ID   PTV3B_DICCH             Reviewed;         631 AA.
AC   P26207;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=PTS system beta-glucoside-specific EIIBCA component;
DE   AltName: Full=EIIBCA-Bgl;
DE            Short=EII-Bgl;
DE   Includes:
DE     RecName: Full=Beta-glucoside-specific phosphotransferase enzyme IIB component;
DE              EC=2.7.1.-;
DE     AltName: Full=PTS system beta-glucoside-specific EIIB component;
DE   Includes:
DE     RecName: Full=Beta-glucoside permease IIC component;
DE     AltName: Full=PTS system beta-glucoside-specific EIIC component;
DE   Includes:
DE     RecName: Full=Beta-glucoside-specific phosphotransferase enzyme IIA component;
DE     AltName: Full=PTS system beta-glucoside-specific EIIA component;
GN   Name=arbF;
OS   Dickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Dickeya.
OX   NCBI_TaxID=556;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1732212; DOI=10.1128/jb.174.3.765-777.1992;
RA   el Hassouni M., Henrissat B., Chippaux M., Barras F.;
RT   "Nucleotide sequences of the arb genes, which control beta-glucoside
RT   utilization in Erwinia chrysanthemi: comparison with the Escherichia coli
RT   bgl operon and evidence for a new beta-glycohydrolase family including
RT   enzymes from eubacteria, archeabacteria, and humans.";
RL   J. Bacteriol. 174:765-777(1992).
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 beta-glucoside transport.
CC   -!- FUNCTION: Acts as both a kinase and a phosphatase on ArbG.
CC       {ECO:0000250}.
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.
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; M81772; AAA24814.1; -; Genomic_DNA.
DR   PIR; B42603; B42603.
DR   AlphaFoldDB; P26207; -.
DR   SMR; P26207; -.
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; IPR011297; PTS_IIABC_b_glu.
DR   InterPro; IPR001996; PTS_IIB_1.
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; TIGR00830; PTBA; 1.
DR   TIGRFAMs; TIGR01995; PTS-II-ABC-beta; 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   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Kinase; Membrane;
KW   Phosphotransferase system; Sugar transport; Transferase; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..631
FT                   /note="PTS system beta-glucoside-specific EIIBCA component"
FT                   /id="PRO_0000186482"
FT   TRANSMEM        120..140
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        146..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        175..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        206..226
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        248..268
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        295..315
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        328..348
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        358..378
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        385..405
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        434..454
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          105..466
FT                   /note="PTS EIIC type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   DOMAIN          501..605
FT                   /note="PTS EIIA type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00416"
FT   ACT_SITE        26
FT                   /note="Phosphocysteine intermediate; for EIIB activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
FT   ACT_SITE        553
FT                   /note="Tele-phosphohistidine intermediate; for EIIA
FT                   activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00416"
SQ   SEQUENCE   631 AA;  66985 MW;  7D0BD27A36BFFFDF CRC64;
     MNYETLASEI RDGVGGQENI ISVIHCATRL RFKLRDNTNA NADALKNNPG IIMVVESGGQ
     FQVVVGNQVA DVYQALLSLD GMARFSDSAA PEEEKKNSLF SGFIDIISSI FTPFVGVMAA
     TGILKGFLAL GVATHVISES SGTYKLLFAA SDALFYFFPI VLGYTAGKKF GGNPFTTLVI
     GATLVHPSMI AAFNAMQAPD HSTLHFLGIP ITFINYSSSV IPILFASWVS CKLEKPLNRW
     LHANIRNFFT PLLCIVISVP LTFLLIGPSA TWLSQMLAGG YQWLYGLNSL LAGAVMGALW
     QVCVIFGLHW GFVPLMLNNF SVIGHDTLLP LLVPAVLGQA GATLGVLLRT QDLKRKGIAG
     SAFSAAIFGI TEPAVYGVTL PLRRPFIFGC IGGALGAAVM GYAHTTMYSF GFPSIFSFTQ
     VIPPTGVDSS VWAAVIGTLL AFAFAALTSW SFGVPKDETQ PAAADSPAVL AETQANAGAV
     RDETLFSPLA GEVLLLEQVA DRTFASGVMG KGIAIRPTQG RLYAPVDGTV ASLFKTHHAI
     GLASRGGAEV LIHVGIDTVR LDGRYFTPHV RVGDVVRQGD LLLEFDGPAI EAAGYDLTTP
     IVITNSEDYR GVEPVASGKV DANAPLTQLV C