ID   PTG3C_STRPN             Reviewed;         726 AA.
AC   P35595;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   26-SEP-2001, sequence version 2.
DT   02-SEP-2026, entry version 168.
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;
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=exp5; OrderedLocusNames=SP_0758;
OS   Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=170187;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-334 / TIGR4;
RX   PubMed=11463916; DOI=10.1126/science.1061217;
RA   Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA   Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA   Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA   Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA   Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA   McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA   Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA   Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT   "Complete genome sequence of a virulent isolate of Streptococcus
RT   pneumoniae.";
RL   Science 293:498-506(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 468-575.
RC   STRAIN=R6x;
RX   PubMed=7934910; DOI=10.1111/j.1365-2958.1993.tb01233.x;
RA   Pearce B.J., Yin Y.B., Masure H.R.;
RT   "Genetic identification of exported proteins in Streptococcus pneumoniae.";
RL   Mol. Microbiol. 9:1037-1050(1993).
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=N(pros)-phospho-L-histidyl-[protein] + D-glucose(out) = 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 {ECO:0000255|PROSITE-
CC       ProRule:PRU00426}; Multi-pass membrane protein {ECO:0000255|PROSITE-
CC       ProRule:PRU00426}.
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; AE005672; AAK74896.1; -; Genomic_DNA.
DR   EMBL; L20559; AAA26881.1; -; Genomic_DNA.
DR   PIR; G95087; G95087.
DR   RefSeq; WP_000974062.1; NC_003028.3.
DR   AlphaFoldDB; P35595; -.
DR   SMR; P35595; -.
DR   EnsemblBacteria; AAK74896; AAK74896; SP_0758.
DR   KEGG; spn:SP_0758; -.
DR   eggNOG; COG1263; Bacteria.
DR   eggNOG; COG1264; Bacteria.
DR   eggNOG; COG2190; Bacteria.
DR   PhylomeDB; P35595; -.
DR   BioCyc; SPNE170187:G1FZB-775-MONOMER; -.
DR   Proteomes; UP000000585; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008982; F:protein-N(PI)-phosphohistidine-carbohydrate phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0090563; F:protein-phosphocysteine-sugar phosphotransferase activity; IEA:TreeGrafter.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:InterPro.
DR   CDD; cd00212; PTS_IIB_glc; 1.
DR   FunFam; 2.70.70.10:FF:000001; PTS system glucose-specific IIA component; 1.
DR   Gene3D; 2.70.70.10; Glucose Permease (Domain IIA); 1.
DR   Gene3D; 3.30.1360.60; Glucose permease domain IIB; 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; IPR050429; PTS_Glucose_EIICBA.
DR   InterPro; IPR001996; PTS_IIB_1.
DR   InterPro; IPR011300; PTS_IIBC.
DR   NCBIfam; TIGR00826; EIIB_glc; 1.
DR   NCBIfam; TIGR00830; PTBA; 1.
DR   NCBIfam; TIGR02003; PTS-II-BC-unk1; 1.
DR   PANTHER; PTHR30009; CYTOCHROME C-TYPE SYNTHESIS PROTEIN AND PTS TRANSMEMBRANE COMPONENT; 1.
DR   PANTHER; PTHR30009:SF8; PTS SYSTEM, IIBC COMPONENT; 1.
DR   Pfam; PF00358; PTS_EIIA_1; 1.
DR   Pfam; PF00367; PTS_EIIB; 1.
DR   Pfam; PF02378; PTS_EIIC; 1.
DR   SUPFAM; SSF51261; Duplicated hybrid motif; 1.
DR   SUPFAM; SSF55604; Glucose permease domain IIB; 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   3: Inferred from homology;
KW   Cell membrane; Kinase; Membrane; Phosphotransferase system;
KW   Reference proteome; Sugar transport; Transferase; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..726
FT                   /note="PTS system glucose-specific EIICBA component"
FT                   /id="PRO_0000186561"
FT   TRANSMEM        18..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        62..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        90..110
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        184..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        311..331
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        344..364
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        419..439
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   DOMAIN          1..453
FT                   /note="PTS EIIC type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   DOMAIN          473..555
FT                   /note="PTS EIIB type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
FT   DOMAIN          596..700
FT                   /note="PTS EIIA type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00416"
FT   ACT_SITE        495
FT                   /note="Phosphocysteine intermediate; for EIIB activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
FT   ACT_SITE        648
FT                   /note="Tele-phosphohistidine intermediate; for EIIA
FT                   activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00416"
FT   CONFLICT        471..472
FT                   /note="AA -> DD (in Ref. 2; AAA26881)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        566
FT                   /note="A -> V (in Ref. 2; AAA26881)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   726 AA;  77995 MW;  7C1F7D55ADE16E81 CRC64;
     MMKDTFKNVL SFEFWQKFGK ALMVVIAVMP AAGLMISIGK SIVMINPTFA PLVITGGILE
     QIGWGVIGNL HILFALAIGG SWAKERAGGA FAAGLAFILI NRITGTIFGV SGDMLKNPDA
     MVTTFFGGSI KVADYFISVL EAPALNMGVF VGIISGFVGA TAYNKYYNFR KLPDALSFFN
     GKRFVPFVVI LRSAIAAILL AAFWPVVQTG INNFGIWIAN SQETAPILAP FLYGTLERLL
     LPFGLHHMLT IPMNYTALGG TYDILTGAAK GTQVFGQDPL WLAWVTDLVN LKGTDASQYQ
     HLLDTVHPAR FKVGQMIGSF GILMGVIVAI YRNVDADKKH KYKGMMIATA LATFLTGVTE
     PIEYMFMFIA TPMYLVYSLV QGAAFAMADV VNLRMHSFGS IEFLTRTPIA ISAGIGMDIV
     NFVWVTVLFA VIMYFIANFM IQKFNYATPG RNGNYETAEG SEETSSEVKV AAGSQAVNII
     NLLGGRVNIV DVDACMTRLR VTVKDADKVG NAEQWKAEGA MGLVMKGQGV QAIYGPKADI
     LKSDIQDILD SGEIIPETLP SQMTEAQQNT VHFKDLTEEV YSVADGQVVA LEQVKDPVFA
     QKMMGDGFAV EPANGNIVSP VSGTVSSIFP TKHAFGIVTE AGLEVLVHIG LDTVSLEGKP
     FTVHVAEGQK VAAGDLLVTA DLDAIRAAGR ETSTVVVFTN GDAIKSVKLE KTGSLAAKTA
     VAKVEL
//