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Database: UniProt
Entry: P39794
LinkDB: P39794
Original site: P39794 
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   05-OCT-2016, entry version 130.
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 /
RC   NCIMB 3610 / 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
RT   genes encoding a putative specific enzyme IITre and a potential
RT   regulator of the 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
RT   degrees region of the Bacillus subtilis chromosome containing genes
RT   for trehalose 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
RT   of the Bacillus subtilis genome reveal genes for a new two-component
RT   system, three spore germination proteins, an iron uptake system and a
RT   general 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.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   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.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   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
RT   a phospho-alpha-(1-1)-glucosidase encoded by the treA gene.";
RL   Mol. Microbiol. 16:111-120(1995).
RN   [6]
RP   INDUCTION.
RX   PubMed=8755887;
RA   Schoeck F., Dahl M.K.;
RT   "Expression of the tre operon of Bacillus subtilis 168 is regulated by
RT   the repressor TreR.";
RL   J. Bacteriol. 178:4576-4581(1996).
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       {ECO:0000250|UniProtKB:P36672, ECO:0000305|PubMed:8917076}.
CC   -!- CATALYTIC ACTIVITY: [Protein]-N(pi)-phospho-L-histidine +
CC       alpha,alpha-trehalose(Side 1) = [protein]-L-histidine +
CC       alpha,alpha-trehalose 6-phosphate(Side 2).
CC       {ECO:0000250|UniProtKB:P36672}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00426}; Multi-pass membrane protein
CC       {ECO:0000255|PROSITE-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-
CC       EIIA-Glc (EIII-Glc) on a cysteinyl residue. Then, it transfers the
CC       phosphoryl group to the sugar substrate concomitantly with the
CC       sugar uptake processed by the PTS EIIC type-1 domain.
CC       {ECO:0000250|UniProtKB:P36672, ECO:0000255|PROSITE-
CC       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
CC       use the glucose-specific phosphotransferase enzyme IIA component
CC       to delivers trehalose-6-phosphate into the cell.
CC       {ECO:0000250|UniProtKB:P36672, ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 PTS EIIB type-1 domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00421}.
CC   -!- SIMILARITY: Contains 1 PTS EIIC type-1 domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00426}.
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   ProteinModelPortal; P39794; -.
DR   IntAct; P39794; 1.
DR   STRING; 224308.Bsubs1_010100004343; -.
DR   TCDB; 4.A.1.2.8; the pts glucose-glucoside (glc) family.
DR   PaxDb; P39794; -.
DR   PRIDE; P39794; -.
DR   EnsemblBacteria; CAB12609; CAB12609; BSU07800.
DR   GeneID; 939188; -.
DR   KEGG; bsu:BSU07800; -.
DR   PATRIC; 18973208; VBIBacSub10457_0818.
DR   eggNOG; ENOG4105C5Y; Bacteria.
DR   eggNOG; COG1263; LUCA.
DR   eggNOG; COG1264; LUCA.
DR   HOGENOM; HOG000102022; -.
DR   InParanoid; P39794; -.
DR   KO; K02818; -.
DR   KO; K02819; -.
DR   OMA; YKFPFVI; -.
DR   PhylomeDB; P39794; -.
DR   BioCyc; BSUB:BSU07800-MONOMER; -.
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: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:0043610; P:regulation of carbohydrate utilization; IBA:GO_Central.
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; 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; Complete proteome; Kinase; Membrane; Phosphoprotein;
KW   Phosphotransferase system; Reference proteome; Sugar transport;
KW   Transferase; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    470       PTS system trehalose-specific EIIBC
FT                                component.
FT                                /FTId=PRO_0000186678.
FT   TRANSMEM    110    130       Helical. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00426}.
FT   TRANSMEM    160    180       Helical. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00426}.
FT   TRANSMEM    183    203       Helical. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00426}.
FT   TRANSMEM    234    254       Helical. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00426}.
FT   TRANSMEM    263    283       Helical. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00426}.
FT   TRANSMEM    301    321       Helical. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00426}.
FT   TRANSMEM    326    346       Helical. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00426}.
FT   TRANSMEM    347    367       Helical. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00426}.
FT   TRANSMEM    403    423       Helical. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00426}.
FT   TRANSMEM    443    463       Helical. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00426}.
FT   DOMAIN        1     88       PTS EIIB type-1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00421}.
FT   DOMAIN      108    470       PTS EIIC type-1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00426}.
FT   ACT_SITE     27     27       Phosphocysteine intermediate; for EIIB
FT                                activity. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00421}.
FT   MOD_RES      27     27       Phosphocysteine; by EIIA.
FT                                {ECO:0000250|UniProtKB:P36672,
FT                                ECO:0000305}.
FT   CONFLICT    140    140       F -> S (in Ref. 1; CAA91014).
FT                                {ECO:0000305}.
FT   CONFLICT    363    363       M -> L (in Ref. 1; CAA91014 and 5;
FT                                CAA56494). {ECO:0000305}.
FT   CONFLICT    465    465       A -> G (in Ref. 1; CAA91014 and 5;
FT                                CAA56494). {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
//
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