ID   PTF3A_BACSU             Reviewed;         635 AA.
AC   P71012; Q7BVR6;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 2.
DT   02-SEP-2026, entry version 154.
DE   RecName: Full=PTS system fructose-specific EIIABC component {ECO:0000250|UniProtKB:P47308};
DE   AltName: Full=EIIABC-Fru {ECO:0000250|UniProtKB:P47308};
DE   Includes:
DE     RecName: Full=PTS system fructose-specific EIIA component {ECO:0000250|UniProtKB:P47308};
DE     AltName: Full=EII-Fru {ECO:0000250|UniProtKB:P47308};
DE     AltName: Full=Fructose-specific phosphotransferase enzyme IIA component {ECO:0000250|UniProtKB:P47308};
DE   Includes:
DE     RecName: Full=PTS system fructose-specific EIIB component {ECO:0000250|UniProtKB:P47308};
DE              EC=2.7.1.202 {ECO:0000250|UniProtKB:P20966};
DE     AltName: Full=EIII-Fru {ECO:0000250|UniProtKB:P47308};
DE     AltName: Full=Fructose-specific phosphotransferase enzyme IIB component {ECO:0000250|UniProtKB:P47308};
DE   Includes:
DE     RecName: Full=PTS system fructose-specific EIIC component {ECO:0000250|UniProtKB:P47308};
DE     AltName: Full=Fructose permease IIC component {ECO:0000250|UniProtKB:P47308};
GN   Name=fruA; OrderedLocusNames=BSU14400;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae;
OC   Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RA   Caldwell R.M., Ferrari E.;
RT   "Sequence analysis of the mobA-ampS region of the Bacillus subtilis
RT   chromosome.";
RL   Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 171-273.
RG   Midwest center for structural genomics (MCSG);
RT   "The structure of a domain of fruA from Bacillus subtilis.";
RL   Submitted (SEP-2007) to the PDB data bank.
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 fructose transport.
CC       {ECO:0000250|UniProtKB:P20966, ECO:0000250|UniProtKB:P47308}.
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:0000250|UniProtKB:P20966};
CC   -!- INTERACTION:
CC       P71012; O34755: ykoT; NbExp=3; IntAct=EBI-5242378, EBI-5242987;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00427}; Multi-pass membrane protein {ECO:0000255|PROSITE-
CC       ProRule:PRU00427}.
CC   -!- DOMAIN: The PTS EIIA type-2 domain is phosphorylated by phospho-HPr on
CC       a histidyl residue. Then, it transfers the phosphoryl group to the PTS
CC       EIIB type-2 domain. {ECO:0000255|PROSITE-ProRule:PRU00417}.
CC   -!- DOMAIN: The PTS EIIB type-2 domain is phosphorylated by phospho-EIIA on
CC       a cysteinyl residue. Then, it transfers the phosphoryl group to the
CC       sugar substrate concomitantly with the sugar uptake processed by the
CC       PTS EIIC type-2 domain. {ECO:0000255|PROSITE-ProRule:PRU00422}.
CC   -!- DOMAIN: The EIIC type-2 domain forms the PTS system translocation
CC       channel and contains the specific substrate-binding site.
CC       {ECO:0000255|PROSITE-ProRule:PRU00427}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF012285; AAC24915.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13313.1; -; Genomic_DNA.
DR   PIR; H69626; H69626.
DR   RefSeq; NP_389323.1; NC_000964.3.
DR   RefSeq; WP_003232350.1; NC_000964.3.
DR   PDB; 2R4Q; X-ray; 1.60 A; A=171-273.
DR   AlphaFoldDB; P71012; -.
DR   SMR; P71012; -.
DR   FunCoup; P71012; 69.
DR   IntAct; P71012; 39.
DR   STRING; 224308.BSU14400; -.
DR   TCDB; 4.A.2.1.4; the pts fructose-mannitol (fru) family.
