PTTBC_ECOLI
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-AUG-2022, entry version 174.
DE RecName: Full=PTS system trehalose-specific EIIBC component {ECO:0000303|PubMed:2160944};
DE AltName: Full=EIIBC-Tre {ECO:0000303|PubMed:2160944};
DE Short=EII-Tre {ECO:0000303|PubMed:2160944};
DE Includes:
DE RecName: Full=Trehalose-specific phosphotransferase enzyme IIB component {ECO:0000303|PubMed:2160944};
DE EC=2.7.1.201 {ECO:0000269|PubMed:2160944};
DE AltName: Full=PTS system trehalose-specific EIIB component {ECO:0000303|PubMed:2160944};
DE Includes:
DE RecName: Full=Trehalose permease IIC component {ECO:0000303|PubMed:2160944};
DE AltName: Full=PTS system trehalose-specific EIIC component {ECO:0000303|PubMed:2160944};
GN Name=treB; OrderedLocusNames=b4240, JW4199;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RC STRAIN=K12;
RX PubMed=7608078; DOI=10.1128/jb.177.14.4043-4052.1995;
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., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT 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 TO
RP 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., Mau B.,
RA 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 MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION,
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT CYS-29.
RX PubMed=2160944; DOI=10.1128/jb.172.6.3450-3461.1990;
RA Boos W., Ehmann U., Forkl H., Klein W., Rimmele M., Postma P.;
RT "Trehalose transport and metabolism in Escherichia coli.";
RL J. Bacteriol. 172:3450-3461(1990).
RN [6]
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 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 trehalose transport at low osmolarity.
CC {ECO:0000269|PubMed:2160944, ECO:0000305|PubMed:7608078}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha,alpha-trehalose(out) + N(pros)-phospho-L-histidyl-
CC [protein] = alpha,alpha-trehalose 6-phosphate(in) + L-histidyl-
CC [protein]; Xref=Rhea:RHEA:33371, Rhea:RHEA-COMP:9745, Rhea:RHEA-
CC COMP:9746, ChEBI:CHEBI:16551, ChEBI:CHEBI:29979, ChEBI:CHEBI:58429,
CC ChEBI:CHEBI:64837; EC=2.7.1.201;
CC Evidence={ECO:0000269|PubMed:2160944};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=16 uM for trehalose {ECO:0000269|PubMed:2160944};
CC Vmax=9 nmol/min/mg enzyme toward trehalose
CC {ECO:0000269|PubMed:2160944};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00426, ECO:0000305|PubMed:2160944}; Multi-pass membrane
CC protein {ECO:0000255|PROSITE-ProRule:PRU00426}.
CC -!- INDUCTION: At low osmolarity, treB is induced by trehalose-6-phosphate,
CC but it becomes uninducible at high osmolarity due to induction of
CC trehalose-6-phosphate phosphatase OstB which is part of the
CC biosynthetic pathway of trehalose synthesis at high osmolarity.
CC Repressed by TreR. {ECO:0000269|PubMed:2160944,
CC ECO:0000269|PubMed:7608078}.
CC -!- DOMAIN: The PTS EIIB type-1 domain is phosphorylated by phospho-EIIA-
CC Glc (EIII-Glc) on a cysteinyl residue. Then, it transfers the
CC phosphoryl group to the sugar substrate concomitantly with the sugar
CC uptake processed by the PTS EIIC type-1 domain. {ECO:0000255|PROSITE-
CC ProRule:PRU00421, ECO:0000305|PubMed:2160944}.
CC -!- DOMAIN: The EIIC domain type-1 forms the PTS system translocation
CC channel and contains the specific substrate-binding site.
CC {ECO:0000255|PROSITE-ProRule:PRU00426}.
CC -!- MISCELLANEOUS: E.coli does not possess a trehalose-specific
CC phosphotransferase enzyme IIA component, however it seems that it use
CC the glucose-specific phosphotransferase enzyme IIA component to
CC delivers trehalose-6-phosphate into the cell.
