PTU3C_STACT
ID PTU3C_STACT Reviewed; 692 AA.
AC Q53922; B9DP63; Q53948;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=PTS system glucoside-specific EIICBA component;
DE AltName: Full=EIICBA-Glc 2;
DE Includes:
DE RecName: Full=Glucoside permease IIC component;
DE AltName: Full=PTS system glucoside-specific EIIC component;
DE Includes:
DE RecName: Full=Glucoside-specific phosphotransferase enzyme IIB component;
DE EC=2.7.1.-;
DE AltName: Full=PTS system glucoside-specific EIIB component;
DE Includes:
DE RecName: Full=Glucoside-specific phosphotransferase enzyme IIA component;
DE AltName: Full=PTS system glucoside-specific EIIA component;
GN Name=glcB; OrderedLocusNames=Sca_1000;
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, SUBSTRATE SPECIFICITY, ACTIVITY
RP REGULATION, SUBCELLULAR LOCATION, AND 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 alpha- and beta-glucoside transport. Can also
CC transport glucose, but not galactose, fructose, mannose, cellobiose,
CC sucrose, maltose, lactose, melibiose and trehalose, as well as N-
CC acetylglucosamine. {ECO:0000269|PubMed:10537210}.
CC -!- ACTIVITY REGULATION: Inhibited by methyl alpha-D-glucoside, methyl
CC beta-D-glucoside, p-nitrophenyl alpha-D-glucoside, o-nitrophenyl beta-
CC D-glucoside and salicin, but not by 2-deoxyglucose.
CC {ECO:0000269|PubMed:10537210}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=19 uM for glucose {ECO:0000269|PubMed:10537210};
CC KM=37.2 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.
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 -!- DOMAIN: The EIIA domain is phosphorylated by phospho-HPr on a histidyl
CC residue. Then, it transfers the phosphoryl group to the EIIB domain.
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DR EMBL; X93360; CAA63743.1; -; Genomic_DNA.
DR EMBL; AM295250; CAL27908.1; -; Genomic_DNA.
DR PIR; S63606; S46953.
DR RefSeq; WP_015900249.1; NC_012121.1.
DR AlphaFoldDB; Q53922; -.
DR SMR; Q53922; -.
DR STRING; 396513.SCA_1000; -.
DR TCDB; 4.A.1.1.14; the pts glucose-glucoside (glc) family.
DR KEGG; sca:SCA_1000; -.
DR eggNOG; COG1263; Bacteria.
DR eggNOG; COG1264; Bacteria.
DR eggNOG; COG2190; Bacteria.
DR HOGENOM; CLU_012312_1_1_9; -.
DR OMA; YLIMTGT; -.
DR OrthoDB; 2035550at2; -.
DR BioCyc; SCAR396513:SCA_RS05020-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..692
FT /note="PTS system glucoside-specific EIICBA component"
FT /id="PRO_0000351419"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 215..235
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 287..307
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 398..418
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT DOMAIN 6..430
FT /note="PTS EIIC type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT DOMAIN 441..522
FT /note="PTS EIIB type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
FT DOMAIN 563..667
FT /note="PTS EIIA type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00416"
FT ACT_SITE 463
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
FT ACT_SITE 615
FT /note="Tele-phosphohistidine intermediate; for EIIA
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00416"
FT CONFLICT 309
FT /note="R -> P (in Ref. 1; CAA63743)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 692 AA; 75403 MW; 0BF5E8208F6227A0 CRC64;
MKNLLKKFFG QLQRIGKALM LPVAILPAAG ILLTFGNAMH NEQILHFAPW MQHHYIQLIS
QIMEASGQVI FDNLPLLFAM GTALGLAGGD GVAGIAALVG YLIMSATMGK IAGITIDDIF
SYADGAKTLG QSAKDPAHAL VLGIPTLQTG VFGGIIIGAL AAWCYNKFYN IQLPQFLGFF
AGKRFVPIIT SLVAIVTGIV LSFVWPPVQD GLNNLSNFLL GKNLALTTFI FGIIERSLIP
FGLHHIFYAP FWFEFGHYVN ESGNLVRGDQ RIWMAQYQDG VPFTAGAFTT GKYPFMMFGL
PAAAFAIYRQ AKPERRKVVG GLMLSAALTS FLTGITEPLE FSFLFVAPIL YVAHVILAGT
SFLIMHLLHV QIGMTFSGGF IDYILYGLLS WDRSNALLVI PVGIAYALIY YFLFTFLIKK
LNLKTPGRED KEVESKDVSV SELPFEVLEA MGNKDNIKHL DACITRLRVE VRDKGLVDVE
KLKQLGASGV LEVGNNMQAI FGPKSDQIKH DMQQIMDGKI TSPAETTVTE DGDVETAEIV
AEGGAVIYAP ITGEAVDLSE VPDKVFSAKM MGDGIAIKPE TGEVVAPFDG KVKMIFPTKH
AIGLESKDGI ELLIHFGLET VKLDGEGFEI LVKENDNIVL GQPLMKVDLN YIKEHADDTI
TPIIITNAGS ANIEVLHTGK VEQGEKLLLV NN
