PTG3C_STACT
ID PTG3C_STACT Reviewed; 675 AA.
AC Q57071; B9DP62;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=PTS system glucose-specific EIICBA component {ECO:0000303|PubMed:10537210};
DE EC=2.7.1.199 {ECO:0000305|PubMed:10537210};
DE AltName: Full=EIICBA-Glc {ECO:0000303|PubMed:10537210};
DE Short=EII-Glc {ECO:0000303|PubMed:10537210};
DE AltName: Full=EIICBA-Glc 1 {ECO:0000305};
DE Includes:
DE RecName: Full=Glucose permease IIC component {ECO:0000303|PubMed:10537210};
DE AltName: Full=PTS system glucose-specific EIIC component {ECO:0000303|PubMed:10537210};
DE Includes:
DE RecName: Full=Glucose-specific phosphotransferase enzyme IIB component {ECO:0000303|PubMed:10537210};
DE AltName: Full=PTS system glucose-specific EIIB component {ECO:0000303|PubMed:10537210};
DE Includes:
DE RecName: Full=Glucose-specific phosphotransferase enzyme IIA component {ECO:0000303|PubMed:10537210};
DE AltName: Full=PTS system glucose-specific EIIA component {ECO:0000303|PubMed:10537210};
GN Name=ptsG; Synonyms=glcA {ECO:0000303|PubMed:10537210};
GN OrderedLocusNames=Sca_0999;
OS Staphylococcus carnosus (strain TM300).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=396513;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8602153; DOI=10.1007/bf02174396;
RA Christiansen I., Hengstenberg W.;
RT "Cloning and sequencing of two genes from Staphylococcus carnosus coding
RT for glucose-specific PTS and their expression in Escherichia coli K-12.";
RL Mol. Gen. Genet. 250:375-379(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TM300;
RX PubMed=19060169; DOI=10.1128/aem.01982-08;
RA Rosenstein R., Nerz C., Biswas L., Resch A., Raddatz G., Schuster S.C.,
RA Goetz F.;
RT "Genome analysis of the meat starter culture bacterium Staphylococcus
RT carnosus TM300.";
RL Appl. Environ. Microbiol. 75:811-822(2009).
RN [3]
RP PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10537210; DOI=10.1099/00221287-145-10-2881;
RA Christiansen I., Hengstenberg W.;
RT "Staphylococcal phosphoenolpyruvate-dependent phosphotransferase system
RT -- two highly similar glucose permeases in Staphylococcus carnosus with
RT different glucoside specificity: protein engineering in vivo?";
RL Microbiology 145:2881-2889(1999).
RN [4]
RP INDUCTION BY GLCT.
RX PubMed=10974121; DOI=10.1099/00221287-146-9-2333;
RA Knezevic I., Bachem S., Sickmann A., Meyer H.E., Stuelke J.,
RA Hengstenberg W.;
RT "Regulation of the glucose-specific phosphotransferase system (PTS) of
RT Staphylococcus carnosus by the antiterminator protein GlcT.";
RL Microbiology 146:2333-2342(2000).
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. Cannot transport galactose,
CC fructose, mannose, cellobiose, sucrose, maltose, lactose, melibiose and
CC trehalose, as well as N-acetylglucosamine.
CC {ECO:0000269|PubMed:10537210}.
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:0000305|PubMed:10537210};
CC -!- ACTIVITY REGULATION: Inhibited by 2-deoxyglucose and methyl beta-D-
CC glucoside, but not by methyl alpha-D-glucoside, p-nitrophenyl alpha-D-
CC glucoside, o-nitrophenyl beta-D-glucoside and salicin.
CC {ECO:0000269|PubMed:10537210}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=12 uM for glucose {ECO:0000269|PubMed:10537210};
CC KM=30.5 uM for glucose (in the presence of Triton X-100)
CC {ECO:0000269|PubMed:10537210};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00426, ECO:0000269|PubMed:10537210}; Multi-pass membrane
CC protein {ECO:0000255|PROSITE-ProRule:PRU00426,
CC ECO:0000269|PubMed:10537210}.
CC -!- INDUCTION: Up-regulated by the antiterminator protein GlcT.
CC {ECO:0000269|PubMed:10974121}.
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; X93360; CAA63742.1; -; Genomic_DNA.
DR EMBL; AM295250; CAL27907.1; -; Genomic_DNA.
DR PIR; S46952; S46952.
DR RefSeq; WP_015900248.1; NC_012121.1.
DR AlphaFoldDB; Q57071; -.
DR SMR; Q57071; -.
DR STRING; 396513.SCA_0999; -.
DR TCDB; 4.A.1.1.13; the pts glucose-glucoside (glc) family.
DR GeneID; 60545310; -.
DR KEGG; sca:SCA_0999; -.
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 BioCyc; SCAR396513:SCA_RS05015-MON; -.
DR Proteomes; UP000000444; 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 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Kinase; Membrane;
KW Phosphotransferase system; Sugar transport; Transferase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..675
FT /note="PTS system glucose-specific EIICBA component"
FT /id="PRO_0000351401"
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 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 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 383..403
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; 73111 MW; 523BAF4EF362B7E2 CRC64;
MWKKFFGQLQ RIGKALMLPV AILPAAGLLL ALGNAFQGDA LQSLMPFIKA EGFQNVAKMM
EGAGGIIFDN LAIIFALGVA IGLASGDGVA AIAAFVGFIV LNKTMGMFLG VTPEKAADAA
TGFANVLGIP TLQTGVFGGI IIGALAAWCY NKFYNISLPS YLGFFAGKRF VPIMMATCSF
ILAFPMAIIW PSIQGGLNAF SEGLLASNTG LAVFLFGFIK RLLIPFGLHH IFHAPFWFEF
GSYKNAAGQI IHGDQRIFIE QIRDNVPLTA GKFMQGEFPV MMFGLPAAAL AIYQTAKKEN
KKVVAGLMLS GALTSFLTGI TEPLEFSFLF VAPLLFFIHA VLDGLSFLIL YLLDLHLGYT
FSGGFIDFFL LGILPNKTQW WLVIPVGLVY AAIYYIIFRF LIVKFNFKTP GREDKEVKSS
NVAASELPFK VLDAMGGKAN IKHLDACITR LRVEVNDKAK VDVQELKDLG ASGVLEVGNN
MQAIFGPKSD QIKHDMQQIM DGKITSPEET TVTEEGDKET AEIAAAGGGV VYAPIKGEVV
DISEVPDKVF SEKMMGDGIA IKPETGEVVA PFDGVVKMVF PTKHAIGLES KDGIELLIHF
GLETVKLEGK GFDILVKEND NIVLGQPLMK VDLDYIKEHA DSTITPIVVT NLNGRTMEVL
QHGEVKQGDK VILVK
