PTFBC_VIBCH
ID PTFBC_VIBCH Reviewed; 580 AA.
AC Q9KM72;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=PTS system fructose-specific EIIB'BC component {ECO:0000250|UniProtKB:P20966};
DE Includes:
DE RecName: Full=PTS system fructose-specific EIIB component {ECO:0000250|UniProtKB:P20966};
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:0000250|UniProtKB:P20966};
DE Includes:
DE RecName: Full=PTS system fructose-specific EIIC component {ECO:0000250|UniProtKB:P20966};
DE AltName: Full=Fructose permease IIC component {ECO:0000250|UniProtKB:P20966};
GN Name=fruA {ECO:0000303|PubMed:33476373};
GN OrderedLocusNames=VC_A0516 {ECO:0000312|EMBL:AAF96419.1};
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
RN [2]
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=33476373; DOI=10.1093/nar/gkab013;
RA Yoon C.K., Kang D., Kim M.K., Seok Y.J.;
RT "Vibrio cholerae FruR facilitates binding of RNA polymerase to the fru
RT promoter in the presence of fructose 1-phosphate.";
RL Nucleic Acids Res. 49:1397-1410(2021).
RN [3]
RP INDUCTION.
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=33649152; DOI=10.1128/jb.00044-21;
RA Beck C., Perry S., Stoebel D.M., Liu J.M.;
RT "Cra and cAMP receptor protein have opposing roles in the regulation of
RT fruB in Vibrio cholerae.";
RL J. Bacteriol. 203:0-0(2021).
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}.
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 {ECO:0000255|PROSITE-
CC ProRule:PRU00427}; Multi-pass membrane protein {ECO:0000255|PROSITE-
CC ProRule:PRU00427}.
CC -!- INDUCTION: Part of the fruBKA (fru) operon, which is induced in the
CC presence of fructose via the FruR (Cra) regulatory protein
CC (PubMed:33476373). Transcription is repressed by FruR in the absence of
CC fructose (PubMed:33649152). CRP activates expression of the fru operon
CC in the absence of glucose (PubMed:33649152). The two regulators can
CC work independently to control the expression of the operon depending on
CC carbon source availability (PubMed:33649152).
CC {ECO:0000269|PubMed:33476373, ECO:0000269|PubMed:33649152}.
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 -!- DISRUPTION PHENOTYPE: Does not affect growth on fructose or on glucose.
CC {ECO:0000269|PubMed:33476373}.
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DR EMBL; AE003853; AAF96419.1; -; Genomic_DNA.
DR PIR; B82450; B82450.
DR RefSeq; NP_232907.1; NC_002506.1.
DR SMR; Q9KM72; -.
DR STRING; 243277.VC_A0516; -.
DR PRIDE; Q9KM72; -.
DR DNASU; 2612387; -.
DR EnsemblBacteria; AAF96419; AAF96419; VC_A0516.
DR KEGG; vch:VC_A0516; -.
DR PATRIC; fig|243277.26.peg.3142; -.
DR eggNOG; COG1299; Bacteria.
DR eggNOG; COG1445; Bacteria.
DR HOGENOM; CLU_013155_4_2_6; -.
DR OMA; CKLMAPH; -.
DR BioCyc; VCHO:VCA0516-MON; -.
DR Proteomes; UP000000584; Chromosome 2.
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:0090563; F:protein-phosphocysteine-sugar phosphotransferase activity; IBA:GO_Central.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05569; PTS_IIB_fructose; 2.
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; IPR003353; PTS_IIB_fruc.
DR InterPro; IPR006327; PTS_IIC_fruc.
DR Pfam; PF02378; PTS_EIIC; 1.
DR Pfam; PF02302; PTS_IIB; 2.
DR SUPFAM; SSF52794; SSF52794; 2.
DR TIGRFAMs; TIGR00829; FRU; 1.
DR TIGRFAMs; TIGR01427; PTS_IIC_fructo; 1.
DR PROSITE; PS51099; PTS_EIIB_TYPE_2; 2.
DR PROSITE; PS51104; PTS_EIIC_TYPE_2; 1.
PE 2: Evidence at transcript level;
KW Cell inner membrane; Cell membrane; Kinase; Membrane; Phosphoprotein;
KW Phosphotransferase system; Reference proteome; Repeat; Sugar transport;
KW Transferase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..580
FT /note="PTS system fructose-specific EIIB'BC component"
FT /id="PRO_5004328287"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 367..387
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 408..428
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 448..468
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 480..500
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 507..527
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 537..557
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 3..100
FT /note="PTS EIIB type-2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00422"
FT DOMAIN 124..221
FT /note="PTS EIIB type-2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00422"
FT DOMAIN 244..579
FT /note="PTS EIIC type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT ACT_SITE 11
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000305"
FT ACT_SITE 132
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000250|UniProtKB:P20966"
FT MOD_RES 11
FT /note="Phosphocysteine; by EIIA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00422"
FT MOD_RES 132
FT /note="Phosphocysteine; by EIIA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00422"
SQ SEQUENCE 580 AA; 59645 MW; 58362E6F29229EA2 CRC64;
MKMKIAIVTA CPSGVANSII AAGLLQQASK TLGWEAYIEC HSTVIAGHTL SEEEINKADL
VILAANGKID MQRFVGKKVY QSPITACTSD PVGYLKQAAE QATELSSEQA TRCDSPATAS
VSAKKIVAIT ACPTGVAHTF MAAEALEAEA TRQGHQIKVE TRGSVGAKNQ LTEQEIAAAD
LVIIAADIDV PLDRFNGKKL YKTSTGLTLK KTAQELSNAF AQAKTFSSSA NSATNEKAEE
KKGVYKHLMT GVSHMLPVVV AGGLIIALSF VFGIEAFKEE GTLAAALMQI GGGSAFALMI
PVLAGYIAFS IADRPGLAPG LIGGMLASST GAGFLGGIVA GFLAGYSAKF IADKVQLPQS
MAALKPILII PFIASLFTGL VMIYVVGGPM SSIMSGMTSF LNNMGSTNAI LLGIVLGAMM
CFDLGGPVNK AAYTFGVGLL ASQTYAPMAA IMAAGMVPAL GMGLATFIAK DKFEAGEREA
GKASFVLGLC FISEGAIPFA AKDPMRVIPA CMVGGAVTGA LSMLFGAKLM APHGGLFVLL
IPNAISPVLL YLVAIAVGTA ITGFGYAMLK KSAQAKAVAA
