PTFBC_XANCP
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 03-AUG-2022, entry version 146.
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; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; 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; NP_637726.1; NC_003902.1.
DR RefSeq; WP_011037515.1; NC_003902.1.
DR AlphaFoldDB; P23355; -.
DR STRING; 340.xcc-b100_1800; -.
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 OMA; CKLMAPH; -.
DR Proteomes; UP000001010; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005351; F:carbohydrate:proton symporter activity; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
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 GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05569; PTS_IIB_fructose; 1.
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 Pfam; PF02302; PTS_IIB; 1.
DR SUPFAM; SSF52794; SSF52794; 2.
DR TIGRFAMs; TIGR00829; FRU; 1.
DR TIGRFAMs; TIGR01427; PTS_IIC_fructo; 1.
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
