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 27-MAR-2024, entry version 147.
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; Bacillota; Bacilli; Bacillales; Bacillaceae; 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}.
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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; NZ_JNCM01000035.1.
DR PDB; 2R4Q; X-ray; 1.60 A; A=171-273.
DR PDBsum; 2R4Q; -.
DR AlphaFoldDB; P71012; -.
DR SMR; P71012; -.
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 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 Gene3D; 3.40.50.2300; -; 1.
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.
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 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 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
//
