ID PTTBC_ECOLI Reviewed; 473 AA.
AC P36672; Q2M667;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 4.
DT 29-MAY-2013, entry version 119.
DE RecName: Full=PTS system trehalose-specific EIIBC component;
DE AltName: Full=EIIBC-Tre;
DE Short=EII-Tre;
DE Includes:
DE RecName: Full=Trehalose-specific phosphotransferase enzyme IIB component;
DE EC=2.7.1.69;
DE AltName: Full=PTS system trehalose-specific EIIB component;
DE Includes:
DE RecName: Full=Trehalose permease IIC component;
DE AltName: Full=PTS system trehalose-specific EIIC component;
GN Name=treB; OrderedLocusNames=b4240, JW4199;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=7608078;
RA Klein W., Horlacher R., Boos W.;
RT "Molecular analysis of treB encoding the Escherichia coli enzyme II
RT specific for trehalose.";
RL J. Bacteriol. 177:4043-4052(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.,
RA Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the
RT region from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION
RP TO 184-194.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA Mau B., Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1474(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains
RT MG1655 and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
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 trehalose transport.
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.
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
CC and contains the specific substrate-binding site.
CC -!- SIMILARITY: Contains 1 PTS EIIB type-1 domain.
CC -!- SIMILARITY: Contains 1 PTS EIIC type-1 domain.
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DR EMBL; U06195; AAC43381.1; -; Genomic_DNA.
DR EMBL; U14003; AAA97137.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77197.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78239.1; -; Genomic_DNA.
DR PIR; C65236; C65236.
DR RefSeq; NP_418661.1; NC_000913.2.
DR RefSeq; YP_492380.1; NC_007779.1.
DR ProteinModelPortal; P36672; -.
DR SMR; P36672; 11-92.
DR MINT; MINT-6478335; -.
DR STRING; 511145.b4240; -.
DR TCDB; 4.A.1.2.4; PTS glucose-glucoside (Glc) family.
DR PaxDb; P36672; -.
DR PRIDE; P36672; -.
DR EnsemblBacteria; AAC77197; AAC77197; b4240.
DR EnsemblBacteria; BAE78239; BAE78239; BAE78239.
DR GeneID; 12933715; -.
DR GeneID; 948761; -.
DR KEGG; ecj:Y75_p4125; -.
DR KEGG; eco:b4240; -.
DR PATRIC; 32124055; VBIEscCol129921_4372.
DR EchoBASE; EB2048; -.
DR EcoGene; EG12127; treB.
DR eggNOG; COG1263; -.
DR HOGENOM; HOG000102022; -.
DR KO; K02818; -.
DR KO; K02819; -.
DR OMA; QQVPEVW; -.
DR ProtClustDB; PRK11007; -.
DR BioCyc; EcoCyc:TREB-MONOMER; -.
DR BioCyc; ECOL316407:JW4199-MONOMER; -.
DR BioCyc; MetaCyc:TREB-MONOMER; -.
DR Genevestigator; P36672; -.
DR GO; GO:0016021; C:integral to 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:EC.
DR GO; GO:0005351; F:sugar:hydrogen symporter activity; IEA:InterPro.
DR GO; GO:0015574; F:trehalose transmembrane transporter 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; IPR011296; PTS_IIBC_treh.
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; TIGR01992; PTS-IIBC-Tre; 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 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Complete proteome; Kinase;
KW Membrane; Phosphotransferase system; Reference proteome;
KW Sugar transport; Transferase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1 473 PTS system trehalose-specific EIIBC
FT component.
FT /FTId=PRO_0000186677.
FT TOPO_DOM 1 110 Cytoplasmic (Potential).
FT TRANSMEM 111 131 Helical; (Potential).
FT TOPO_DOM 132 158 Periplasmic (Potential).
FT TRANSMEM 159 179 Helical; (Potential).
FT TOPO_DOM 180 187 Cytoplasmic (Potential).
FT TRANSMEM 188 208 Helical; (Potential).
FT TOPO_DOM 209 225 Periplasmic (Potential).
FT TRANSMEM 226 246 Helical; (Potential).
FT TOPO_DOM 247 258 Cytoplasmic (Potential).
FT TRANSMEM 259 279 Helical; (Potential).
FT TOPO_DOM 280 300 Periplasmic (Potential).
FT TRANSMEM 301 321 Helical; (Potential).
FT TOPO_DOM 322 340 Cytoplasmic (Potential).
FT TRANSMEM 341 361 Helical; (Potential).
FT TOPO_DOM 362 370 Periplasmic (Potential).
FT TRANSMEM 371 391 Helical; (Potential).
FT TOPO_DOM 392 398 Cytoplasmic (Potential).
FT TRANSMEM 399 419 Helical; (Potential).
FT TOPO_DOM 420 440 Periplasmic (Potential).
FT TRANSMEM 441 461 Helical; (Potential).
FT TOPO_DOM 462 473 Cytoplasmic (Potential).
FT DOMAIN 1 89 PTS EIIB type-1.
FT DOMAIN 109 473 PTS EIIC type-1.
FT ACT_SITE 29 29 Phosphocysteine intermediate; for EIIB
FT activity (By similarity).
FT CONFLICT 126 127 GL -> PF (in Ref. 1; AAC43381).
FT CONFLICT 184 194 GGTPILGIVLG -> AQRRSLVSCLA (in Ref. 2;
FT AAA97137).
FT CONFLICT 187 187 Missing (in Ref. 1; AAC43381).
FT CONFLICT 307 307 A -> Q (in Ref. 1; AAC43381).
FT CONFLICT 429 473 PGILSIQPSYWQVFALAMAIAIIIPIVLTSFIYQRKYRLGT
FT LDIV -> RNSLDSTELLAGVCAGNGYRHHHPDCTHLVYLS
FT AEIPPGHAGHCLIFFGAQLRSHSQE (in Ref. 1;
FT AAC43381).
SQ SEQUENCE 473 AA; 51081 MW; 7437F8822B624944 CRC64;
MMSKINQTDI DRLIELVGGR GNIATVSHCI TRLRFVLNQP ANARPKEIEQ LPMVKGCFTN
AGQFQVVIGT NVGDYYQALI ASTGQAQVDK EQVKKAARHN MKWHEQLISH FAVIFFPLLP
ALISGGLILG FRNVIGDLPM SNGQTLAQMY PSLQTIYDFL WLIGEAIFFY LPVGICWSAV
KKMGGTPILG IVLGVTLVSP QLMNAYLLGQ QLPEVWDFGM FSIAKVGYQA QVIPALLAGL
ALGVIETRLK RIVPDYLYLV VVPVCSLILA VFLAHALIGP FGRMIGDGVA FAVRHLMTGS
FAPIGAALFG FLYAPLVITG VHQTTLAIDL QMIQSMGGTP VWPLIALSNI AQGSAVIGII
ISSRKHNERE ISVPAAISAW LGVTEPAMYG INLKYRFPML CAMIGSGLAG LLCGLNGVMA
NGIGVGGLPG ILSIQPSYWQ VFALAMAIAI IIPIVLTSFI YQRKYRLGTL DIV
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