ID PTGCB_ECOL6 Reviewed; 477 AA.
AC P69787; P05053;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 01-MAY-2013, entry version 64.
DE RecName: Full=PTS system glucose-specific EIICB component;
DE AltName: Full=EIICB-Glc;
DE Short=EII-Glc;
DE Includes:
DE RecName: Full=Glucose permease IIC component;
DE AltName: Full=PTS system glucose-specific EIIC component;
DE Includes:
DE RecName: Full=Glucose-specific phosphotransferase enzyme IIB component;
DE EC=2.7.1.69;
DE AltName: Full=PTS system glucose-specific EIIB component;
GN Name=ptsG; OrderedLocusNames=c1373;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P.,
RA Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D.,
RA Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T.,
RA Mobley H.L.T., Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence
RT of uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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 glucose transport. This
CC enzyme is also a chemoreceptor monitoring the environment for
CC changes in sugar concentration (By similarity).
CC -!- CATALYTIC ACTIVITY: Protein EIIB N(pi)-phospho-L-
CC histidine/cysteine + sugar = protein EIIB + sugar phosphate.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane
CC protein (By similarity).
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.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AE014075; AAN79843.1; -; Genomic_DNA.
DR RefSeq; NP_753283.1; NC_004431.1.
DR ProteinModelPortal; P69787; -.
DR SMR; P69787; 396-476.
DR STRING; 199310.c1373; -.
DR PRIDE; P69787; -.
DR EnsemblBacteria; AAN79843; AAN79843; c1373.
DR GeneID; 1035072; -.
DR KEGG; ecc:c1373; -.
DR PATRIC; 18280755; VBIEscCol75197_1302.
DR HOGENOM; HOG000250993; -.
DR KO; K02778; -.
DR KO; K02779; -.
DR OMA; FSDWAAH; -.
DR ProtClustDB; PRK11089; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005355; F:glucose transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:EC.
DR GO; GO:0005351; F:sugar:hydrogen symporter activity; IEA:InterPro.
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_phosph_CS.
DR InterPro; IPR004719; PTrfase_sys_maltose/Glc-sp_IIC.
DR InterPro; IPR001996; PTS_EIIB_1.
DR InterPro; IPR003352; PTS_EIIC.
DR InterPro; IPR013013; PTS_EIIC_1.
DR InterPro; IPR011535; PTS_Glc-like_IIB_component.
DR InterPro; IPR011299; PTS_IIBC_glc.
DR Pfam; PF00367; PTS_EIIB; 1.
DR Pfam; PF02378; PTS_EIIC; 1.
DR SUPFAM; SSF55604; PTS_EIIB; 1.
DR TIGRFAMs; TIGR00826; EIIB_glc; 1.
DR TIGRFAMs; TIGR00852; pts-Glc; 1.
DR TIGRFAMs; TIGR02002; PTS-II-BC-glcB; 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; Complete proteome; Kinase;
KW Membrane; Phosphotransferase system; Sugar transport; Transferase;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1 477 PTS system glucose-specific EIICB
FT component.
FT /FTId=PRO_0000186529.
FT TOPO_DOM 1 14 Cytoplasmic (Potential).
FT TRANSMEM 15 35 Helical; (Potential).
FT TOPO_DOM 36 50 Periplasmic (Potential).
FT TRANSMEM 51 71 Helical; (Potential).
FT TOPO_DOM 72 79 Cytoplasmic (Potential).
FT TRANSMEM 80 100 Helical; (Potential).
FT TOPO_DOM 101 111 Periplasmic (Potential).
FT TRANSMEM 112 132 Helical; (Potential).
FT TOPO_DOM 133 151 Cytoplasmic (Potential).
FT TRANSMEM 152 172 Helical; (Potential).
FT TOPO_DOM 173 190 Periplasmic (Potential).
FT TRANSMEM 191 211 Helical; (Potential).
FT TOPO_DOM 212 249 Cytoplasmic (Potential).
FT TRANSMEM 250 270 Helical; (Potential).
FT TOPO_DOM 271 279 Periplasmic (Potential).
FT TRANSMEM 280 300 Helical; (Potential).
FT TOPO_DOM 301 309 Cytoplasmic (Potential).
FT TRANSMEM 310 330 Helical; (Potential).
FT TOPO_DOM 331 355 Periplasmic (Potential).
FT TRANSMEM 356 376 Helical; (Potential).
FT TOPO_DOM 377 477 Cytoplasmic (Potential).
FT DOMAIN 1 388 PTS EIIC type-1.
FT DOMAIN 399 477 PTS EIIB type-1.
FT ACT_SITE 421 421 Phosphocysteine intermediate; for EIIB
FT activity (By similarity).
SQ SEQUENCE 477 AA; 50677 MW; D97A80FD64B74F73 CRC64;
MFKNAFANLQ KVGKSLMLPV SVLPIAGILL GVGSANFSWL PAVVSHVMAE AGGSVFANMP
LIFAIGVALG FTNNDGVSAL AAVVAYGIMV KTMAVVAPLV LHLPAEEIAS KHLADTGVLG
GIISGAIAAY MFNRFYRIKL PEYLGFFAGK RFVPIISGLA AIFTGVVLSF IWPPIGSAIQ
TFSQWAAYQN PVVAFGIYGF IERCLVPFGL HHIWNVPFQM QIGEYTNAAG QVFHGDIPRY
MAGDPTAGKL SGGFLFKMYG LPAAAIAIWH SAKPENRAKV GGIMISAALT SFLTGITEPI
EFSFMFVAPI LYIIHAILAG LAFPICILLG MRDGTSFSHG LIDFIVLSGN SSKLWLFPIV
GIGYAIVYYT IFRVLIKALD LKTPGREDAT EDAKATGTSE MAPALVAAFG GKENITNLDA
CITRLRVSVA DVSKVDQAGL KKLGAAGVVV AGSGVQAIFG TKSDNLKTEM DEYIRNH
//