PTFB_BACSU
ID PTFB_BACSU Reviewed; 163 AA.
AC P26380;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=PTS system fructose-specific EIIB component {ECO:0000303|PubMed:2117666};
DE EC=2.7.1.202 {ECO:0000269|PubMed:9033408};
DE AltName: Full=EIIB-Fru {ECO:0000303|PubMed:2117666};
DE AltName: Full=Fructose-specific phosphotransferase enzyme IIB component {ECO:0000303|PubMed:2117666};
DE AltName: Full=lev-PTS {ECO:0000303|PubMed:2117666};
DE AltName: Full=p18 {ECO:0000303|PubMed:2117666};
GN Name=levE {ECO:0000303|PubMed:2117666}; Synonyms=sacL;
GN OrderedLocusNames=BSU27060;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=168;
RX PubMed=2117666; DOI=10.1016/0022-2836(90)90284-s;
RA Martin-Verstraete I., Debarbouille M., Klier A., Rapoport G.;
RT "Levanase operon of Bacillus subtilis includes a fructose-specific
RT phosphotransferase system regulating the expression of the operon.";
RL J. Mol. Biol. 214:657-671(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9141695; DOI=10.1099/00221287-143-4-1321;
RA Parro V., San Roman M., Galindo I., Purnelle B., Bolotin A., Sorokin A.,
RA Mellado R.P.;
RT "A 23911 bp region of the Bacillus subtilis genome comprising genes located
RT upstream and downstream of the lev operon.";
RL Microbiology 143:1321-1326(1997).
RN [3]
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 [4]
RP INDUCTION.
RX PubMed=2495266; DOI=10.1128/jb.171.4.1885-1892.1989;
RA Martin I., Debarbouille M., Klier A., Rapoport G.;
RT "Induction and metabolite regulation of levanase synthesis in Bacillus
RT subtilis.";
RL J. Bacteriol. 171:1885-1892(1989).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF HIS-15, PHOSPHORYLATION AT
RP HIS-15, AND ACTIVE SITE.
RX PubMed=9033408; DOI=10.1021/bi961813w;
RA Charrier V., Deutscher J., Galinier A., Martin-Verstraete I.;
RT "Protein phosphorylation chain of a Bacillus subtilis fructose-specific
RT phosphotransferase system and its participation in regulation of the
RT expression of the lev operon.";
RL Biochemistry 36:1163-1172(1997).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), FUNCTION, AND ACTIVE SITE.
RX PubMed=9551099; DOI=10.1006/jmbi.1997.1544;
RA Schauder S., Nunn R.S., Lanz R., Erni B., Schirmer T.;
RT "Crystal structure of the IIB subunit of a fructose permease (IIBLev) from
RT Bacillus subtilis.";
RL J. Mol. Biol. 276:591-602(1998).
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. The
CC enzyme II LevDE PTS system is involved in fructose transport.
CC {ECO:0000269|PubMed:9033408, ECO:0000305|PubMed:2117666,
CC ECO:0000305|PubMed:9551099}.
CC -!- FUNCTION: LevD and LevE act as negative regulators of the levanase
CC operon. They may be involved in a PTS-mediated phosphorylation of a
CC regulator. {ECO:0000269|PubMed:2117666}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-fructose(out) + N(pros)-phospho-L-histidyl-[protein] = D-
CC fructose 1-phosphate(in) + L-histidyl-[protein];
CC Xref=Rhea:RHEA:49252, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:9746,
CC ChEBI:CHEBI:29979, ChEBI:CHEBI:37721, ChEBI:CHEBI:58674,
CC ChEBI:CHEBI:64837; EC=2.7.1.202;
CC Evidence={ECO:0000269|PubMed:9033408};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:2117666}.
CC -!- INDUCTION: By fructose and LevR. {ECO:0000269|PubMed:2495266}.
CC -!- DOMAIN: The PTS EIIB type-4 domain is phosphorylated by phospho-EIIA on
CC a histidyl residue. Then, it transfers the phosphoryl group to the
CC sugar substrate concomitantly with the sugar uptake processed by the
CC PTS EIIC type-4 domain. {ECO:0000255|PROSITE-ProRule:PRU00424}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA63462.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB14648.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X56098; CAA39578.1; -; Genomic_DNA.
