PTFB2_ECO57
ID PTFB2_ECO57 Reviewed; 106 AA.
AC P69818; P32673;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=PTS system fructose-like EIIB component 2 {ECO:0000250|UniProtKB:P20966};
DE EC=2.7.1.202 {ECO:0000250|UniProtKB:P20966};
DE AltName: Full=Fructose-like phosphotransferase enzyme IIB component 2 {ECO:0000250|UniProtKB:P20966};
GN Name=frwB; OrderedLocusNames=Z5506, ECs4879;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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 FrwABC 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: Cytoplasm {ECO:0000305}.
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}.
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DR EMBL; AE005174; AAG59152.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB38302.1; -; Genomic_DNA.
DR PIR; D86086; D86086.
DR PIR; G91238; G91238.
DR RefSeq; NP_312906.1; NC_002695.1.
DR RefSeq; WP_000161265.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P69818; -.
DR SMR; P69818; -.
DR STRING; 155864.EDL933_5286; -.
DR DNASU; 960182; -.
DR EnsemblBacteria; AAG59152; AAG59152; Z5506.
DR EnsemblBacteria; BAB38302; BAB38302; ECs_4879.
DR GeneID; 67417533; -.
DR GeneID; 915006; -.
DR KEGG; ece:Z5506; -.
DR KEGG; ecs:ECs_4879; -.
DR PATRIC; fig|386585.9.peg.5103; -.
DR eggNOG; COG1445; Bacteria.
DR HOGENOM; CLU_013155_2_1_6; -.
DR OMA; TPHDIAQ; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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: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; IPR003353; PTS_IIB_fruc.
DR Pfam; PF02302; PTS_IIB; 1.
DR SUPFAM; SSF52794; SSF52794; 1.
DR TIGRFAMs; TIGR00829; FRU; 1.
DR PROSITE; PS51099; PTS_EIIB_TYPE_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Kinase; Phosphoprotein; Phosphotransferase system;
KW Reference proteome; Sugar transport; Transferase; Transport.
FT CHAIN 1..106
FT /note="PTS system fructose-like EIIB component 2"
FT /id="PRO_0000186503"
FT DOMAIN 1..103
FT /note="PTS EIIB type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00422"
FT ACT_SITE 10
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P20966, ECO:0000305"
FT MOD_RES 10
FT /note="Phosphocysteine; by EIIA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00422"
SQ SEQUENCE 106 AA; 11248 MW; F712189F18489D3D CRC64;
MTKIIAVTAC PSGVAHTYMA AEALESAAKA KGWEVKVETQ GSIGLENELT AEDVASADMV
ILTKDIGIKF EERFAGKTIV RVNISDAVKR ADAIMSKIEA HLAQTA
