PTFAH_SALTY
ID PTFAH_SALTY Reviewed; 376 AA.
AC P17127;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 149.
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:0000303|PubMed:2546043};
DE AltName: Full=Pseudo-HPr {ECO:0000303|PubMed:2546043};
DE Includes:
DE RecName: Full=Phosphocarrier protein HPr {ECO:0000303|PubMed:2546043};
DE Short=Protein H {ECO:0000305};
DE Includes:
DE RecName: Full=PTS system fructose-specific EIIA component {ECO:0000303|PubMed:2546043};
DE AltName: Full=EIIA-Fru {ECO:0000303|PubMed:2546043};
DE AltName: Full=EIII-Fru {ECO:0000303|PubMed:2546043};
DE AltName: Full=Fructose-specific phosphotransferase enzyme IIA component {ECO:0000303|PubMed:2546043};
GN Name=fruB; Synonyms=fpr, fruF {ECO:0000303|PubMed:2546043};
GN OrderedLocusNames=STM2206;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP INDUCTION.
RX PubMed=2546043; DOI=10.1007/bf00334399;
RA Geerse R.H., Izzo F., Postma P.W.;
RT "The PEP: fructose phosphotransferase system in Salmonella typhimurium: FPr
RT combines enzyme IIIFru and pseudo-HPr activities.";
RL Mol. Gen. Genet. 216:517-525(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP PROTEIN SEQUENCE OF 250-269, FUNCTION, CATALYTIC ACTIVITY, AND DOMAIN.
RX PubMed=3281935; DOI=10.1016/s0021-9258(18)60679-9;
RA Sutrina S.L., Chin A.M., Esch F., Saier M.H. Jr.;
RT "Purification and characterization of the fructose-inducible HPr-like
RT protein, FPr, and the fructose-specific enzyme III of the
RT phosphoenolpyruvate: sugar phosphotransferase system of Salmonella
RT typhimurium.";
RL J. Biol. Chem. 263:5061-5069(1988).
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:0000269|PubMed:2546043, ECO:0000269|PubMed:3281935}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Induced by fructose and repressed by FruR.
CC {ECO:0000269|PubMed:2546043}.
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:0000269|PubMed:3281935}.
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DR EMBL; X14243; CAA32459.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL21110.1; -; Genomic_DNA.
DR PIR; JE0023; JE0023.
DR RefSeq; NP_461151.1; NC_003197.2.
DR RefSeq; WP_000487287.1; NC_003197.2.
DR AlphaFoldDB; P17127; -.
DR SMR; P17127; -.
DR STRING; 99287.STM2206; -.
DR PaxDb; P17127; -.
DR EnsemblBacteria; AAL21110; AAL21110; STM2206.
DR GeneID; 1253728; -.
DR KEGG; stm:STM2206; -.
DR PATRIC; fig|99287.12.peg.2335; -.
DR HOGENOM; CLU_046384_0_0_6; -.
DR OMA; QGIEWGE; -.
DR PhylomeDB; P17127; -.
DR BioCyc; SENT99287:STM2206-MON; -.
DR SABIO-RK; P17127; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0090563; F:protein-phosphocysteine-sugar phosphotransferase activity; IBA:GO_Central.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IBA:GO_Central.
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 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Kinase; Phosphoprotein;
KW Phosphotransferase system; Reference proteome; Sugar transport;
KW Transferase; Transport.
FT CHAIN 1..376
FT /note="Multiphosphoryl transfer protein"
FT /id="PRO_0000186519"
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"
SQ SEQUENCE 376 AA; 39594 MW; 40131F4BB2DA4855 CRC64;
MFQLSVQDIH PGEQAGNKEE 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
