PTFAH_SALTI
ID PTFAH_SALTI Reviewed; 376 AA.
AC Q8Z591;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Multiphosphoryl transfer protein {ECO:0000250|UniProtKB:P44715};
DE Short=MTP {ECO:0000250|UniProtKB:P44715};
DE AltName: Full=Diphosphoryl transfer protein {ECO:0000250|UniProtKB:P69811};
DE Short=DTP {ECO:0000250|UniProtKB:P69811};
DE AltName: Full=Phosphotransferase FPr protein {ECO:0000250|UniProtKB:P17127};
DE AltName: Full=Pseudo-HPr {ECO:0000250|UniProtKB:P17127};
DE Includes:
DE RecName: Full=Phosphocarrier protein HPr {ECO:0000250|UniProtKB:P17127};
DE Short=Protein H {ECO:0000250|UniProtKB:P17127};
DE Includes:
DE RecName: Full=PTS system fructose-specific EIIA component {ECO:0000250|UniProtKB:P17127};
DE AltName: Full=EIIA-Fru {ECO:0000250|UniProtKB:P17127};
DE AltName: Full=EIII-Fru {ECO:0000250|UniProtKB:P17127};
DE AltName: Full=Fructose-specific phosphotransferase enzyme IIA component {ECO:0000250|UniProtKB:P17127};
GN Name=fruB; OrderedLocusNames=STY2442, t0650;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
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:P17127}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Induced by fructose and repressed by FruR.
CC {ECO:0000250|UniProtKB:P17127}.
CC -!- DOMAIN: The PTS EIIA type-2 domain is phosphorylated by phospho-HPr on
CC a histidyl residue. Then, it transfers the phosphoryl group to the PTS
CC EIIB type-2 domain. {ECO:0000255|PROSITE-ProRule:PRU00417}.
CC -!- DOMAIN: In contrast to classical PTS systems, the fructose-specific PTS
CC has no requirement for HPr; FruB combines a IIA domain with a HPr
CC domain. {ECO:0000250|UniProtKB:P17127}.
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DR EMBL; AL513382; CAD02588.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO68350.1; -; Genomic_DNA.
DR RefSeq; NP_456764.1; NC_003198.1.
DR RefSeq; WP_000487294.1; NZ_PZMG01000001.1.
DR AlphaFoldDB; Q8Z591; -.
DR SMR; Q8Z591; -.
DR STRING; 220341.16503445; -.
DR EnsemblBacteria; AAO68350; AAO68350; t0650.
DR KEGG; stt:t0650; -.
DR KEGG; sty:STY2442; -.
DR PATRIC; fig|220341.7.peg.2468; -.
DR eggNOG; COG1925; Bacteria.
DR eggNOG; COG4668; Bacteria.
DR HOGENOM; CLU_046384_0_0_6; -.
DR OMA; QGIEWGE; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00367; PTS-HPr_like; 1.
DR CDD; cd00211; PTS_IIA_fru; 1.
DR Gene3D; 3.30.1340.10; -; 1.
DR Gene3D; 3.40.930.10; -; 1.
DR InterPro; IPR000032; HPr-like.
DR InterPro; IPR035895; HPr-like_sf.
DR InterPro; IPR016152; PTrfase/Anion_transptr.
DR InterPro; IPR002178; PTS_EIIA_type-2_dom.
DR InterPro; IPR001020; PTS_HPr_His_P_site.
DR InterPro; IPR002114; PTS_HPr_Ser_P_site.
DR Pfam; PF00381; PTS-HPr; 1.
DR Pfam; PF00359; PTS_EIIA_2; 1.
DR PRINTS; PR00107; PHOSPHOCPHPR.
DR SUPFAM; SSF55594; SSF55594; 1.
DR SUPFAM; SSF55804; SSF55804; 2.
DR TIGRFAMs; TIGR01003; PTS_HPr_family; 1.
DR PROSITE; PS51094; PTS_EIIA_TYPE_2; 1.
DR PROSITE; PS00372; PTS_EIIA_TYPE_2_HIS; 1.
DR PROSITE; PS51350; PTS_HPR_DOM; 1.
DR PROSITE; PS00369; PTS_HPR_HIS; 1.
DR PROSITE; PS00589; PTS_HPR_SER; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Kinase; Phosphoprotein; Phosphotransferase system;
KW Sugar transport; Transferase; Transport.
FT CHAIN 1..376
FT /note="Multiphosphoryl transfer protein"
FT /id="PRO_0000186518"
FT DOMAIN 2..142
FT /note="PTS EIIA type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00417"
FT DOMAIN 285..375
FT /note="HPr"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00681"
FT REGION 156..284
FT /note="M domain"
FT /evidence="ECO:0000250|UniProtKB:P44715"
FT ACT_SITE 62
FT /note="Tele-phosphohistidine intermediate; for EIIA
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00417"
FT ACT_SITE 299
FT /note="Pros-phosphohistidine intermediate; for HPr
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00681"
FT MOD_RES 62
FT /note="Phosphohistidine; by HPr"
FT /evidence="ECO:0000305"
FT MOD_RES 299
FT /note="Phosphohistidine; by EI"
FT /evidence="ECO:0000305"
FT CONFLICT 15
FT /note="V -> A (in Ref. 2; AAO68350)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 376 AA; 39622 MW; DFEE6517821DF550 CRC64;
MFQLSVQDIH PGEQVGNKEE AIRQIAAALA QAGNVAGGYV DGMLAREQQT STFLGNGIAI
PHGTTDTRDQ VLKTGVQVFQ FPQGVTWGEG QVAYVAIGIA ASSDEHLGLL RQLTHVLSDD
SVAEQLKSAT TAEELRALLM GEKQSEQLKL DNETMTLDVI ASSLVTLQAL NAARLKEAGA
VDAAFVAKTI NDSPMNLGQG IWLNDSAEGN LRSAVAVSRA TQAFDVEGEK AALLVTVAMN
DEQPIAVLKR LGDLLLNNKA DRLLSADAAT LLALLTSDDA LTDDVLSAEF VVRNEHGLHA
RPGTMLVNTI KQFNSEITVT NLDGTGKPAN GRSLMKVVAL GVKKGHRLRF TAQGEDAEQA
LKAIGDAIAA GLGEGA
