PTG3C_STRPN
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 03-AUG-2022, entry version 152.
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; Firmicutes; 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=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 {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; NZ_AKVY01000001.1.
DR AlphaFoldDB; P35595; -.
DR SMR; P35595; -.
DR STRING; 170187.SP_0758; -.
DR EnsemblBacteria; AAK74896; AAK74896; SP_0758.
DR KEGG; spn:SP_0758; -.
DR eggNOG; COG1263; Bacteria.
DR eggNOG; COG1264; Bacteria.
DR eggNOG; COG2190; Bacteria.
DR OMA; EFMFMFV; -.
DR PhylomeDB; P35595; -.
DR BioCyc; SPNE170187:G1FZB-775-MON; -.
DR Proteomes; UP000000585; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
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; IPR011300; PTS_IIBC.
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; TIGR02003; PTS-II-BC-unk1; 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 Sugar transport; Transferase; Transmembrane; Transmembrane helix;
KW 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
