PTFA_BACSU
ID PTFA_BACSU Reviewed; 146 AA.
AC P26379;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=PTS system fructose-specific EIIA component {ECO:0000303|PubMed:2117666};
DE AltName: Full=EIIA-Fru {ECO:0000303|PubMed:2117666};
DE AltName: Full=Fructose-specific phosphotransferase enzyme IIA component {ECO:0000303|PubMed:2117666};
DE AltName: Full=lev-PTS {ECO:0000303|PubMed:2117666};
DE AltName: Full=p16 {ECO:0000303|PubMed:2117666};
GN Name=levD {ECO:0000303|PubMed:2117666}; Synonyms=sacL;
GN OrderedLocusNames=BSU27070;
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-9, ACTIVE SITE, AND
RP PHOSPHORYLATION AT HIS-9.
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).
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 -!- 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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:2117666}.
CC -!- INDUCTION: By fructose and LevR. {ECO:0000269|PubMed:2495266}.
CC -!- DOMAIN: The EIIA type-4 domain is phosphorylated by phospho-HPr on a
CC histidyl residue. Then, it transfers the phosphoryl group to the EIIB
CC type-4 domain. {ECO:0000255|PROSITE-ProRule:PRU00419}.
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DR EMBL; X56098; CAA39577.1; -; Genomic_DNA.
DR EMBL; X92868; CAA63461.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14649.1; -; Genomic_DNA.
DR PIR; S11398; S11398.
DR RefSeq; NP_390585.1; NC_000964.3.
DR RefSeq; WP_003246144.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P26379; -.
DR SMR; P26379; -.
DR STRING; 224308.BSU27070; -.
DR TCDB; 4.A.6.1.2; the pts mannose-fructose-sorbose (man) family.
DR iPTMnet; P26379; -.
DR PaxDb; P26379; -.
DR PRIDE; P26379; -.
DR EnsemblBacteria; CAB14649; CAB14649; BSU_27070.
DR GeneID; 936536; -.
DR KEGG; bsu:BSU27070; -.
DR PATRIC; fig|224308.179.peg.2940; -.
DR eggNOG; COG2893; Bacteria.
DR InParanoid; P26379; -.
DR OMA; RNITCAS; -.
DR PhylomeDB; P26379; -.
DR BioCyc; BSUB:BSU27070-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; 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; cd00006; PTS_IIA_man; 1.
DR Gene3D; 3.40.50.510; -; 1.
DR InterPro; IPR013789; PTS_EIIA_man.
DR InterPro; IPR004701; PTS_EIIA_man-typ.
DR InterPro; IPR036662; PTS_EIIA_man-typ_sf.
DR InterPro; IPR033887; PTS_IIA_man.
DR Pfam; PF03610; EIIA-man; 1.
DR SUPFAM; SSF53062; SSF53062; 1.
DR TIGRFAMs; TIGR00824; EIIA-man; 1.
DR PROSITE; PS51096; PTS_EIIA_TYPE_4; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Kinase; Phosphoprotein; Phosphotransferase system;
KW Reference proteome; Sugar transport; Transferase; Transport.
FT CHAIN 1..146
FT /note="PTS system fructose-specific EIIA component"
FT /id="PRO_0000186523"
FT DOMAIN 1..124
FT /note="PTS EIIA type-4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00419"
FT ACT_SITE 9
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00419,
FT ECO:0000269|PubMed:9033408"
FT MOD_RES 9
FT /note="Phosphohistidine; by HPr"
FT /evidence="ECO:0000269|PubMed:9033408"
FT MUTAGEN 9
FT /note="H->A: Phosphorylation is only slightly increased."
FT /evidence="ECO:0000269|PubMed:9033408"
SQ SEQUENCE 146 AA; 16257 MW; D2198A13D6EF1C9D CRC64;
MISVIISGHG DFPIALKESS GMIFGEENNL IAVPFFKGEG IQTLQEKYHQ ALKDIPEEHE
VLFLVDIFGG TPYNAAASFI AEDQRMDMAA GVNLPILLEV LSLREHLALK DLLNNLKAMS
QQSFQVCSEH LEKVKTANQD TREDEL
