PTFC_HALVD
ID PTFC_HALVD Reviewed; 375 AA.
AC D4GYE5;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 25-MAY-2022, entry version 54.
DE RecName: Full=PTS system fructose-specific EIIC component {ECO:0000303|PubMed:22493022};
DE AltName: Full=EIIC-Fru {ECO:0000303|PubMed:22493022};
DE AltName: Full=Fructose permease IIC {ECO:0000303|PubMed:22493022};
GN Name=ptfC {ECO:0000303|PubMed:20333302}; OrderedLocusNames=HVO_1499;
GN ORFNames=C498_11236;
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 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=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
RN [3]
RP IDENTIFICATION, INDUCTION, FUNCTION, AND DISRUPTION PHENOTYPE.
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00427}; Multi-pass membrane protein {ECO:0000255|PROSITE-
CC ProRule:PRU00427}.
CC -!- INDUCTION: Expression is highly up-regulated in presence of fructose.
CC {ECO:0000269|PubMed:22493022}.
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 are unable to grow on
CC fructose. Growth on glucose is unaffected.
CC {ECO:0000269|PubMed:22493022}.
CC -!- MISCELLANEOUS: PTS-type transport systems are very rare in archaea.
CC {ECO:0000305}.
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DR EMBL; CP001956; ADE05002.1; -; Genomic_DNA.
DR EMBL; AOHU01000090; ELY28263.1; -; Genomic_DNA.
DR RefSeq; WP_004043436.1; NZ_AOHU01000090.1.
DR AlphaFoldDB; D4GYE5; -.
DR SMR; D4GYE5; -.
DR STRING; 309800.C498_11236; -.
DR TCDB; 4.A.2.1.15; the pts fructose-mannitol (fru) family.
DR EnsemblBacteria; ADE05002; ADE05002; HVO_1499.
DR EnsemblBacteria; ELY28263; ELY28263; C498_11236.
DR GeneID; 8924700; -.
DR KEGG; hvo:HVO_1499; -.
DR PATRIC; fig|309800.29.peg.2141; -.
DR eggNOG; arCOG10196; Archaea.
DR HOGENOM; CLU_013155_0_1_2; -.
DR OMA; QGQNGIQ; -.
DR OrthoDB; 48210at2157; -.
DR Proteomes; UP000008243; Chromosome.
DR Proteomes; UP000011532; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005351; F:carbohydrate:proton symporter activity; IEA:InterPro.
DR GO; GO:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:InterPro.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR InterPro; IPR003352; PTS_EIIC.
DR InterPro; IPR013014; PTS_EIIC_2.
DR InterPro; IPR006327; PTS_IIC_fruc.
DR Pfam; PF02378; PTS_EIIC; 1.
DR TIGRFAMs; TIGR01427; PTS_IIC_fructo; 1.
DR PROSITE; PS51104; PTS_EIIC_TYPE_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Membrane; Phosphotransferase system; Reference proteome;
KW Sugar transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..375
FT /note="PTS system fructose-specific EIIC component"
FT /id="PRO_0000428984"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 279..299
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 301..321
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 340..360
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT DOMAIN 16..370
FT /note="PTS EIIC type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
SQ SEQUENCE 375 AA; 38141 MW; CD7FC79518867C01 CRC64;
MANDAEDAVR SYLTSVKEDL MTGVSFMIPF VTIGGIFLAL GYAVASLSNN VQDVFNSTGT
AGWFLAQIGV AGLTLMVPVL GAYIAYAIAD RPGLAPGFIL SYIIQQGNVL QAAGDVIGLQ
GGSAGAGYLG AIVAGFLAGI VARWFKQRDV PEFIAPMMPV LLIPVATTAV LTPVMLFVLG
VPISIANAGL TEFLSNMQGG GQAILLGGIL GAMMAADMGG PINKVAYVFS VGLISEGVTA
PMAAVMIAGM VPPIGLALSN FIAPQKYAAE MYENAKSGVL LGFSFITEGA IPYAAADPAR
VIPSVVAGSA VAGAASMALG VNMPAPHGGI FVVPLSNQPF MFIACILLGS IVTAVIATAI
KPNFDAKMAA QSSDD