DR   jPOST; P71012; -.
DR   PaxDb; 224308-BSU14400; -.
DR   DNASU; 938757; -.
DR   EnsemblBacteria; CAB13313; CAB13313; BSU_14400.
DR   GeneID; 938757; -.
DR   KEGG; bsu:BSU14400; -.
DR   PATRIC; fig|224308.179.peg.1570; -.
DR   eggNOG; COG1299; Bacteria.
DR   eggNOG; COG1445; Bacteria.
DR   eggNOG; COG1762; Bacteria.
DR   InParanoid; P71012; -.
DR   OrthoDB; 9782569at2; -.
DR   PhylomeDB; P71012; -.
DR   BioCyc; BSUB:BSU14400-MONOMER; -.
DR   EvolutionaryTrace; P71012; -.
DR   Proteomes; UP000001570; Chromosome.
DR   AbasyAtlas; P71012; -.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005351; F:carbohydrate:proton symporter activity; IEA:InterPro.
DR   GO; GO:0022877; F:protein-N(PI)-phosphohistidine-fructose phosphotransferase system transporter activity; IEA:InterPro.
DR   GO; GO:0090563; F:protein-phosphocysteine-sugar phosphotransferase activity; IBA:GO_Central.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IBA:GO_Central.
DR   CDD; cd00211; PTS_IIA_fru; 1.
DR   CDD; cd05569; PTS_IIB_fructose; 1.
DR   FunFam; 3.40.50.2300:FF:000014; PTS system fructose-like transporter subunit IIB; 1.
DR   FunFam; 3.40.930.10:FF:000009; PTS system, fructose specific IIABC component; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.40.930.10; Mannitol-specific EII, Chain A; 1.
DR   InterPro; IPR050864; Bacterial_PTS_Sugar_Transport.
DR   InterPro; IPR016152; PTrfase/Anion_transptr.
DR   InterPro; IPR002178; PTS_EIIA_type-2_dom.
DR   InterPro; IPR036095; PTS_EIIB-like_sf.
DR   InterPro; IPR013011; PTS_EIIB_2.
DR   InterPro; IPR003501; PTS_EIIB_2/3.
DR   InterPro; IPR003352; PTS_EIIC.
DR   InterPro; IPR013014; PTS_EIIC_2.
DR   InterPro; IPR004715; PTS_IIA_fruc.
DR   InterPro; IPR003353; PTS_IIB_fruc.
DR   InterPro; IPR006327; PTS_IIC_fruc.
DR   NCBIfam; TIGR00829; FRU; 1.
DR   NCBIfam; TIGR00848; fruA; 1.
DR   NCBIfam; TIGR01427; PTS_IIC_fructo; 1.
DR   PANTHER; PTHR30505; FRUCTOSE-LIKE PERMEASE; 1.
DR   PANTHER; PTHR30505:SF28; PTS SYSTEM 2-O-ALPHA-MANNOSYL-D-GLYCERATE-SPECIFIC EIIABC COMPONENT; 1.
DR   Pfam; PF00359; PTS_EIIA_2; 1.
DR   Pfam; PF02378; PTS_EIIC; 1.
DR   Pfam; PF02302; PTS_IIB; 1.
DR   SUPFAM; SSF55804; Phoshotransferase/anion transport protein; 1.
DR   SUPFAM; SSF52794; PTS system IIB component-like; 1.
DR   PROSITE; PS51094; PTS_EIIA_TYPE_2; 1.
DR   PROSITE; PS00372; PTS_EIIA_TYPE_2_HIS; 1.
DR   PROSITE; PS51099; PTS_EIIB_TYPE_2; 1.
DR   PROSITE; PS51104; PTS_EIIC_TYPE_2; 1.
