Q57071};
GN Name=ptsG; Synonyms=crr, ptsX; OrderedLocusNames=BSU13890;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1508157; DOI=10.1007/bf00283853;
RA Zagorec M., Postma P.W.;
RT "Cloning and nucleotide sequence of the ptsG gene of Bacillus subtilis.";
RL Mol. Gen. Genet. 234:325-328(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 361-699.
RC STRAIN=168;
RX PubMed=2497294; DOI=10.1111/j.1365-2958.1989.tb00109.x;
RA Gonzy-Treboul G., Zagorec M., Rain-Guion M.-C., Steinmetz M.;
RT "Phosphoenolpyruvate:sugar phosphotransferase system of Bacillus subtilis:
RT nucleotide sequence of ptsX, ptsH and the 5'-end of ptsI and evidence for a
RT ptsHI operon.";
RL Mol. Microbiol. 3:103-112(1989).
RN [4]
RP SEQUENCE REVISION.
RX PubMed=1956301; DOI=10.1111/j.1365-2958.1991.tb01898.x;
RA Gonzy-Treboul G., de Waard J.H., Zagorec M., Postma P.W.;
RT "The glucose permease of the phosphotransferase system of Bacillus
RT subtilis: evidence for IIGlc and IIIGlc domains.";
RL Mol. Microbiol. 5:1241-1249(1991).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 483-558.
RX PubMed=2120236; DOI=10.1016/s0021-9258(17)44791-0;
RA Sutrina S.L., Reddy P., Saier M.H. Jr., Reizer J.;
RT "The glucose permease of Bacillus subtilis is a single polypeptide chain
RT that functions to energize the sucrose permease.";
RL J. Biol. Chem. 265:18581-18589(1990).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF EIIA DOMAIN.
RX PubMed=1911744; DOI=10.1021/bi00104a004;
RA Liao D.-I., Kapadia G., Reddy P., Saier M.H. Jr., Reizer J., Herzberg O.;
RT "Structure of the IIA domain of the glucose permease of Bacillus subtilis
RT at 2.2-A resolution.";
RL Biochemistry 30:9583-9594(1991).
RN [7]
RP STRUCTURE BY NMR OF EIIA DOMAIN.
RX PubMed=1906345; DOI=10.1021/bi00242a013;
RA Fairbrother W.J., Cavanagh J., Dyson H.J., Plamer A.G. III, Sutrina S.L.,
RA Reizer J., Saier M.H. Jr., Wright P.E.;
RT "Polypeptide backbone resonance assignments and secondary structure of
RT Bacillus subtilis enzyme IIIglc determined by two-dimensional and three-
RT dimensional heteronuclear NMR spectroscopy.";
RL Biochemistry 30:6896-6907(1991).
RN [8]
RP STRUCTURE BY NMR OF EIAA DOMAIN.
RX PubMed=9593197;
RX DOI=10.1002/(sici)1097-0134(19980515)31:3<258::aid-prot3>3.0.co;2-f;
RA Chen Y., Case D.A., Reizer J., Saier M.H. Jr., Wright P.E.;
RT "High-resolution solution structure of Bacillus subtilis IIAglc.";
RL Proteins 31:258-270(1998).
CC -!- FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase
CC system (sugar PTS), a major carbohydrate active transport system,
CC catalyzes the phosphorylation of incoming sugar substrates
CC concomitantly with their translocation across the cell membrane. This
CC system is involved in glucose transport.
CC {ECO:0000250|UniProtKB:Q57071}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose(out) + N(pros)-phospho-L-histidyl-[protein] = D-
CC glucose 6-phosphate(in) + L-histidyl-[protein]; Xref=Rhea:RHEA:33367,
CC Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:9746, ChEBI:CHEBI:4167,
CC ChEBI:CHEBI:29979, ChEBI:CHEBI:61548, ChEBI:CHEBI:64837;
CC EC=2.7.1.199; Evidence={ECO:0000250|UniProtKB:Q57071};
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- DOMAIN: The EIIC domain forms the PTS system translocation channel and
CC contains the specific substrate-binding site. {ECO:0000255|PROSITE-
CC ProRule:PRU00426}.
CC -!- DOMAIN: The EIIB domain is phosphorylated by phospho-EIIA on a
CC cysteinyl or histidyl residue, depending on the transported sugar.
CC Then, it transfers the phosphoryl group to the sugar substrate
CC concomitantly with the sugar uptake processed by the EIIC domain.
CC {ECO:0000255|PROSITE-ProRule:PRU00421}.
CC -!- DOMAIN: The EIIA domain is phosphorylated by phospho-HPr on a histidyl
CC residue. Then, it transfers the phosphoryl group to the EIIB domain.
CC {ECO:0000255|PROSITE-ProRule:PRU00416}.
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DR EMBL; Z11744; CAA77803.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13262.1; -; Genomic_DNA.
DR EMBL; X12832; CAA31315.1; -; Genomic_DNA.
DR EMBL; M60344; AAA22498.1; -; Genomic_DNA.
DR PIR; S25083; WQBSGS.
DR RefSeq; NP_389272.1; NC_000964.3.
DR RefSeq; WP_003244661.1; NZ_JNCM01000035.1.
DR PDB; 1AX3; NMR; -; A=539-699.
DR PDB; 1GPR; X-ray; 1.90 A; A=539-699.
DR PDBsum; 1AX3; -.
DR PDBsum; 1GPR; -.
DR AlphaFoldDB; P20166; -.
