PTFB_HALVD
ID PTFB_HALVD Reviewed; 158 AA.
AC D4GYE1;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=PTS system fructose-specific EIIB component {ECO:0000303|PubMed:22493022};
DE EC=2.7.1.202 {ECO:0000250|UniProtKB:P20966};
DE AltName: Full=EIIB-Fru {ECO:0000303|PubMed:22493022};
DE AltName: Full=Fructose-specific phosphotransferase enzyme IIB component {ECO:0000303|PubMed:22493022};
GN Name=ptfB {ECO:0000303|PubMed:20333302}; Synonyms=fruA1;
GN OrderedLocusNames=HVO_1495;
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
RN [2]
RP FUNCTION, IDENTIFICATION, AND INDUCTION.
RC STRAIN=DS2 / DS70;
RX PubMed=22493022; DOI=10.1128/jb.00200-12;
RA Pickl A., Johnsen U., Schoenheit P.;
RT "Fructose degradation in the haloarchaeon Haloferax volcanii involves a
RT bacterial type phosphoenolpyruvate-dependent phosphotransferase system,
RT fructose-1-phosphate kinase, and class II fructose-1,6-bisphosphate
RT aldolase.";
RL J. Bacteriol. 194:3088-3097(2012).
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 PtfABC PTS system is involved in fructose transport.
CC {ECO:0000269|PubMed:22493022}.
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 -!- INDUCTION: Expression is highly up-regulated in presence of fructose.
CC {ECO:0000269|PubMed:22493022}.
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 -!- MISCELLANEOUS: PTS-type transport systems are very rare in archaea.
CC {ECO:0000305}.
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DR EMBL; CP001956; ADE04643.1; -; Genomic_DNA.
DR RefSeq; WP_013035585.1; NZ_AOHU01000090.1.
DR AlphaFoldDB; D4GYE1; -.
DR SMR; D4GYE1; -.
DR STRING; 309800.C498_11256; -.
DR TCDB; 4.A.2.1.15; the pts fructose-mannitol (fru) family.
DR EnsemblBacteria; ADE04643; ADE04643; HVO_1495.
DR GeneID; 8924329; -.
DR KEGG; hvo:HVO_1495; -.
DR eggNOG; arCOG10194; Archaea.
DR HOGENOM; CLU_013155_2_1_2; -.
DR OMA; IAVCACP; -.
DR OrthoDB; 114557at2157; -.
DR Proteomes; UP000008243; 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:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Cytoplasm; Kinase; Phosphoprotein; Phosphotransferase system;
KW Reference proteome; Sugar transport; Transferase; Transport.
FT CHAIN 1..158
FT /note="PTS system fructose-specific EIIB component"
FT /id="PRO_0000428983"
FT DOMAIN 1..98
FT /note="PTS EIIB type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00422"
FT REGION 104..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..132
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 9
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P20966, ECO:0000305"
FT MOD_RES 9
FT /note="Phosphocysteine; by EIIA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00422"
SQ SEQUENCE 158 AA; 16279 MW; 5430C7ED0ADD79DC CRC64;
MKLVAVTSCP TGIAHSQMAA ENLLQAGERL GHDIDVEVQG AMGTQDELAS DAIAEADAVI
ITSDTSVSRD RFDGKLVLKG TVKDGVNNAE AVVQKAVELA EAGKTGSVTF GSGDDGEDAD
VGADDSSDDA DAAESDEPVR RGGDPEKGLF ARLKKLFS
