ID   PTG3C_STAS1             Reviewed;         678 AA.
AC   Q4A0C4;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 2.
DT   03-AUG-2022, entry version 107.
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=EIICBA-Glc {ECO:0000250|UniProtKB:Q57071};
DE            Short=EII-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; OrderedLocusNames=SSP0336;
OS   Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS   20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=342451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX   PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA   Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA   Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT   "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT   pathogenesis of uncomplicated urinary tract infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE17481.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AP008934; BAE17481.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q4A0C4; -.
DR   SMR; Q4A0C4; -.
DR   STRING; 342451.SSP0336; -.
DR   EnsemblBacteria; BAE17481; BAE17481; SSP0336.
DR   KEGG; ssp:SSP0336; -.
DR   PATRIC; fig|342451.11.peg.340; -.
DR   eggNOG; COG1263; Bacteria.
DR   eggNOG; COG1264; Bacteria.
DR   eggNOG; COG2190; Bacteria.
DR   HOGENOM; CLU_012312_1_1_9; -.
DR   Proteomes; UP000006371; 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: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: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; IPR011299; PTS_IIBC_glc.
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; 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   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..678
FT                   /note="PTS system glucose-specific EIICBA component"
FT                   /id="PRO_0000351406"
FT   TRANSMEM        16..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        63..83
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        126..146
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        170..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        211..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        273..293
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        303..323
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        329..349
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        355..375
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        382..402
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   DOMAIN          3..414
FT                   /note="PTS EIIC type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   DOMAIN          425..506
FT                   /note="PTS EIIB type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
FT   DOMAIN          547..651
FT                   /note="PTS EIIA type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00416"
FT   ACT_SITE        447
FT                   /note="Phosphocysteine intermediate; for EIIB activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
FT   ACT_SITE        599
FT                   /note="Tele-phosphohistidine intermediate; for EIIA
FT                   activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00416"
FT   CONFLICT        1
FT                   /note="M -> S (in Ref. 1; BAE17481)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   678 AA;  73829 MW;  C84758A55C1DFE13 CRC64;
     MFKKLFGQLQ RIGKALMLPV AILPAAGLLL AIGTAMQGES LQHYLPFIQN GGIQSVAEMM
     TGAGGIIFDN LPMIFAMGVA IGLASGDGVA AIAAFVGYLV MNKTMGAFLH VSPDNVNDAA
     SGYASVLGIP TLQTGVFGGI IIGALAAWCY NKFYNISLPS YLGFFAGKRF VPIMMATTSF
     ILAFPMAWIW PSIQTGLNAF SEGLLDSNTG LAVFLFGFIK RLLIPFGLHH IFHAPFWFEF
     GAWKNAAGEM IHGDQRIFIE QIREGSKLTA GKFMQGEFPV MMFGLPAAAL AIYHTAKPEN
     KKVVAGLMGS AALTSFLTGI TEPLEFSFLF VAPVLFFVHA ILDGLSFLIL YLLNVHLGYT
     FSGGFIDYVL LGVLPNKTQW WLVIPVGVVY AFIYYFVFRF LILKFKYKTP GREDKQAQFT
     NSSASELPFN VLKAMGGEEN IKHLDACITR LRVEVKEKGK VDVAGLKALG ASGVLEVGNN
     MQAIFGPKSD QIKHDMSLIM KGEITKPQET TVTEEESEEV VHIERASEVN IYAPGNGQVI
     PLSEVPDQVF AQKMMGDGVG FIPADGKIVA PFDGTVKTIF PTKHAIGLES DQGLELLIHI
     GIDTVKLNGE GFESFVETDD RVHKGQVLMQ IDLDYITAHA PSTVTPLIIT NLEDRQLSVE
     DVKDVTAEQL IIKVIDDK