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Database: UniProt
Entry: O06900
LinkDB: O06900
Original site: O06900 
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-SEP-2014, entry version 96.
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=2.7.1.69;
DE     AltName: Full=PTS system alpha-glucoside-specific EIIB component;
GN   Name=malB;
OS   Fusobacterium mortiferum.
OC   Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae;
OC   Fusobacterium.
OX   NCBI_TaxID=850;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 25557 / CCUG 14475;
RX   PubMed=11882720;
RA   Pikis A., Immel S., Robrish S.A., Thompson J.;
RT   "Metabolism of sucrose and its five isomers by Fusobacterium
RT   mortiferum.";
RL   Microbiology 148:843-852(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 443-526.
RC   STRAIN=ATCC 25557 / CCUG 14475;
RX   PubMed=9209025;
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
CC       phosphotransferase system (sugar PTS), a major carbohydrate active
CC       -transport system, catalyzes the phosphorylation of incoming sugar
CC       substrates concomitantly with their translocation across the cell
CC       membrane. This system is involved in alpha-glucoside transport.
CC   -!- CATALYTIC ACTIVITY: Protein EIIB N(pi)-phospho-L-
CC       histidine/cysteine + sugar = protein EIIB + sugar phosphate.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (Probable).
CC   -!- DOMAIN: The EIIC domain forms the PTS system translocation channel
CC       and 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.
CC   -!- SIMILARITY: Contains 1 PTS EIIB type-1 domain.
CC   -!- SIMILARITY: Contains 1 PTS EIIC type-1 domain.
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DR   EMBL; U81185; AAB63014.2; -; Genomic_DNA.
DR   ProteinModelPortal; 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:UniProtKB-EC.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1360.60; -; 1.
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       PTS system alpha-glucoside-specific EIICB
FT                                component.
FT                                /FTId=PRO_0000186477.
FT   TRANSMEM     12     32       Helical; (Potential).
FT   TRANSMEM     59     79       Helical; (Potential).
FT   TRANSMEM     88    108       Helical; (Potential).
FT   TRANSMEM    132    152       Helical; (Potential).
FT   TRANSMEM    173    193       Helical; (Potential).
FT   TRANSMEM    200    220       Helical; (Potential).
FT   TRANSMEM    224    244       Helical; (Potential).
FT   TRANSMEM    274    294       Helical; (Potential).
FT   TRANSMEM    305    325       Helical; (Potential).
FT   TRANSMEM    330    350       Helical; (Potential).
FT   TRANSMEM    355    375       Helical; (Potential).
FT   TRANSMEM    381    401       Helical; (Potential).
FT   DOMAIN        1    417       PTS EIIC type-1.
FT   DOMAIN      447    526       PTS EIIB type-1.
FT   ACT_SITE    469    469       Phosphocysteine intermediate; for EIIB
FT                                activity (By similarity).
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
//
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