PTFBC_HAEIN
ID PTFBC_HAEIN Reviewed; 556 AA.
AC P44714;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=PTS system fructose-specific EIIB'BC component {ECO:0000250|UniProtKB:P20966};
DE AltName: Full=EIIB'BC-Fru {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:0000250|UniProtKB:P20966}; OrderedLocusNames=HI_0446;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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
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:0000250|UniProtKB:P23355}.
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}.
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DR EMBL; L42023; AAC22105.1; -; Genomic_DNA.
DR PIR; I64068; I64068.
DR RefSeq; NP_438607.1; NC_000907.1.
DR RefSeq; WP_005693715.1; NC_000907.1.
DR AlphaFoldDB; P44714; -.
DR SMR; P44714; -.
DR STRING; 71421.HI_0446; -.
DR EnsemblBacteria; AAC22105; AAC22105; HI_0446.
DR KEGG; hin:HI_0446; -.
DR PATRIC; fig|71421.8.peg.466; -.
DR eggNOG; COG1299; Bacteria.
DR eggNOG; COG1445; Bacteria.
DR eggNOG; COG3925; Bacteria.
DR HOGENOM; CLU_013155_4_1_6; -.
DR OMA; CKLMAPH; -.
DR PhylomeDB; P44714; -.
DR BioCyc; HINF71421:G1GJ1-462-MON; -.
DR Proteomes; UP000000579; 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; 1.
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 3: Inferred from homology;
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..556
FT /note="PTS system fructose-specific EIIB'BC component"
FT /id="PRO_0000186509"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 324..344
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 349..369
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 390..410
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 431..451
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 468..488
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 490..510
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 529..549
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT DOMAIN 1..85
FT /note="PTS EIIB type-2 1"
FT /evidence="ECO:0000250|UniProtKB:P20966"
FT DOMAIN 106..201
FT /note="PTS EIIB type-2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00422"
FT DOMAIN 224..556
FT /note="PTS EIIC type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT ACT_SITE 112
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000250|UniProtKB:P20966, ECO:0000305"
FT MOD_RES 112
FT /note="Phosphocysteine; by EIIA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00422"
SQ SEQUENCE 556 AA; 57706 MW; 31D8E77BFDBA7E42 CRC64;
MKLFLTQSAN VGDVKAYLLH EVFRAAAQKA NVSIVGTPAE ADLVLVFGSV LPNNPDLVGK
KVFIIGEAIA MISPEVTLAN ALANGADYVA PKSAVSFTGV SGVKNIVAVT ACPTGVAHTF
MSAEAIEAYA KKQGWNVKVE TRGQVGAGNE ITVEEVAAAD LVFVAADIDV PLDKFKGKPM
YRTSTGLALK KTEQEFDKAF KEAKIFDGGN NAGTKEESRE KKGVYKHLMT GVSHMLPLVV
AGGLLIAISF MFSFNVIENT GVFQDLPNML INIGSGVAFK LMIAVFAGYV AFSIADRPGL
AVGLIAGMLA SEAGAGILGG IIAGFLAGYV VKGLNVIIRL PASLTSLKPI LILPLLGSMI
VGLTMIYLIN PPVAEIMKEL SNWLTSMGEV NAIVLGAIIG AMMCIDMGGP VNKAAYTFSV
GLIASQVYTP MAAAMAAGMV PPIGMTVATW IARNKFTVSQ CDAGKASFVL GLCFISEGAL
PFVAADPIRV IISSVIGGAV AGAISMGLNI TLQAPHGGLF VIPFVSEPLK YLGAIAIGAL
STGVVYAIIK SKNNAE
