PTTBC_BACSU
ID PTTBC_BACSU Reviewed; 470 AA.
AC P39794; O34771;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 3.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=PTS system trehalose-specific EIIBC component {ECO:0000303|PubMed:8917076};
DE AltName: Full=EIIBC-Tre {ECO:0000303|PubMed:8917076};
DE Short=EII-Tre {ECO:0000303|PubMed:8917076};
DE Includes:
DE RecName: Full=Trehalose-specific phosphotransferase enzyme IIB component {ECO:0000303|PubMed:8917076};
DE EC=2.7.1.201 {ECO:0000250|UniProtKB:P36672};
DE AltName: Full=PTS system trehalose-specific EIIB component {ECO:0000303|PubMed:8917076};
DE Includes:
DE RecName: Full=Trehalose permease IIC component {ECO:0000303|PubMed:8917076};
DE AltName: Full=PTS system trehalose-specific EIIC component {ECO:0000303|PubMed:8917076};
GN Name=treP; Synonyms=treB; OrderedLocusNames=BSU07800;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=8917076; DOI=10.1016/0378-1119(96)00120-5;
RA Schoeck F., Dahl M.K.;
RT "Analysis of DNA flanking the treA gene of Bacillus subtilis reveals genes
RT encoding a putative specific enzyme IITre and a potential regulator of the
RT trehalose operon.";
RL Gene 175:59-63(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / AC327;
RX PubMed=8969503; DOI=10.1099/13500872-142-11-3057;
RA Yamamoto H., Uchiyama S., Sekiguchi J.;
RT "Cloning and sequencing of a 40.6 kb segment in the 73 degrees-76 degrees
RT region of the Bacillus subtilis chromosome containing genes for trehalose
RT metabolism and acetoin utilization.";
RL Microbiology 142:3057-3065(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / AC327;
RX PubMed=9272861; DOI=10.1016/s0378-1119(97)00130-3;
RA Yamamoto H., Uchiyama S., Nugroho F.A., Sekiguchi J.;
RT "Cloning and sequencing of a 35.7 kb in the 70 degree-73 degree region of
RT the Bacillus subtilis genome reveal genes for a new two-component system,
RT three spore germination proteins, an iron uptake system and a general
RT stress response protein.";
RL Gene 194:191-199(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 324-470.
RC STRAIN=168;
RX PubMed=7651129; DOI=10.1111/j.1365-2958.1995.tb02396.x;
RA Helfert C., Gotsche S., Dahl M.K.;
RT "Cleavage of trehalose-phosphate in Bacillus subtilis is catalysed by a
RT phospho-alpha-(1-1)-glucosidase encoded by the treA gene.";
RL Mol. Microbiol. 16:111-120(1995).
RN [6]
RP INDUCTION.
RX PubMed=8755887; DOI=10.1128/jb.178.15.4576-4581.1996;
RA Schoeck F., Dahl M.K.;
RT "Expression of the tre operon of Bacillus subtilis 168 is regulated by the
RT repressor TreR.";
RL J. Bacteriol. 178:4576-4581(1996).
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.
CC {ECO:0000250|UniProtKB:P36672, ECO:0000305|PubMed:8917076}.
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:0000250|UniProtKB:P36672};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00426}; Multi-pass membrane protein {ECO:0000255|PROSITE-
CC ProRule:PRU00426}.
CC -!- INDUCTION: Induced by trehalose-6-phosphate. Repressed by TreR.
CC {ECO:0000269|PubMed:8755887}.
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.
CC {ECO:0000250|UniProtKB:P36672, ECO:0000255|PROSITE-ProRule:PRU00421}.
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: B.subtilis 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:0000250|UniProtKB:P36672, ECO:0000305}.
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DR EMBL; Z54245; CAA91014.1; -; Genomic_DNA.
DR EMBL; D83967; BAA23409.1; -; Genomic_DNA.
DR EMBL; D86417; BAA22289.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12609.1; -; Genomic_DNA.
DR EMBL; X80203; CAA56494.1; -; Genomic_DNA.
DR PIR; C69725; C69725.
DR RefSeq; NP_388661.1; NC_000964.3.
DR RefSeq; WP_003233682.1; NZ_JNCM01000032.1.
DR AlphaFoldDB; P39794; -.
DR SMR; P39794; -.
DR IntAct; P39794; 1.
DR STRING; 224308.BSU07800; -.
DR TCDB; 4.A.1.2.8; the pts glucose-glucoside (glc) family.
DR jPOST; P39794; -.
DR PaxDb; P39794; -.
DR PRIDE; P39794; -.
DR EnsemblBacteria; CAB12609; CAB12609; BSU_07800.
DR GeneID; 939188; -.
DR KEGG; bsu:BSU07800; -.
DR PATRIC; fig|224308.179.peg.844; -.
DR eggNOG; COG1263; Bacteria.
DR eggNOG; COG1264; Bacteria.
DR InParanoid; P39794; -.
DR OMA; VVTGMHH; -.
DR PhylomeDB; P39794; -.
DR BioCyc; BSUB:BSU07800-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0015574; F:trehalose transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0015771; P:trehalose transport; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Cell membrane; Kinase; Membrane; Phosphoprotein; Phosphotransferase system;
KW Reference proteome; Sugar transport; Transferase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..470
FT /note="PTS system trehalose-specific EIIBC component"
FT /id="PRO_0000186678"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 301..321
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 326..346
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 347..367
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 443..463
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT DOMAIN 1..88
FT /note="PTS EIIB type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
FT DOMAIN 108..470
FT /note="PTS EIIC type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT ACT_SITE 27
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
FT MOD_RES 27
FT /note="Phosphocysteine; by EIIA"
FT /evidence="ECO:0000250|UniProtKB:P36672, ECO:0000305"
FT CONFLICT 140
FT /note="F -> S (in Ref. 1; CAA91014)"
FT /evidence="ECO:0000305"
FT CONFLICT 363
FT /note="M -> L (in Ref. 1; CAA91014 and 5; CAA56494)"
FT /evidence="ECO:0000305"
FT CONFLICT 465
FT /note="A -> G (in Ref. 1; CAA91014 and 5; CAA56494)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 470 AA; 50000 MW; 7A741850A2697D53 CRC64;
MGELNKSARQ IVEAVGGAEN IAAATHCVTR LRFALIDESK VDQEMLDQID VVKGSFSTNG
QFQVVIGQGT VNKVYAELVK ETGIGESTKD EVKKASEKNM NPLQRAVKTL ADIFIPILPA
IVTAGLLMGI NNILTAEGIF FSTKSIVQVY PQWADLANMI NLIAGTAFTF LPALIGWSAV
KRFGGNPLLG IVLGVMLVHP DLLNAWGYGA AEQSGEIPVW NLFGLEVQKV GYQGQVLPIL
LASYMLAKIE VFLTKRTPEG IQLLVVAPIT LLLTGFASFI IIGPITFAIG NVLTSGLISV
FGSFAALGGL LYGGFYSALV ITGMHHTFLA VDLQLIGSKL GGTFLWPMLA LSNIAQGSAA
LAMMFIVKDE KQKGLSLTSG ISAYLGITEP AIFGVNLRYR FPFIIAMVSS GLAGMYISSQ
GVLASSVGVG GVPGIFSIMS QYWGAFAIGM AIVLIVPFAG TYAYARFKHK
