PTUCB_FUSMR
ID PTUCB_FUSMR Reviewed; 526 AA.
AC O06900;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 116.
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=malB;
OS Fusobacterium mortiferum.
OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Fusobacterium.
OX NCBI_TaxID=850;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 25557 / DSM 19809 / CCUG 14475 / VPI 4123A;
RX PubMed=11882720; DOI=10.1099/00221287-148-3-843;
RA Pikis A., Immel S., Robrish S.A., Thompson J.;
RT "Metabolism of sucrose and its five isomers by Fusobacterium mortiferum.";
RL Microbiology 148:843-852(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 443-526.
RC STRAIN=ATCC 25557 / DSM 19809 / CCUG 14475 / VPI 4123A;
RX PubMed=9209025; DOI=10.1128/jb.179.13.4129-4137.1997;
RA Bouma C.L., Reizer J., Reizer A., Robrish S.A., Thompson J.;
RT "6-phospho-alpha-D-glucosidase from Fusobacterium mortiferum: cloning,
RT expression, and assignment to family 4 of the glycosylhydrolases.";
RL J. Bacteriol. 179:4129-4137(1997).
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 -!- 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; U81185; AAB63014.2; -; Genomic_DNA.
DR AlphaFoldDB; O06900; -.
DR SMR; O06900; -.
DR TCDB; 4.A.1.1.4; the pts glucose-glucoside (glc) family.
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 Pfam; PF00367; PTS_EIIB; 1.
DR Pfam; PF02378; PTS_EIIC; 1.
DR SUPFAM; SSF55604; SSF55604; 1.
DR TIGRFAMs; TIGR00826; EIIB_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..526
FT /note="PTS system alpha-glucoside-specific EIICB component"
FT /id="PRO_0000186477"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 355..375
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT DOMAIN 1..417
FT /note="PTS EIIC type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT DOMAIN 447..526
FT /note="PTS EIIB type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
FT ACT_SITE 469
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
SQ SEQUENCE 526 AA; 57313 MW; E5FDE7287202D84E CRC64;
MLKHFQRLGG ALFAPVLLFP FAGLVVALTI ILKNPDFVGE LANTNGTFYK MITVIEEGGW
TVFRQLPLIF AIGLPIGLAK KAHPRACLAV LATYLTYNYF ISAILTFWGP SFGVDFTQNV
GGVSGLTTIA GIKTLDTSIV GAIVISGITI YIHNKFFDTK LPDFLGTFQG TTLVSAIAFV
VMIPCAYITC LVWPKIQMGI SSLQALMVTS GTFGVWLYTF LERILIPTGL HHFIYGPFIF
GPAVVDTGIQ VAWAENLLNF ANSTQPLKEL FPQGGFALHG NSKIFGCIGI ALAMYKTARP
EKKKIVSGLL IPAALTAALV GITEPLEFTF LFIAPFLFVV HAVLAATMAA VMYAFGVVKY
GSGIIEIAAL NWLPLMKNHS GVMFTQLAIG VVFIGIHYLV FKFLIEKYNV KTSGREDEEE
ETKLYTKADW KAKNGEGKET NSSDLYSGKA KAFLEAFGGK DNIEQVNNCA TRLRISVKDE
KKVGPDIQFK AAGAHGVVRN GKAFQVIVGL SVPQVRESFE NLMEQN