DR EMBL; X92868; CAA63462.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL009126; CAB14648.1; ALT_INIT; Genomic_DNA.
DR PIR; S11399; S11399.
DR RefSeq; NP_390584.1; NC_000964.3.
DR PDB; 1BLE; X-ray; 2.90 A; A=1-163.
DR PDBsum; 1BLE; -.
DR AlphaFoldDB; P26380; -.
DR SMR; P26380; -.
DR STRING; 224308.BSU27060; -.
DR TCDB; 4.A.6.1.2; the pts mannose-fructose-sorbose (man) family.
DR iPTMnet; P26380; -.
DR PaxDb; P26380; -.
DR PRIDE; P26380; -.
DR EnsemblBacteria; CAB14648; CAB14648; BSU_27060.
DR GeneID; 937078; -.
DR KEGG; bsu:BSU27060; -.
DR PATRIC; fig|224308.43.peg.2822; -.
DR eggNOG; COG3444; Bacteria.
DR InParanoid; P26380; -.
DR BioCyc; BSUB:BSU27060-MON; -.
DR EvolutionaryTrace; P26380; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; 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:InterPro.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00001; PTS_IIB_man; 1.
DR Gene3D; 3.40.35.10; -; 1.
DR InterPro; IPR004720; PTS_IIB_sorbose-sp.
DR InterPro; IPR036667; PTS_IIB_sorbose-sp_sf.
DR InterPro; IPR018455; PTS_IIB_sorbose-sp_subgr.
DR Pfam; PF03830; PTSIIB_sorb; 1.
DR SUPFAM; SSF52728; SSF52728; 1.
DR TIGRFAMs; TIGR00854; pts-sorbose; 1.
DR PROSITE; PS51101; PTS_EIIB_TYPE_4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Kinase; Phosphoprotein; Phosphotransferase system;
KW Reference proteome; Sugar transport; Transferase; Transport.
FT CHAIN 1..163
FT /note="PTS system fructose-specific EIIB component"
FT /id="PRO_0000186524"
FT DOMAIN 1..163
FT /note="PTS EIIB type-4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00424"
FT ACT_SITE 15
FT /note="Pros-phosphohistidine intermediate"
FT /evidence="ECO:0000269|PubMed:9033408,
FT ECO:0000305|PubMed:9551099"
FT MOD_RES 15
FT /note="Phosphohistidine; by EIIA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00424,
FT ECO:0000269|PubMed:9033408"
FT MUTAGEN 15
FT /note="H->A: Unable to be phosphorylated."
FT /evidence="ECO:0000269|PubMed:9033408"
FT STRAND 3..10
FT /evidence="ECO:0007829|PDB:1BLE"
FT HELIX 18..26
FT /evidence="ECO:0007829|PDB:1BLE"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:1BLE"
FT HELIX 36..40
FT /evidence="ECO:0007829|PDB:1BLE"
FT HELIX 42..49
FT /evidence="ECO:0007829|PDB:1BLE"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:1BLE"
FT HELIX 63..71
FT /evidence="ECO:0007829|PDB:1BLE"
FT TURN 74..77
FT /evidence="ECO:0007829|PDB:1BLE"
FT STRAND 79..87
FT /evidence="ECO:0007829|PDB:1BLE"
FT HELIX 88..94
FT /evidence="ECO:0007829|PDB:1BLE"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:1BLE"
FT STRAND 102..108
FT /evidence="ECO:0007829|PDB:1BLE"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:1BLE"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:1BLE"
FT HELIX 125..136
FT /evidence="ECO:0007829|PDB:1BLE"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:1BLE"
FT HELIX 154..159
FT /evidence="ECO:0007829|PDB:1BLE"
SQ SEQUENCE 163 AA; 18215 MW; F3C10058A8333177 CRC64;
MMNIVLARID DRFIHGQILT RWIKVHAADR IIVVSDDIAQ DEMRKTLILS VAPSNVKASA
VSVSKMAKAF HSPRYEGVTA MLLFENPSDI VSLIEAGVPI KTVNVGGMRF ENHRRQITKS
VSVTEQDIKA FETLSDKGVK LELRQLPSDA SEDFVQILRN VTK
