PTSBC_STAXY
ID PTSBC_STAXY Reviewed; 480 AA.
AC P51184;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 117.
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 Staphylococcus xylosus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1288;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 20267 / Isolate C2A;
RX PubMed=8232209; DOI=10.1007/bf00280198;
RA Wagner E., Goetz F., Brueckner R.;
RT "Cloning and characterization of the scrA gene encoding the sucrose-
RT specific Enzyme II of the phosphotransferase system from Staphylococcus
RT xylosus.";
RL Mol. Gen. Genet. 241:33-41(1993).
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 membrane {ECO:0000305}; Multi-pass membrane
CC 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; X69800; CAA49461.1; -; Genomic_DNA.
DR PIR; S39978; S39978.
DR RefSeq; WP_042362143.1; NZ_QXUG01000052.1.
DR AlphaFoldDB; P51184; -.
DR SMR; P51184; -.
DR STRING; 1288.SXYLSMQ121_0549; -.
DR GeneID; 45496183; -.
DR KEGG; sxl:SXYLSMQ121_0549; -.
DR KEGG; sxo:SXYL_00555; -.
DR eggNOG; COG1263; Bacteria.
DR eggNOG; COG1264; Bacteria.
DR OrthoDB; 196185at2; -.
DR BioCyc; MetaCyc:MON-12607; -.
DR BRENDA; 2.7.1.211; 5886.
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 Pfam; PF00367; PTS_EIIB; 1.
DR Pfam; PF02378; PTS_EIIC; 1.
DR SUPFAM; SSF55604; SSF55604; 1.
DR TIGRFAMs; TIGR00826; EIIB_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 membrane; Kinase; Membrane; Phosphotransferase system;
KW Sugar transport; Transferase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..480
FT /note="PTS system sucrose-specific EIIBC component"
FT /id="PRO_0000186671"
FT TRANSMEM 109..129
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 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 349..369
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 405..425
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 449..469
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..480
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 480 AA; 51326 MW; AB4E1D9785D84E47 CRC64;
MNYKKSAENI LQALGGEDNV EAMTHCATRL RLVLKDEGLV DEKALGDMDV VKGTFSTGGQ
YQVIIGSGTV NKVFSELEKI TGKEASSVSE VKTQGTKNMN PFQRFVKMLS DIFVPIIPAI
VAGGLLMGIN NILTAPGIFY DNQSLIEVQN QFSGLAEMIN IFANAPFTLL PILIGFSAAK
RFGGNAYLGA ALGMILVHPE LMSAYDYPKA LEAGKEIPHW NLFGLEINQV GYQGQVLPML
VATYILATIE KGLRKVIPTV LDNLLTPLLA ILSTGFITFS FVGPLTRTLG YWLSDGLTWL
YEFGGAIGGL IFGLLYAPIV ITGMHHSFIA IETQLIADSS STGGSFIFPI ATMSNIAQGA
AALAAFFIIK ENKKLKGVAS AAGVSALLGI TEPAMFGVNL KLRYPFIGAI VGSGIGSAYI
AFFKVKAIAL GTAGIPGFIS ISGQNNGWLH YGIAMIIAFI VAFGVTYALS YRKKYRNIEA
