PTSBC_VIBAL
ID PTSBC_VIBAL Reviewed; 479 AA.
AC P22825;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 112.
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 Vibrio alginolyticus.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=663;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2174811; DOI=10.1016/0378-1119(90)90408-j;
RA Blatch G.L., Scholle R.R., Woods D.R.;
RT "Nucleotide sequence and analysis of the Vibrio alginolyticus sucrose
RT uptake-encoding region.";
RL Gene 95:17-23(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-12.
RX PubMed=2060795; DOI=10.1016/0378-1119(91)90222-w;
RA Blatch G.L., Woods D.R.;
RT "Nucleotide sequence and analysis of the Vibrio alginolyticus scr
RT repressor-encoding gene (scrR).";
RL Gene 101:45-50(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; M76768; AAA27555.1; -; Genomic_DNA.
DR EMBL; M35009; AAA27557.2; -; Genomic_DNA.
DR PIR; JQ0781; JQ0781.
DR AlphaFoldDB; P22825; -.
DR SMR; P22825; -.
DR STRING; 663.BAU10_17435; -.
DR eggNOG; COG1263; Bacteria.
DR eggNOG; COG1264; Bacteria.
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; Sugar transport; Transferase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..479
FT /note="PTS system sucrose-specific EIIBC component"
FT /id="PRO_0000186672"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 264..284
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 345..365
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 376..396
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 448..468
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 120..477
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 479 AA; 49890 MW; FBF906B5170E3EB7 CRC64;
MNYPAVAKEL LTLLGGKSNI TALAHCATRL RLAVADEQKI DEQAIDNLEG VKGQFKVAGQ
YQIIFGSGIV NQVYAEMAKL TGMSEMSTND VASAGAEKQN IVQPAVKGLS DIFVPIIPAI
VAGGLLMGIY NLLTAQGLFI DGKSLIEANP GLTDLANMIN TFANAPFVYL PILLAFSASK
KFGGNPYLGA ALGMLMVHPD LLNGWGFGGA SVSGNIPVWN ILGFEIQKVG YQGSVLPVLV
SAFILAKVEL GLRKVIPSVL DNLLTPLLAI FIAGLLTFTV VGPFTRDIGF LLGDGLNWLY
NTAGFVGGAV FGLIYAPFVI TGMHHSFIAI ETQLLADIAT TGGTFIFPIA AMSNVSQGAA
ALAVGVMSKD KKMKGIAIPS GVTGLLGITE PAMFGVNLKL RYPFIAAVCA AALSSAFITM
FNVKAQALGA AGLPGIISIT PDKIGYYIAG MVIAFLTAFV LTIVLGIGDR AKVGKKAAA
