PTGCB_SALTY
ID PTGCB_SALTY Reviewed; 477 AA.
AC P37439;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=PTS system glucose-specific EIICB component {ECO:0000303|PubMed:6292227};
DE AltName: Full=EIICB-Glc {ECO:0000303|PubMed:6292227};
DE Short=EII-Glc {ECO:0000303|PubMed:6292227};
DE Includes:
DE RecName: Full=Glucose permease IIC component {ECO:0000303|PubMed:6292227};
DE AltName: Full=PTS system glucose-specific EIIC component {ECO:0000303|PubMed:6292227};
DE Includes:
DE RecName: Full=Glucose-specific phosphotransferase enzyme IIB component {ECO:0000303|PubMed:6292227};
DE EC=2.7.1.199 {ECO:0000269|PubMed:6292227};
DE AltName: Full=PTS system glucose-specific EIIB component {ECO:0000303|PubMed:6292227};
GN Name=ptsG; OrderedLocusNames=STM1203;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SB3507;
RA Stolz B., Wehrli C., Erni B.;
RL Submitted (AUG-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE
RP SPECIFICITY.
RX PubMed=6292227; DOI=10.1016/s0021-9258(19)45412-4;
RA Stock J.B., Waygood E.B., Meadow N.D., Postma P.W., Roseman S.;
RT "Sugar transport by the bacterial phosphotransferase system. The glucose
RT receptors of the Salmonella typhimurium phosphotransferase system.";
RL J. Biol. Chem. 257:14543-14552(1982).
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. The
CC enzyme II complex composed of PtsG and Crr is involved in glucose
CC transport. Also functions as a chemoreceptor monitoring the environment
CC for changes in sugar concentration. It can also phosphorylate mannose,
CC methyl alpha-glucoside and 2-deoxy-glucose.
CC {ECO:0000269|PubMed:6292227}.
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:0000269|PubMed:6292227};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6 uM for methyl alpha-glucoside {ECO:0000269|PubMed:6292227};
CC KM=10 uM for glucose {ECO:0000269|PubMed:6292227};
CC KM=40 uM for mannose {ECO:0000269|PubMed:6292227};
CC KM=200 uM for 2-deoxy-glucose {ECO:0000269|PubMed:6292227};
CC Vmax=126 umol/min/mg enzyme with methyl alpha-glucoside as substrate
CC {ECO:0000269|PubMed:6292227};
CC Vmax=126 umol/min/mg enzyme with glucose as substrate
CC {ECO:0000269|PubMed:6292227};
CC Vmax=10 umol/min/mg enzyme with mannose as substrate
CC {ECO:0000269|PubMed:6292227};
CC Vmax=10 umol/min/mg enzyme with 2-deoxy-glucose as substrate
CC {ECO:0000269|PubMed:6292227};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00426}; Multi-pass membrane protein {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 EIIC domain forms the PTS system translocation channel and
CC contains the specific substrate-binding site. {ECO:0000255|PROSITE-
CC ProRule:PRU00426}.
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DR EMBL; X74629; CAA52702.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20132.1; -; Genomic_DNA.
DR PIR; S36620; S36620.
DR RefSeq; NP_460173.1; NC_003197.2.
DR RefSeq; WP_000475705.1; NC_003197.2.
DR AlphaFoldDB; P37439; -.
DR SMR; P37439; -.
DR STRING; 99287.STM1203; -.
DR PaxDb; P37439; -.
DR PRIDE; P37439; -.
DR EnsemblBacteria; AAL20132; AAL20132; STM1203.
DR GeneID; 1252721; -.
DR GeneID; 66755606; -.
DR KEGG; stm:STM1203; -.
DR PATRIC; fig|99287.12.peg.1272; -.
DR HOGENOM; CLU_012312_1_0_6; -.
DR OMA; AWAFNRF; -.
DR PhylomeDB; P37439; -.
DR BioCyc; SENT99287:STM1203-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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:0090564; F:protein-phosphocysteine-glucose phosphotransferase system transporter activity; IBA:GO_Central.
DR GO; GO:0090563; F:protein-phosphocysteine-sugar phosphotransferase activity; IBA:GO_Central.
DR GO; GO:1904659; P:glucose transmembrane transport; IBA:GO_Central.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00212; PTS_IIB_glc; 1.
DR Gene3D; 3.30.1360.60; -; 1.
DR InterPro; IPR036878; Glu_permease_IIB.
DR InterPro; IPR018113; PTrfase_EIIB_Cys.
DR InterPro; IPR003352; PTS_EIIC.
DR InterPro; IPR013013; PTS_EIIC_1.
DR InterPro; IPR001996; PTS_IIB_1.
DR InterPro; IPR011299; PTS_IIBC_glc.
DR InterPro; IPR004719; PTS_maltose/Glc_sub_IIC.
DR Pfam; PF00367; PTS_EIIB; 1.
DR Pfam; PF02378; PTS_EIIC; 1.
DR SUPFAM; SSF55604; SSF55604; 1.
DR TIGRFAMs; TIGR00826; EIIB_glc; 1.
DR TIGRFAMs; TIGR00852; pts-Glc; 1.
DR TIGRFAMs; TIGR02002; PTS-II-BC-glcB; 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 inner membrane; Cell membrane; Kinase; Membrane; Phosphoprotein;
KW Phosphotransferase system; Reference proteome; Sugar transport;
KW Transferase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..477
FT /note="PTS system glucose-specific EIICB component"
FT /id="PRO_0000186531"
FT TOPO_DOM 1..14
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 36..50
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 72..79
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 101..111
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 133..151
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 173..190
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 212..248
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 270..279
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 301..309
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 310..330
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 331..355
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 356..376
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 377..477
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 1..388
FT /note="PTS EIIC type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT DOMAIN 399..477
FT /note="PTS EIIB type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
FT ACT_SITE 421
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000250|UniProtKB:P69786,
FT ECO:0000255|PROSITE-ProRule:PRU00421"
FT MOD_RES 421
FT /note="Phosphocysteine"
FT /evidence="ECO:0000250|UniProtKB:P69786"
FT CONFLICT 218
FT /note="F -> S (in Ref. 1; CAA52702)"
FT /evidence="ECO:0000305"
FT CONFLICT 379
FT /note="L -> F (in Ref. 1; CAA52702)"
FT /evidence="ECO:0000305"
FT CONFLICT 477
FT /note="S -> H (in Ref. 1; CAA52702)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 477 AA; 50497 MW; 8CD10142542FF797 CRC64;
MFKNAFANLQ KVGKSLMLPV SVLPIAGILL GVGSANFSWL PAVVSHVMAE AGGSVFANMP
LIFAIGVALG FTNNDGVSAL AAVVAYGIMV KTMAVVAPLV LHLPAEEIAA KHLADTGVLG
GIISGAIAAY MFNRFYRIKL PEYLGFFAGK RFVPIISGLA AIFTGVVLSF VWPPIGTAIQ
AFSQWAAYQN PVVAFGIYGF IERCLVPFGL HHIWNVPFQM QIGEYTNAAG QVFHGDIPRY
MAGDPTAGML SGGFLFKMYG LPAAAIAIWH SAKPENRAKV GGIMISAALT SFLTGITEPI
EFSFMFVAPI LYIIHAILAG LAFPICILLG MRDGTSFSHG LIDFIVLSGN SSKLWLFPIV
GAGYAIVYYT VFRVLIKALD LKTPGREDTT DDAKAGATSE MAPALVAAFG GKENITNLDA
CITRLRVSVA DVAKVDQAGL KKLGAAGVVV AGSGVQAIFG TKSDNLKTEM DEYIRNS
