PTG3C_GEOSE
ID PTG3C_GEOSE Reviewed; 324 AA.
AC P42015;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 111.
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};
DE Flags: Fragment;
GN Name=ptsG;
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=XL-65-6;
RX PubMed=7670643; DOI=10.1099/13500872-141-6-1443;
RA Lai X., Ingram L.O.;
RT "Discovery of a ptsHI operon, which includes a third gene (ptsT), in the
RT thermophile Bacillus stearothermophilus.";
RL Microbiology 141:1443-1449(1995).
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 (By similarity).
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; U12340; AAA86047.1; -; Genomic_DNA.
DR AlphaFoldDB; P42015; -.
DR SMR; P42015; -.
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; IPR001996; PTS_IIB_1.
DR Pfam; PF00358; PTS_EIIA_1; 1.
DR Pfam; PF00367; PTS_EIIB; 1.
DR SUPFAM; SSF51261; SSF51261; 1.
DR SUPFAM; SSF55604; SSF55604; 1.
DR TIGRFAMs; TIGR00826; EIIB_glc; 1.
DR TIGRFAMs; TIGR00830; PTBA; 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.
PE 3: Inferred from homology;
KW Cell membrane; Kinase; Membrane; Phosphotransferase system;
KW Sugar transport; Transferase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN <1..324
FT /note="PTS system glucose-specific EIICBA component"
FT /id="PRO_0000186556"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT DOMAIN <1..63
FT /note="PTS EIIC type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT DOMAIN 78..159
FT /note="PTS EIIB type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
FT DOMAIN 194..298
FT /note="PTS EIIA type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00416"
FT REGION 156..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 100
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
FT ACT_SITE 246
FT /note="Tele-phosphohistidine intermediate; for EIIA
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00416"
FT NON_TER 1
SQ SEQUENCE 324 AA; 34674 MW; 89B712E6A6624F3F CRC64;
HLLNVKIGMT FSGGVIDFLL FGVLPNRTAW WLVIPVGLVF AVIYYFGFRF AIRKWDLATP
GREKTVEEAP KAEAAAAGDL PYEVLAALGG KENIEHLDAC ITRLRVSVHD IGRVDKDRLK
ALGAAGVLEV GNNVQAIFGP KSDMLKGQIQ DIMQGKAPAR AEEKPKTAAS EAAESETIAS
PMSGEIVPLA EVPDQVFSQK MMGDGFAVMP TDGTVVSPVD GKIINVFPTK HAIGIQSAGG
HEILIHVGID TVKLNGQGFE ALVKEGDEVK KGQPILRVDL DYVKQNAPSI VTPVIFTNLQ
AGETVHVNKQ GPVARGEDAV VTIR
