ID   PTFBC_XANCP             Reviewed;         580 AA.
AC   P23355;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2002, sequence version 2.
DT   02-SEP-2026, entry version 159.
DE   RecName: Full=PTS system fructose-specific EIIB'BC component {ECO:0000305|PubMed:1655739};
DE   AltName: Full=EIIB'BC-Fru {ECO:0000305|PubMed:1655739};
DE   Includes:
DE     RecName: Full=PTS system fructose-specific EIIB component {ECO:0000303|PubMed:1655739};
DE              EC=2.7.1.202 {ECO:0000250|UniProtKB:P20966};
DE     AltName: Full=EIII-Fru {ECO:0000250|UniProtKB:P20966};
DE     AltName: Full=Fructose-specific phosphotransferase enzyme IIB component {ECO:0000303|PubMed:1655739};
DE   Includes:
DE     RecName: Full=PTS system fructose-specific EIIC component {ECO:0000303|PubMed:1655739};
DE     AltName: Full=Fructose permease IIC component {ECO:0000303|PubMed:1655739};
GN   Name=fruA {ECO:0000303|PubMed:1655739}; OrderedLocusNames=XCC2372;
OS   Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS   528 / LMG 568 / P 25).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Lysobacterales; Lysobacteraceae; Xanthomonas.
OX   NCBI_TaxID=190485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, DOMAIN,
RP   AND ACTIVE SITE.
RC   STRAIN=ATCC 13951 / NCIB 11803 / NRRL B-1459;
RX   PubMed=1655739; DOI=10.1016/s0021-9258(18)55249-2;
RA   de Crecy-Lagard V., Bouvet O.M., Lejeune P., Danchin A.;
RT   "Fructose catabolism in Xanthomonas campestris pv. campestris. Sequence of
RT   the PTS operon, characterization of the fructose-specific enzymes.";
RL   J. Biol. Chem. 266:18154-18161(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX   PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA   Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA   Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA   Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA   Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA   Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA   Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA   Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA   Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA   Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA   Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA   Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA   Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT   specificities.";
RL   Nature 417:459-463(2002).
RN   [3]
RP   PROTEIN SEQUENCE OF 404-547, FUNCTION, AND INDUCTION.
RX   PubMed=1650911; DOI=10.1007/bf00273939;
RA   de Crecy-Lagard V., Lejeune P., Bouvet O.M., Danchin A.;
RT   "Identification of two fructose transport and phosphorylation pathways in
RT   Xanthomonas campestris pv. campestris.";
RL   Mol. Gen. Genet. 227:465-472(1991).
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 FruAB PTS system is involved in fructose transport.
CC       {ECO:0000250|UniProtKB:P20966, ECO:0000269|PubMed:1655739,
CC       ECO:0000305|PubMed:1650911}.
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   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:P20966, ECO:0000255|PROSITE-ProRule:PRU00427};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:P20966,
CC       ECO:0000255|PROSITE-ProRule:PRU00427}.
CC   -!- INDUCTION: By fructose. {ECO:0000269|PubMed:1650911}.
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: In the N-terminal, the PTS system fructose-specific possesses a
CC       duplicated EIIB domain (EIIB' domain) which lacks the active site and
CC       functions to facilitate phosphoryl transfer between the EIIA domain of
CC       diphosphoryl transfer protein (DTP) and the EIIB domain. The presence
CC       of the EIIB' domain is required for normal high affinity recognition of
CC       DTP by the PTS system fructose-specific as well as for normal rates of
CC       phosphoryl transfer between the EIIA and EIIB domains of DTP and PTS
CC       system fructose-specific, respectively. {ECO:0000250|UniProtKB:P20966}.
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   -!- DISRUPTION PHENOTYPE: Cells lacking this gene grow normally on glucose
CC       but are unable to grow on fructose. {ECO:0000269|PubMed:1655739}.
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DR   EMBL; M69242; AAA27602.1; -; Genomic_DNA.
DR   EMBL; AE008922; AAM41650.1; -; Genomic_DNA.
DR   PIR; B40944; B40944.
DR   RefSeq; WP_011037515.1; NC_003902.1.
DR   AlphaFoldDB; P23355; -.
DR   STRING; 190485.XCC2372; -.
DR   EnsemblBacteria; AAM41650; AAM41650; XCC2372.
DR   KEGG; xcc:XCC2372; -.
DR   PATRIC; fig|190485.4.peg.2526; -.
DR   eggNOG; COG1299; Bacteria.
DR   eggNOG; COG1445; Bacteria.
DR   HOGENOM; CLU_013155_4_2_6; -.
DR   OrthoDB; 9782569at2; -.
DR   Proteomes; UP000001010; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
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:0090582; F:protein-phosphocysteine-D-fructose-phosphotransferase system transporter activity; ISS:UniProtKB.
DR   GO; GO:0090563; F:protein-phosphocysteine-sugar phosphotransferase activity; IBA:GO_Central.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; ISS:UniProtKB.
