ID   PTS3B_PEDPE             Reviewed;         651 AA.
AC   P43470;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=PTS system sucrose-specific EIIBCA component;
DE   AltName: Full=EIIBCA-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;
DE   Includes:
DE     RecName: Full=Sucrose-specific phosphotransferase enzyme IIA component;
DE     AltName: Full=PTS system sucrose-specific EIIA component;
GN   Name=scrA;
OS   Pediococcus pentosaceus.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Pediococcus.
OX   NCBI_TaxID=1255;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=PPE1.0;
RA   Leenhouts K.K.J., Bolhuis A.A., Kok J.J., Venema G.G.;
RT   "The sucrose and raffinose operons of Pediococcus pentosaceus PPE1.0.";
RL   Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases.
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.
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; Z32771; CAA83668.1; -; Genomic_DNA.
DR   EMBL; L32093; AAA25567.1; -; Genomic_DNA.
DR   PIR; S44257; S44257.
DR   AlphaFoldDB; P43470; -.
DR   SMR; P43470; -.
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; 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; IPR010973; PTS_IIBC_sucr.
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; TIGR01996; PTS-II-BC-sucr; 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   4: Predicted;
KW   Cell membrane; Kinase; Membrane; Phosphotransferase system;
KW   Sugar transport; Transferase; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..651
FT                   /note="PTS system sucrose-specific EIIBCA component"
FT                   /id="PRO_0000186675"
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        204..224
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        226..246
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        404..424
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        444..464
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   DOMAIN          1..86
FT                   /note="PTS EIIB type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
FT   DOMAIN          121..481
FT                   /note="PTS EIIC type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   DOMAIN          510..614
FT                   /note="PTS EIIA type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00416"
FT   ACT_SITE        25
FT                   /note="Phosphocysteine intermediate; for EIIB activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
FT   ACT_SITE        562
FT                   /note="Tele-phosphohistidine intermediate; for EIIA
FT                   activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00416"
SQ   SEQUENCE   651 AA;  68455 MW;  C87BA09D550A77F8 CRC64;
     MNHQEVADRV LNAIGKNNIQ AAAHCATRLR LVIKDESKID QQALDDDADV KGTFETNGQY
     QIIIGPGDVD KVYDALIVKT GLKEVTPDDI KAVAAAGQNK NPLMDFLKVL SDIFIPIVPA
     LVAGGLLMAL NNVLTAEHLF MAKSVVEVYP GLKGIAEMIN AMASAPFTFL PILLGFSATK
     RFGGNPYLGA TMGMIMVLPS LVNGYSVATT MAAGKMVYWN VFGLHVAQAG YQGQVLPVLG
     VAFILATLEK FFHKHIKGAF DFTFTPMFAI VITGFLTFTI VGPVLRTVSD ALTNGLVGLY
     NSTGWIGMGI FGLLYSAIVI TGLHQTFPAI ETQLLANVAK TGGSFIFPVA SMANIGQGAA
     TLAIFFATKS QKQKALTSSA GVSALLGITE PAIFGVNLKM KFPFVFAAIA SGIASAFLGL
     FHVLSVAMGP ASVIGFISIA SKSIPAFMLS AVISFVVAFI PTFIYAKRTL GDDRDQVKSP
     APTSTVINVN DEIISAPVTG ASESLKQVND QVFSAEIMGK GAAIVPSSDQ VVAPADGVIT
     VTYDSHHAYG IKTTAGAEIL IHLGLDTVNL NGEHFTTNVQ KGDTVHQGDL LGTFDIAALK
     AANYDPTVML IVTNTANYAN VERLKVTNVQ AGEQLVALTA PAASSVAATT V