PTFAH_ECO57
ID PTFAH_ECO57 Reviewed; 376 AA.
AC P69812; P24217; P94759;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
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:P69811};
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:P69811};
GN Name=fruB {ECO:0000250|UniProtKB:P69811}; OrderedLocusNames=Z3427, ECs3061;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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:P69811}.
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:P69811}.
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DR EMBL; AE005174; AAG57307.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB36484.1; -; Genomic_DNA.
DR PIR; E91011; E91011.
DR RefSeq; NP_311088.1; NC_002695.1.
DR RefSeq; WP_000487246.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P69812; -.
DR SMR; P69812; -.
DR STRING; 155864.EDL933_3333; -.
DR EnsemblBacteria; AAG57307; AAG57307; Z3427.
DR EnsemblBacteria; BAB36484; BAB36484; ECs_3061.
DR GeneID; 916765; -.
DR KEGG; ece:Z3427; -.
DR KEGG; ecs:ECs_3061; -.
DR PATRIC; fig|386585.9.peg.3190; -.
DR eggNOG; COG1925; Bacteria.
DR eggNOG; COG4668; Bacteria.
DR HOGENOM; CLU_046384_0_0_6; -.
DR OMA; QGIEWGE; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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 Reference proteome; Sugar transport; Transferase; Transport.
FT CHAIN 1..376
FT /note="Multiphosphoryl transfer protein"
FT /id="PRO_0000186517"
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; 39648 MW; D4D953E69E2090FF CRC64;
MFQLSVQDIH PGEKAGDKEE AIRQVAAALV QAGNVAEGYV NGMLAREQQT STFLGNGIAI
PHGTTDTRDQ VLKTGVQVFQ FPEGVTWGDG QVAYVAIGIA ASSDEHLGLL RQLTHVLSDD
SVAEQLKSAT TAEELRALLM GEKQSEQLKL DNEMLTLDIV ASDLLTLQAL NAARLKEAGA
VDATFVTKAI NEQPLNLGQG IWLSDSAEGN LRSAIAVSRA ANAFDVDGET AAMLVSVAMN
DDQPIAVLKR LADLLLDNKA DRLLKADAAT LLALLTSDDA PTDDVLSAEF VVRNEHGLHA
RPGTMLVNTI KQFNSDITVT NLDGTGKPAN GRSLMKVVAL GVKKGHRLRF TAQGADAEQA
LKAIGDAIAA GLGEGA