DR BMRB; P20166; -.
DR SMR; P20166; -.
DR STRING; 224308.BSU13890; -.
DR TCDB; 4.A.1.1.9; the pts glucose-glucoside (glc) family.
DR jPOST; P20166; -.
DR PaxDb; P20166; -.
DR PRIDE; P20166; -.
DR EnsemblBacteria; CAB13262; CAB13262; BSU_13890.
DR GeneID; 939255; -.
DR KEGG; bsu:BSU13890; -.
DR PATRIC; fig|224308.179.peg.1515; -.
DR eggNOG; COG1263; Bacteria.
DR eggNOG; COG1264; Bacteria.
DR eggNOG; COG2190; Bacteria.
DR InParanoid; P20166; -.
DR OMA; AWAFNRF; -.
DR PhylomeDB; P20166; -.
DR BioCyc; BSUB:BSU13890-MON; -.
DR SABIO-RK; P20166; -.
DR EvolutionaryTrace; P20166; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005355; F:glucose transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:InterPro.
DR GO; GO:0090563; F:protein-phosphocysteine-sugar phosphotransferase activity; IBA:GO_Central.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00212; PTS_IIB_glc; 1.
DR Gene3D; 2.70.70.10; -; 1.
DR Gene3D; 3.30.1360.60; -; 1.
DR InterPro; IPR011055; Dup_hybrid_motif.
DR InterPro; IPR036878; Glu_permease_IIB.
DR InterPro; IPR018113; PTrfase_EIIB_Cys.
DR InterPro; IPR001127; PTS_EIIA_1_perm.
DR InterPro; IPR003352; PTS_EIIC.
DR InterPro; IPR013013; PTS_EIIC_1.
DR InterPro; IPR001996; PTS_IIB_1.
DR InterPro; IPR011299; PTS_IIBC_glc.
DR InterPro; IPR004719; PTS_maltose/Glc_sub_IIC.
DR Pfam; PF00358; PTS_EIIA_1; 1.
DR Pfam; PF00367; PTS_EIIB; 1.
DR Pfam; PF02378; PTS_EIIC; 1.
DR SUPFAM; SSF51261; SSF51261; 1.
DR SUPFAM; SSF55604; SSF55604; 1.
DR TIGRFAMs; TIGR00826; EIIB_glc; 1.
DR TIGRFAMs; TIGR00830; PTBA; 1.
DR TIGRFAMs; TIGR00852; pts-Glc; 1.
DR TIGRFAMs; TIGR02002; PTS-II-BC-glcB; 1.
DR PROSITE; PS51093; PTS_EIIA_TYPE_1; 1.
DR PROSITE; PS00371; PTS_EIIA_TYPE_1_HIS; 1.
DR PROSITE; PS51098; PTS_EIIB_TYPE_1; 1.
DR PROSITE; PS01035; PTS_EIIB_TYPE_1_CYS; 1.
DR PROSITE; PS51103; PTS_EIIC_TYPE_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Kinase; Membrane; Phosphotransferase system;
KW Reference proteome; Sugar transport; Transferase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..699
FT /note="PTS system glucose-specific EIICBA component"
FT /id="PRO_0000186557"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 283..303
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 338..358
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 365..385
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 388..408
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT DOMAIN 1..424
FT /note="PTS EIIC type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT DOMAIN 439..520
FT /note="PTS EIIB type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
FT DOMAIN 568..672
FT /note="PTS EIIA type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00416"
FT ACT_SITE 461
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
FT ACT_SITE 620
FT /note="Tele-phosphohistidine intermediate; for EIIA
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00416"
FT STRAND 557..562
FT /evidence="ECO:0007829|PDB:1AX3"
FT HELIX 563..565
FT /evidence="ECO:0007829|PDB:1AX3"
FT STRAND 566..568
FT /evidence="ECO:0007829|PDB:1AX3"
FT HELIX 569..572
FT /evidence="ECO:0007829|PDB:1AX3"
FT STRAND 577..584
FT /evidence="ECO:0007829|PDB:1AX3"
FT STRAND 586..592
FT /evidence="ECO:0007829|PDB:1AX3"
FT STRAND 595..599
FT /evidence="ECO:0007829|PDB:1AX3"
FT STRAND 602..614
FT /evidence="ECO:0007829|PDB:1AX3"
FT STRAND 616..620
FT /evidence="ECO:0007829|PDB:1AX3"
FT STRAND 622..624
FT /evidence="ECO:0007829|PDB:1AX3"
FT TURN 625..632
FT /evidence="ECO:0007829|PDB:1AX3"
FT STRAND 633..636
FT /evidence="ECO:0007829|PDB:1AX3"
FT STRAND 641..643
FT /evidence="ECO:0007829|PDB:1AX3"
FT STRAND 645..652
FT /evidence="ECO:0007829|PDB:1AX3"
FT HELIX 654..657
FT /evidence="ECO:0007829|PDB:1AX3"
FT HELIX 658..660
FT /evidence="ECO:0007829|PDB:1AX3"
FT STRAND 666..672
FT /evidence="ECO:0007829|PDB:1AX3"
FT HELIX 673..675
FT /evidence="ECO:0007829|PDB:1AX3"
FT STRAND 678..681
FT /evidence="ECO:0007829|PDB:1AX3"
FT STRAND 685..687
FT /evidence="ECO:0007829|PDB:1AX3"
FT STRAND 692..698
FT /evidence="ECO:0007829|PDB:1AX3"
SQ 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
