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Database: UniProt
Entry: Q7NTK0_CHRVO
LinkDB: Q7NTK0_CHRVO
Original site: Q7NTK0_CHRVO 
ID   Q7NTK0_CHRVO            Unreviewed;       554 AA.
AC   Q7NTK0;
DT   15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2003, sequence version 1.
DT   27-MAR-2024, entry version 118.
DE   RecName: Full=protein-N(pi)-phosphohistidine--D-fructose phosphotransferase {ECO:0000256|ARBA:ARBA00012799};
DE            EC=2.7.1.202 {ECO:0000256|ARBA:ARBA00012799};
GN   Name=fruA {ECO:0000313|EMBL:AAQ60723.1};
GN   OrderedLocusNames=CV_3054 {ECO:0000313|EMBL:AAQ60723.1};
OS   Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC
OS   12614 / NCIMB 9131 / NCTC 9757).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC   Chromobacteriaceae; Chromobacterium.
OX   NCBI_TaxID=243365 {ECO:0000313|EMBL:AAQ60723.1, ECO:0000313|Proteomes:UP000001424};
RN   [1] {ECO:0000313|EMBL:AAQ60723.1, ECO:0000313|Proteomes:UP000001424}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 /
RC   NCTC 9757 {ECO:0000313|Proteomes:UP000001424};
RX   PubMed=14500782; DOI=10.1073/pnas.1832124100;
RA   Vasconcelos A.T.R., de Almeida D.F., Almeida F.C., de Almeida L.G.P.,
RA   de Almeida R., Goncalves J.A.A., Andrade E.M., Antonio R.V., Araripe J.,
RA   de Araujo M.F.F., Filho S.A., Azevedo V., Batista A.J., Bataus L.A.M.,
RA   Batista J.S., Belo A., vander Berg C., Blamey J., Bogo M., Bonato S.,
RA   Bordignon J., Brito C.A., Brocchi M., Burity H.A., Camargo A.A.,
RA   Cardoso D.D.P., Carneiro N.P., Carraro D.M., Carvalho C.M.B.,
RA   Cascardo J.C.M., Cavada B.S., Chueire L.M.O., Pasa T.B.C., Duran N.,
RA   Fagundes N., Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S.,
RA   Ferrari L.P., Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A.,
RA   Furlan L.R., Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B.,
RA   Grattapaglia D., Grisard E.C., Guimaraes C.T., Hanna E.S., Hungria M.,
RA   Jardim S.N., Laurino J., Leoi L.C.T., Fassarella L., Lima A.,
RA   Loureiro M.F., Lyra M.C.P., Macedo M., Madeira H.M.F., Manfio G.P.,
RA   Maranhao A.Q., Martins W.S., di Mauro S.M.Z., de Medeiros S.R.B.,
RA   Meissner R.D.V., Menck C.F.M., Moreira M.A.M., Nascimento F.F.,
RA   Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A.,
RA   Pedrosa F.O., Pena S.J.D., Perreira J.O., Perreira M., Pinto L.S.R.C.,
RA   Pinto L.S., Porto J.I.R., Potrich D.P., Neto C.E.R., Reis A.M.M.,
RA   Rigo L.U., Rondinelli E., dos Santos E.B.P., Santos F.R., Schneider M.P.C.,
RA   Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R.,
RA   Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M.,
RA   Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R.,
RA   Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.;
RT   "The complete genome sequence of Chromobacterium violaceum reveals
RT   remarkable and exploitable bacterial adaptability.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003).
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:0000256|ARBA:ARBA00001401};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; AE016825; AAQ60723.1; -; Genomic_DNA.
DR   RefSeq; WP_011136601.1; NC_005085.1.
DR   AlphaFoldDB; Q7NTK0; -.
DR   STRING; 243365.CV_3054; -.
DR   KEGG; cvi:CV_3054; -.
DR   eggNOG; COG1299; Bacteria.
DR   eggNOG; COG1445; Bacteria.
DR   HOGENOM; CLU_013155_4_2_4; -.
DR   OrthoDB; 9782569at2; -.
DR   Proteomes; UP000001424; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005351; F:carbohydrate:proton symporter activity; IEA:InterPro.
DR   GO; GO:0103111; F:D-glucosamine PTS permease activity; IEA:UniProtKB-EC.
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   CDD; cd05569; PTS_IIB_fructose; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
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   NCBIfam; TIGR00829; FRU; 1.
DR   NCBIfam; TIGR01427; PTS_IIC_fructo; 1.
DR   PANTHER; PTHR30505; FRUCTOSE-LIKE PERMEASE; 1.
DR   PANTHER; PTHR30505:SF0; FRUCTOSE-LIKE PTS SYSTEM EIIBC COMPONENT-RELATED; 1.
DR   Pfam; PF02302; PTS_IIB; 1.
DR   SUPFAM; SSF52794; PTS system IIB component-like; 2.
DR   PROSITE; PS51099; PTS_EIIB_TYPE_2; 1.
DR   PROSITE; PS51104; PTS_EIIC_TYPE_2; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Phosphotransferase system {ECO:0000256|ARBA:ARBA00022683};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001424};
KW   Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AAQ60723.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        229..253
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        265..287
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        299..324
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        345..364
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        384..400
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        412..438
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        485..505
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        525..547
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          99..194
FT                   /note="PTS EIIB type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51099"
FT   DOMAIN          219..554
FT                   /note="PTS EIIC type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51104"
SQ   SEQUENCE   554 AA;  56382 MW;  FA67E3FFD9FC8C66 CRC64;
     MSIVAIIRAP ERSTQARLAA EALRQAAQRQ GKRIDIEIDG QPALGADILQ AASQILLVDC
     PDDARAGQKP ARRATLDAVL ADPAAQLDGA AAAERALSIV AITGCPTGIA HTFMAAEGLV
     QGAKALGHAM RVETQGSVGA QNALTDAEIA AADLVVIAAD TQVQLDRFAG KRLFKSGTKA
     AIGDGKALIR RAIAEAQPWS GAAAPAAQAA GKEKTKDGPY RHLMTGVSFM LPFVTAGGIL
     IALAFALGGI YAFDDAHKGT LAWSLFQIGA KSAFALMVPI LAGYIAYSVA DRPGIAPGMV
     GGMLAASLGS GFLGGIVAGF IAGYGTRELN RRIQLGQHLD GLKPVLILPV LGSLLTGLLM
     IYVVGQPVAA VLAALTDALK GMQGSSALAL GALLGAMMAF DMGGPVNKAA YAFATGLIAS
     QVYTPMAAVM AAGMTPPLGI ALATRLFRDR FTVDEHEAGK AAAVLGLAFI SEGAIPFAAR
     DPFRVIPALM AGSALAGAVS MTMGVELKVP HGGVFVLPIP NAVEHLASYL AALAAGTAVT
     ALALGLLKKR IPQA
//
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