DR   CDD; cd05569; PTS_IIB_fructose; 1.
DR   FunFam; 3.40.50.2300:FF:000014; PTS system fructose-like transporter subunit IIB; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   InterPro; IPR050864; Bacterial_PTS_Sugar_Transport.
DR   InterPro; IPR036095; PTS_EIIB-like_sf.
DR   InterPro; IPR013011; PTS_EIIB_2.
DR   InterPro; IPR003501; PTS_EIIB_2/3.
DR   InterPro; IPR013014; PTS_EIIC_2.
DR   InterPro; IPR003353; PTS_IIB_fruc.
DR   InterPro; IPR006327; PTS_IIC_fruc.
DR   NCBIfam; TIGR00829; FRU; 1.
DR   NCBIfam; TIGR01427; PTS_IIC_fructo; 1.
DR   PANTHER; PTHR30505; FRUCTOSE-LIKE PERMEASE; 1.
DR   PANTHER; PTHR30505:SF0; FRUCTOSE-LIKE PTS SYSTEM EIIBC COMPONENT-RELATED; 1.
DR   Pfam; PF02302; PTS_IIB; 1.
DR   SUPFAM; SSF52794; PTS system IIB component-like; 2.
DR   PROSITE; PS51099; PTS_EIIB_TYPE_2; 1.
DR   PROSITE; PS51104; PTS_EIIC_TYPE_2; 1.
PE   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Direct protein sequencing; Kinase;
KW   Membrane; Phosphoprotein; Phosphotransferase system; Reference proteome;
KW   Repeat; Sugar transport; Transferase; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..580
FT                   /note="PTS system fructose-specific EIIB'BC component"
FT                   /id="PRO_0000186515"
FT   TRANSMEM        254..274
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT   TRANSMEM        289..309
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT   TRANSMEM        332..352
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT   TRANSMEM        369..389
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT   TRANSMEM        410..430
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT   TRANSMEM        451..471
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT   TRANSMEM        483..503
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT   TRANSMEM        509..529
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT   TRANSMEM        549..571
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT   DOMAIN          1..99
FT                   /note="PTS EIIB type-2 1"
FT                   /evidence="ECO:0000250|UniProtKB:P23387,
FT                   ECO:0000305|PubMed:1655739"
FT   DOMAIN          120..215
FT                   /note="PTS EIIB type-2 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00422"
FT   DOMAIN          243..580
FT                   /note="PTS EIIC type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT   ACT_SITE        126
FT                   /note="Phosphocysteine intermediate; for EIIB activity"
FT                   /evidence="ECO:0000250|UniProtKB:P20966,
FT                   ECO:0000305|PubMed:1655739"
FT   MOD_RES         126
FT                   /note="Phosphocysteine; by EIIA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00422"
FT   CONFLICT        150
FT                   /note="Q -> H (in Ref. 1; AAA27602)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        260..264
FT                   /note="AGGLL -> LAACW (in Ref. 1; AAA27602)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        350
FT                   /note="V -> L (in Ref. 1; AAA27602)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        408..409
FT                   /note="GS -> AG (in Ref. 1; AAA27602)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        494..495
FT                   /note="VT -> DS (in Ref. 1; AAA27602)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        568
FT                   /note="L -> V (in Ref. 1; AAA27602)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   580 AA;  58647 MW;  E6A3B52A7F45662B CRC64;
     MSSSIVVIAA GERSTEAVLA AEALRRAATA AGRSVTIEIR SDQGVLGALP TELTNGAAHV
     LIVGDADADT ARFGDAQLLH LSLGAVLDDP AAAVSQLAAT TAPASTSATT DASGAGGKRI
     VAITSCPTGI AHTFMAAEGL QQAAKKLGYQ MRVETQGSVG AQDALTDEEI RAADVVIIAA
     DREVDLARFG GKRLFKSGTK PAINDGPALI QKALAEAGVH GGAAPVAGAN ATSDAKGNAR
     TGAYKHLMTG VSFMLPFVTA GGLLIALAFA LGGIYAGDDA HQGTLAWSLF QIGAKAGFTL
     MVPALAGYIA YSIADRPGIA PGMIGGLVAA NLNAGFLGGI IAGFIAGYGV AALNRYIKLP
     RNLEGLKPVL ILPVLGTLLV GLAMMYVFGQ PVADLLAWLT AWLRGMQGSS ALLLGLLLGG
     MMAFDMGGPV NKAAYAFSTG LIASQVYTPM AAAMVAGMTP PLGIALATWV FRNRFTVEER
     GSATAAGVLG LAFVTEGAIP YAARDPLRTI PALVIGSAVA GAISMTAGAE LKAPHGGIFV
     LLIPNAVTHL LNYVLALVVG VVVTAVALRL LKKPVADVIA
//