ID   PTG3C_STAHJ             Reviewed;         675 AA.
AC   Q4L945;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 126.
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=SH0521;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC1435;
RX   PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA   Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP006716; BAE03830.1; -; Genomic_DNA.
DR   RefSeq; WP_011274846.1; NC_007168.1.
DR   AlphaFoldDB; Q4L945; -.
DR   SMR; Q4L945; -.
DR   STRING; 279808.SH0521; -.
DR   EnsemblBacteria; BAE03830; BAE03830; SH0521.
DR   GeneID; 58063286; -.
DR   KEGG; sha:SH0521; -.
DR   eggNOG; COG1263; Bacteria.
DR   eggNOG; COG1264; Bacteria.
DR   eggNOG; COG2190; Bacteria.
DR   HOGENOM; CLU_012312_1_1_9; -.
DR   OMA; AWAFNRF; -.
DR   OrthoDB; 2035550at2; -.
DR   Proteomes; UP000000543; 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   Sugar transport; Transferase; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..675
FT                   /note="PTS system glucose-specific EIICBA component"
FT                   /id="PRO_0000351405"
FT   TRANSMEM        16..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        59..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        81..101
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        173..193
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        199..219
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        328..348
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        378..398
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"
SQ   SEQUENCE   675 AA;  73214 MW;  6119AECA0C7FFB6D CRC64;
     MFKKLFGQLQ RIGKALMLPV AILPAAGLLL AIGTAFQGEA LQQYLPFIKN GVIQNIANMM
     TGAGGIIFDN LPIIFALGVA IGLAGGDGVA AIAAFVGFII MNKTMGAFLN VTPAQLEDPS
     KGFANVLGIP TLQTGVFGGI IIGALAAWCY NKFYNISLPS YLGFFAGKRF VPIMMATTSF
     ILAFPMAWIW PFIQNGLNAF STGLLDSNTG LAVFLFGFIK RLLIPFGLHH IFHAPFWFEF
     GSWKNAAGEI IRGDQRIFIE QIREGVHLTS GKFMQGEFPV MMFGLPAAAL AIYQTAKPEN
     KKVVGGLMLS AALTSFLTGI TEPLEFSFLF VAPLLFFIHA VLDGLSFLTL YLLNLHLGYT
     FSGGFIDFVL LGILPNKTPW WLVIPVGLVY AVIYYVVFRF LIVKFNFKTP GREDKQASVA
     NTSASKLPFD VLDAMGGKEN IKHLDACITR LRVEVNDKSK VDVEGLKALG ASGVLEVGNN
     MQAIFGPKSD QIKHDMARIM NGDITKPSET TVTEDTSDEP VQLEEVKETD IYAPGTGHII
     PLSEVPDKVF SEKMMGDGIG FVPEKGGIVA PFDGTVKTIF PTKHAIGLES DTGIEVLIHI
     GIDTVKLNGE GFESLVDVNE PVTQGQPLMK INLAYLKEHA PSVVTPVIIT NQGDKTLTFD
     DVDSVDPGKR IMTIK