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 01-MAY-2013, entry version 108.
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=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].
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).
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 membrane; Multi-pass membrane protein
CC (Probable).
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; 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 ProteinModelPortal; P39794; -.
DR SMR; P39794; 2-93.
DR STRING; 224308.BSU07800; -.
DR TCDB; 4.A.1.2.8; PTS glucose-glucoside (Glc) family.
DR PaxDb; P39794; -.
DR EnsemblBacteria; CAB12609; CAB12609; BSU07800.
DR GeneID; 939188; -.
DR KEGG; bsu:BSU07800; -.
DR PATRIC; 18973208; VBIBacSub10457_0818.
DR GenoList; BSU07800; -.
DR eggNOG; COG1263; -.
DR HOGENOM; HOG000102022; -.
DR KO; K02818; -.
DR KO; K02819; -.
DR OMA; NIAAATH; -.
DR ProtClustDB; CLSK873252; -.
DR BioCyc; BSUB:BSU07800-MONOMER; -.
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 4: Predicted;
KW Cell membrane; Complete proteome; Kinase; Membrane;
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; (Potential).
FT TRANSMEM 160 180 Helical; (Potential).
FT TRANSMEM 183 203 Helical; (Potential).
FT TRANSMEM 234 254 Helical; (Potential).
FT TRANSMEM 263 283 Helical; (Potential).
FT TRANSMEM 301 321 Helical; (Potential).
FT TRANSMEM 326 346 Helical; (Potential).
FT TRANSMEM 347 367 Helical; (Potential).
FT TRANSMEM 403 423 Helical; (Potential).
FT TRANSMEM 443 463 Helical; (Potential).
FT DOMAIN 1 88 PTS EIIB type-1.
FT DOMAIN 108 470 PTS EIIC type-1.
FT ACT_SITE 26 26 Pros-phosphohistidine intermediate; for
FT EIIB activity (By similarity).
FT CONFLICT 140 140 F -> S (in Ref. 1; CAA91014).
FT CONFLICT 363 363 M -> L (in Ref. 1 and 5).
FT CONFLICT 465 465 A -> G (in Ref. 1 and 5).
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
//