DR   PDBsum; 2R4Q; -.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Membrane; Phosphoprotein;
KW   Phosphotransferase system; Reference proteome; Sugar transport;
KW   Transferase; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..635
FT                   /note="PTS system fructose-specific EIIABC component"
FT                   /id="PRO_0000360665"
FT   TRANSMEM        312..332
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT   TRANSMEM        350..370
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT   TRANSMEM        392..412
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT   TRANSMEM        428..448
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT   TRANSMEM        470..490
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT   TRANSMEM        511..531
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT   TRANSMEM        544..564
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT   TRANSMEM        569..589
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT   TRANSMEM        608..628
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT   DOMAIN          5..149
FT                   /note="PTS EIIA type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00417"
FT   DOMAIN          172..267
FT                   /note="PTS EIIB type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00422"
FT   DOMAIN          301..635
FT                   /note="PTS EIIC type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT   REGION          149..168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          273..293
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        152..162
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        67
FT                   /note="Tele-phosphohistidine intermediate; for EIIA
FT                   activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00417"
FT   ACT_SITE        178
FT                   /note="Phosphocysteine intermediate; for EIIB activity"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         67
FT                   /note="Phosphohistidine; by HPr"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         178
FT                   /note="Phosphocysteine; by EIIA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00422"
FT   STRAND          172..177
FT                   /evidence="ECO:0007829|PDB:2R4Q"
FT   HELIX           185..199
FT                   /evidence="ECO:0007829|PDB:2R4Q"
FT   STRAND          203..209
FT                   /evidence="ECO:0007829|PDB:2R4Q"
FT   STRAND          212..215
FT                   /evidence="ECO:0007829|PDB:2R4Q"
FT   HELIX           216..218
FT                   /evidence="ECO:0007829|PDB:2R4Q"
FT   HELIX           219..224
FT                   /evidence="ECO:0007829|PDB:2R4Q"
FT   STRAND          228..234
FT                   /evidence="ECO:0007829|PDB:2R4Q"
FT   HELIX           239..241
FT                   /evidence="ECO:0007829|PDB:2R4Q"
FT   STRAND          244..249
FT                   /evidence="ECO:0007829|PDB:2R4Q"
FT   HELIX           251..256
FT                   /evidence="ECO:0007829|PDB:2R4Q"
FT   HELIX           258..266
FT                   /evidence="ECO:0007829|PDB:2R4Q"
SQ   SEQUENCE   635 AA;  67184 MW;  753F12C2AFDD7F84 CRC64;
     MKITELLTKH TIKLNIESKE KENVIDEMVT VLDKAGKLND RQAYKEAILN RESQSSTGIG
     EGIAIPHAKT ASVINPAIAF GRSKDGVDYE SLDGQPAHLV FMIAATEGAN NTHLEALSRL
     STLLMREEIR KQLLEAESED AIIDIINQHD KDDDEEEEEE EAAPAPAGKG KILAVTACPT
     GIAHTFMAAD ALKEKAKELG VEIKVETNGS SGIKHKLTAQ EIEDAPAIIV AADKQVEMER
     FKGKRVLQVP VTAGIRRPQE LIEKAMNQDA PIYQGSGGGS AASNDDEEAK GKSGSGIGNT
     FYKHLMSGVS NMLPFVVGGG ILVAISFFWG IHSADPNDPS YNTFAAALNF IGGDNALKLI
     VAVLAGFIAM SIADRPGFAP GMVGGFMATQ ANAGFLGGLI AGFLAGYVVI LLKKVFTFIP
     QSLDGLKPVL IYPLFGIFIT GVLMQFVVNT PVAAFMNFLT NWLESLGTGN LVLMGIILGG
     MMAIDMGGPL NKAAFTFGIA MIDAGNYAPH AAIMAGGMVP PLGIALATTI FRNKFTQRDR
     EAGITCYFMG AAFVTEGAIP FAAADPLRVI PAAVVGAAVA GGLTEFFRVT LPAPHGGVFV
     AFITNHPMLY LLSIVIGAVV MAIILGIVKK PVTEK
//