ID   PTUCB_KLEPN             Reviewed;         540 AA.
AC   Q9AGA7;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=PTS system alpha-glucoside-specific EIICB component;
DE   Includes:
DE     RecName: Full=Alpha-glucoside permease IIC component;
DE     AltName: Full=PTS system alpha-glucoside-specific EIIC component;
DE   Includes:
DE     RecName: Full=Alpha-glucoside-specific phosphotransferase enzyme IIB component;
DE              EC=2.7.1.-;
DE     AltName: Full=PTS system alpha-glucoside-specific EIIB component;
GN   Name=aglA;
OS   Klebsiella pneumoniae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=573;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 23357 / A-11;
RX   PubMed=11473129; DOI=10.1074/jbc.m106504200;
RA   Thompson J., Robrish S.A., Immel S., Lichtenthaler F.W., Hall B.G.,
RA   Pikis A.;
RT   "Metabolism of sucrose and its five linkage-isomeric alpha-D-glucosyl-D-
RT   fructoses by Klebsiella pneumoniae. Participation and properties of
RT   sucrose-6-phosphate hydrolase and phospho-alpha-glucosidase.";
RL   J. Biol. Chem. 276:37415-37425(2001).
RN   [2]
RP   FUNCTION.
RC   STRAIN=ATCC 23357 / A-11;
RX   PubMed=11322729; DOI=10.1016/s0008-6215(01)00028-3;
RA   Thompson J., Robrish S.A., Pikis A., Brust A., Lichtenthaler F.W.;
RT   "Phosphorylation and metabolism of sucrose and its five linkage-isomeric
RT   alpha-D-glucosyl-D-fructoses by Klebsiella pneumoniae.";
RL   Carbohydr. Res. 331:149-161(2001).
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 alpha-glucoside transport.
CC       {ECO:0000269|PubMed:11322729}.
CC   -!- FUNCTION: Involved in the transport and simultaneous phosphorylation at
CC       O-6 of the glucosyl moiety of sucrose and its five linkage-isomeric
CC       alpha-D-glucosyl-D-fructoses. Can also transport maltose, isomaltose
CC       and maltitol, phosphorylating at O-6 of their non-reducing glucose
CC       portion. {ECO:0000269|PubMed:11322729}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- DOMAIN: The EIIC domain forms the PTS system translocation channel and
CC       contains the specific substrate-binding site.
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.
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DR   EMBL; AF337811; AAK01456.1; -; Genomic_DNA.
DR   RefSeq; WP_002923307.1; NZ_WYAM01000023.1.
DR   AlphaFoldDB; Q9AGA7; -.
DR   SMR; Q9AGA7; -.
DR   TCDB; 4.A.1.1.10; the pts glucose-glucoside (glc) family.
DR   OrthoDB; 2035550at2; -.
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; IPR010975; PTS_IIBC_a_glc.
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; TIGR02005; PTS-IIBC-alpha; 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..540
FT                   /note="PTS system alpha-glucoside-specific EIICB component"
FT                   /id="PRO_0000186478"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        87..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        130..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        174..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        201..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        225..245
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        277..297
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        307..327
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        352..372
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        384..404
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   DOMAIN          1..420
FT                   /note="PTS EIIC type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   DOMAIN          448..530
FT                   /note="PTS EIIB type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
FT   ACT_SITE        470
FT                   /note="Phosphocysteine intermediate; for EIIB activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
SQ   SEQUENCE   540 AA;  58373 MW;  538C20D65233D1D8 CRC64;
     MLSQIQRFGG AMFTPVLLFP FAGIVVGIAI MLRNPMFVGE ALTAPDSLFA QIVHIIEEGG
     WTVFRNMPLI FAVGLPIGLA KQAQGRACLA VLVSFLTWNY FINAMGMTWG HFFGVDFSAE
     PTAGSGLTMI AGIKTLDTSI IGAIVISGLV TALHNRYFDK PLPVFLGIFQ GSSFVVIVAF
     LAMIPCAWLT LLGWPKVQLG IESLQAFLRS AGALGVWVYI FLERILIPTG LHHFVYGPFI
     FGPAVVEGGL QVYWAEHLQA FSQSTEPLKT LFPEGGFALH GNSKVFGSVG IALALYFTAA
     PENRVKVAGL LIPATLTAML VGITEPLEFT FLFISPLLFA VHAVLAATMA TVMYICGVVG
     NFGGGLLDQF LPQNWIPMFH HHASMMFIQI GIGLCFTALY FVVFRTLILR LNLKTPGREE
     SEIKLYSKAD YQAARGKTTA AAAPETRLGQ AAGFLQALGG ADNIESINNC ATRLRIALVD
     MAKTQSDDVF KALGAHGVVR RGNGIQVIVG LHVPQVRDQL ENLMKDSLST EHTTMTEAVS