PTSBC_SALTM
ID PTSBC_SALTM Reviewed; 456 AA.
AC P08470;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=PTS system sucrose-specific EIIBC component;
DE AltName: Full=EIIBC-Scr;
DE Short=EII-Scr;
DE Includes:
DE RecName: Full=Sucrose-specific phosphotransferase enzyme IIB component;
DE EC=2.7.1.-;
DE AltName: Full=PTS system sucrose-specific EIIB component;
DE Includes:
DE RecName: Full=Sucrose permease IIC component;
DE AltName: Full=PTS system sucrose-specific EIIC component;
GN Name=scrA;
OS Salmonella typhimurium.
OG Plasmid pUR400.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90371;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3285123; DOI=10.1111/j.1365-2958.1988.tb00002.x;
RA Ebner R., Lengeler J.W.;
RT "DNA sequence of the gene scrA encoding the sucrose transport protein
RT EnzymeII(Scr) of the phosphotransferase system from enteric bacteria:
RT homology of the EnzymeII(Scr) and EnzymeII(Bgl) proteins.";
RL Mol. Microbiol. 2:9-17(1988).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=8412665; DOI=10.1111/j.1365-2958.1993.tb01681.x;
RA Jahreis K., Lengeler J.W.;
RT "Molecular analysis of two ScrR repressors and of a ScrR-FruR hybrid
RT repressor for sucrose and D-fructose specific regulons from enteric
RT bacteria.";
RL Mol. Microbiol. 9:195-209(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8628219; DOI=10.1007/bf02174179;
RA Titgemeyer F., Jahreis K., Ebner R., Lengeler J.W.;
RT "Molecular analysis of the scrA and scrB genes from Klebsiella pneumoniae
RT and plasmid pUR400, which encode the sucrose transport protein Enzyme II
RT Scr of the phosphotransferase system and a sucrose-6-phosphate invertase.";
RL Mol. Gen. Genet. 250:197-206(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7.
RC STRAIN=6153-62;
RX PubMed=1846143; DOI=10.1128/jb.173.2.449-456.1991;
RA Hardesty C., Ferran C., DiRienzo J.M.;
RT "Plasmid-mediated sucrose metabolism in Escherichia coli: characterization
RT of scrY, the structural gene for a phosphoenolpyruvate-dependent sucrose
RT phosphotransferase system outer membrane porin.";
RL J. Bacteriol. 173:449-456(1991).
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 sucrose transport.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
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 EIIC domain forms the PTS system translocation channel and
CC contains the specific substrate-binding site.
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DR EMBL; Y00541; CAA68605.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X67750; CAA47973.1; -; Genomic_DNA.
DR EMBL; M38416; AAA98418.1; -; Genomic_DNA.
DR PIR; B39127; B39127.
DR PIR; S01036; WQEBST.
DR AlphaFoldDB; P08470; -.
DR SMR; P08470; -.
DR TCDB; 4.A.1.2.1; the pts glucose-glucoside (glc) family.
DR BRENDA; 2.7.1.211; 5542.
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: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; 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; IPR010973; PTS_IIBC_sucr.
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; TIGR01996; PTS-II-BC-sucr; 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 4: Predicted;
KW Cell inner membrane; Cell membrane; Kinase; Membrane;
KW Phosphotransferase system; Plasmid; Sugar transport; Transferase;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..456
FT /note="PTS system sucrose-specific EIIBC component"
FT /id="PRO_0000186670"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 288..308
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 360..380
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 388..408
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 428..448
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT DOMAIN 1..87
FT /note="PTS EIIB type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
FT DOMAIN 107..456
FT /note="PTS EIIC type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT ACT_SITE 26
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
SQ SEQUENCE 456 AA; 47865 MW; 98A6F1620AE50885 CRC64;
MDFEQISCSL LPLLGGKENI ASAAHCATRL RLVLVDDSLA DQQAIGKVEG VKGCFRNAGQ
MQIIFGTGVV NKVYAAFTQA AGISESSKSE AADIAAKKLN PFQRIARLLS NIFVPIIPAI
VASGLLMGLL GMVKTYGWVD PGNAIYIMLD MCSSAAFIIL PILIGFTAAR EFGGNPYLGA
TLGGILTHPA LTNAWGVAAG FHTMNFFGFE IAMIGYQGTV FPVLLAVWFM SIVEKQLRRA
IPDALDLILT PFLTVIISGF IALLIIGPAG RALGDGISFV LSTLISHAGW LAGLLFGGLY
SVIVITGIHH SFHAVEAGLL GNPSIGVNFL LPIWAMANVA QGGACLAVWF KTKDAKIKAI
TLPSAFSAML GITEAAIFGI NLRFVKPFIA ALIGGAAGGA WVVSVHVYMT AVGLTAIPGM
AIVQASSLLN YIIGMVIAFG VAFTVSLVLK YKTDAE