CC {ECO:0000305|PubMed:2160944}.
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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; WP_001407733.1; NZ_LN832404.1.
DR AlphaFoldDB; P36672; -.
DR SMR; P36672; -.
DR BioGRID; 4262709; 12.
DR IntAct; P36672; 1.
DR MINT; P36672; -.
DR STRING; 511145.b4240; -.
DR TCDB; 4.A.1.2.4; the pts glucose-glucoside (glc) family.
DR iPTMnet; P36672; -.
DR jPOST; P36672; -.
DR PaxDb; P36672; -.
DR PRIDE; P36672; -.
DR EnsemblBacteria; AAC77197; AAC77197; b4240.
DR EnsemblBacteria; BAE78239; BAE78239; BAE78239.
DR GeneID; 948761; -.
DR KEGG; ecj:JW4199; -.
DR KEGG; eco:b4240; -.
DR PATRIC; fig|1411691.4.peg.2461; -.
DR EchoBASE; EB2048; -.
DR eggNOG; COG1263; Bacteria.
DR eggNOG; COG1264; Bacteria.
DR HOGENOM; CLU_012312_2_1_6; -.
DR InParanoid; P36672; -.
DR OMA; PMGVWNF; -.
DR PhylomeDB; P36672; -.
DR BioCyc; EcoCyc:TREB-MON; -.
DR BioCyc; MetaCyc:TREB-MON; -.
DR BRENDA; 2.7.1.201; 2026.
DR SABIO-RK; P36672; -.
DR PRO; PR:P36672; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
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:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:InterPro.
DR GO; GO:0090563; F:protein-phosphocysteine-sugar phosphotransferase activity; IBA:GO_Central.
DR GO; GO:0090589; F:protein-phosphocysteine-trehalose phosphotransferase system transporter activity; IDA:EcoCyc.
DR GO; GO:0015574; F:trehalose transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IDA:EcoCyc.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0015771; P:trehalose transport; IDA:EcoCyc.
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; 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; Kinase; Membrane; Phosphoprotein;
KW Phosphotransferase system; Reference proteome; Sugar transport;
KW Transferase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..473
FT /note="PTS system trehalose-specific EIIBC component"
FT /id="PRO_0000186677"
FT TOPO_DOM 1..110
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 132..158
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 180..187
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 209..225
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 247..258
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 259..279
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 280..300
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 301..321
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 322..340
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 341..361
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 362..370
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 371..391
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 392..398
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 399..419
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 420..440
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 441..461
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 462..473
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 1..89
FT /note="PTS EIIB type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
FT DOMAIN 109..473
FT /note="PTS EIIC type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT ACT_SITE 29
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
FT MOD_RES 29
FT /note="Phosphocysteine; by EIIA"
FT /evidence="ECO:0000305|PubMed:2160944"
FT CONFLICT 126..127
FT /note="GL -> PF (in Ref. 1; AAC43381)"
FT /evidence="ECO:0000305"
FT CONFLICT 184..194
FT /note="GGTPILGIVLG -> AQRRSLVSCLA (in Ref. 2; AAA97137)"
FT /evidence="ECO:0000305"
FT CONFLICT 187
FT /note="Missing (in Ref. 1; AAC43381)"
FT /evidence="ECO:0000305"
FT CONFLICT 307
FT /note="A -> Q (in Ref. 1; AAC43381)"
FT /evidence="ECO:0000305"
FT CONFLICT 429..473
FT /note="PGILSIQPSYWQVFALAMAIAIIIPIVLTSFIYQRKYRLGTLDIV -> RNS
FT LDSTELLAGVCAGNGYRHHHPDCTHLVYLSAEIPPGHAGHCLIFFGAQLRSHSQE (in
FT Ref. 1; AAC43381)"
FT /evidence="ECO:0000305"
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
