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Database: UniProt
Entry: P36672
LinkDB: P36672
Original site: P36672 
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   03-SEP-2014, entry version 131.
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 277:1453-1462(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_000913.3.
DR   RefSeq; YP_492380.1; NC_007779.1.
DR   ProteinModelPortal; P36672; -.
DR   SMR; P36672; 11-92.
DR   IntAct; P36672; 1.
DR   MINT; MINT-6478335; -.
DR   STRING; 511145.b4240; -.
DR   TCDB; 4.A.1.2.4; the 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; VIGDIKM; -.
DR   OrthoDB; EOG6ND0GQ; -.
DR   PhylomeDB; P36672; -.
DR   BioCyc; EcoCyc:TREB-MONOMER; -.
DR   BioCyc; ECOL316407:JW4199-MONOMER; -.
DR   BioCyc; MetaCyc:TREB-MONOMER; -.
DR   PRO; PR:P36672; -.
DR   Genevestigator; P36672; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0022879; F:protein-N(PI)-phosphohistidine-trehalose phosphotransferase system transporter activity; IDA:EcoCyc.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IDA:EcoCyc.
DR   GO; GO:0015771; P:trehalose transport; IDA:EcoCyc.
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; IPR011296; PTS_IIBC_treh.
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; 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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