PTG3C_STAES
ID PTG3C_STAES Reviewed; 675 AA.
AC Q7CCJ4;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=SE_2102;
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(2003).
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; AE015929; AAO05744.1; -; Genomic_DNA.
DR RefSeq; NP_765657.1; NC_004461.1.
DR RefSeq; WP_001832339.1; NZ_WBME01000013.1.
DR AlphaFoldDB; Q7CCJ4; -.
DR SMR; Q7CCJ4; -.
DR STRING; 176280.SE_2102; -.
DR EnsemblBacteria; AAO05744; AAO05744; SE_2102.
DR GeneID; 50017816; -.
DR KEGG; sep:SE_2102; -.
DR PATRIC; fig|176280.10.peg.2053; -.
DR eggNOG; COG1263; Bacteria.
DR eggNOG; COG1264; Bacteria.
DR eggNOG; COG2190; Bacteria.
DR HOGENOM; CLU_012312_1_1_9; -.
DR OMA; AWAFNRF; -.
DR Proteomes; UP000001411; 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_0000351404"
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 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 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; 73359 MW; AD6EC55F6C15C4C2 CRC64;
MFKKLFGQMQ RIGKALMLPV AILPAAGLLL AIGTAFQGEA LQHYLPFIKN DIVQQIANML
TGAGGIIFDN LPIIFALGVA IGLAGGDGVA AIAAFVGFII LNKTMGAFLH VTPDKLSDPT
NGYANVLGIP TLQTGVFGGI IIGALAAWCY NKFYNITLPS YLGFFAGKRF VPIMMATTSF
ILAFPMAIIW PTIQNGLNAF SEGLLDSNTG LAVFLFGFIK RLLIPFGLHH IFHAPFWFEF
GSWKNAAGEI IRGDQRIFIE QIREGAHLTS GKFMQGEFPV MMFGLPAAAL AIYQTAKPEN
KKVVAGLMIS AALTSFLTGI TEPLEFSFLF VAPFLFVIHA VLDGLSFLTL YLLNVHLGYT
FSGGFIDYVL LGILPNKTAW WLVIPVGIIY AVIYYFVFRF LIVKFNYKTP GREDKKSSVT
TTSASQLPFD VLKAMGGKEN IKHLDACITR LRVEVNEKSK VDVAGLKSLG ASGVLEVGNN
MQAIFGPKSD QIKHDMAKII SGEITKPSET TIDEEVSDDP VHVEDIVETE IYAPGHGEII
PLSEVPDKVF SEKMMGDGIG FVPDSGEIVA PFDGTVKTIF PTKHAIGLES DSGVEVLIHI
GIDTVKLNGE GFESLVNTDE PVTQGQPLMK IDLEYLKEHA PSIITPVIIT NQEDKTLTIE
DVKQVDPGKA IMTIK
