PTFX2_ECOLI
ID PTFX2_ECOLI Reviewed; 833 AA.
AC P32670; Q2M8P3;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Multiphosphoryl transfer protein 2 {ECO:0000305|PubMed:7773398};
DE Short=MTP 2 {ECO:0000305|PubMed:7773398};
DE AltName: Full=Triphosphoryl transfer protein 2 {ECO:0000250|UniProtKB:P77439};
DE Short=TTP 2 {ECO:0000250|UniProtKB:P77439};
DE Includes:
DE RecName: Full=Phosphoenolpyruvate-protein phosphotransferase {ECO:0000303|PubMed:7773398};
DE EC=2.7.3.9 {ECO:0000250|UniProtKB:P08839};
DE AltName: Full=Enzyme I-Ani {ECO:0000303|PubMed:7773398};
DE AltName: Full=Phosphotransferase system enzyme I {ECO:0000303|PubMed:7773398};
DE Includes:
DE RecName: Full=Phosphocarrier protein HPr {ECO:0000250|UniProtKB:P77439};
DE Short=Protein H {ECO:0000250|UniProtKB:P77439};
DE Includes:
DE RecName: Full=PTS system fructose-like EIIA component {ECO:0000303|PubMed:7773398};
DE EC=2.7.1.202 {ECO:0000250|UniProtKB:P20966};
DE AltName: Full=Fructose-like phosphotransferase enzyme IIA component {ECO:0000303|PubMed:7773398};
GN Name=ptsA {ECO:0000303|PubMed:7773398}; Synonyms=frwA, yijH;
GN OrderedLocusNames=b3947, JW5555;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=16397293; DOI=10.1093/nar/gkj405;
RA Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R.,
RA Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T.,
RA Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H.,
RA Thomson N.R., Wishart D., Wanner B.L.;
RT "Escherichia coli K-12: a cooperatively developed annotation snapshot
RT -- 2005.";
RL Nucleic Acids Res. 34:1-9(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP DISCUSSION OF SEQUENCE, AND FUNCTION.
RX PubMed=7773398; DOI=10.1099/13500872-141-4-961;
RA Reizer J., Reizer A., Saier M.H. Jr.;
RT "Novel phosphotransferase system genes revealed by bacterial genome
RT analysis -- a gene cluster encoding a unique Enzyme I and the proteins of a
RT fructose-like permease system.";
RL Microbiology 141:961-971(1995).
CC -!- FUNCTION: Multifunctional protein that includes general (non sugar-
CC specific) and sugar-specific components of the phosphoenolpyruvate-
CC dependent sugar phosphotransferase system (sugar PTS). This major
CC carbohydrate active transport system catalyzes the phosphorylation of
CC incoming sugar substrates concomitantly with their translocation across
CC the cell membrane. The enzyme II FrwABC PTS system is involved in
CC fructose transport. {ECO:0000305|PubMed:7773398}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-histidyl-[protein] + phosphoenolpyruvate = N(pros)-phospho-
CC L-histidyl-[protein] + pyruvate; Xref=Rhea:RHEA:23880, Rhea:RHEA-
CC COMP:9745, Rhea:RHEA-COMP:9746, ChEBI:CHEBI:15361, ChEBI:CHEBI:29979,
CC ChEBI:CHEBI:58702, ChEBI:CHEBI:64837; EC=2.7.3.9;
CC Evidence={ECO:0000250|UniProtKB:P08839};
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:0000250|UniProtKB:P20966};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P08839};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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-like PTS has
CC no requirement for HPr and Enzyme I; PtsA combines a IIA domain with an
CC Enzyme I and a HPr domains. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC43053.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U00006; AAC43053.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U00096; AAT48236.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77363.1; -; Genomic_DNA.
DR RefSeq; WP_001174077.1; NZ_LN832404.1.
DR RefSeq; YP_026278.1; NC_000913.3.
DR AlphaFoldDB; P32670; -.
DR SMR; P32670; -.
DR BioGRID; 4262062; 11.
DR ComplexPortal; CPX-5994; Frw fuctose-like enzyme II complex.
DR DIP; DIP-10601N; -.
DR STRING; 511145.b3947; -.
DR TCDB; 4.A.2.1.10; the pts fructose-mannitol (fru) family.
DR jPOST; P32670; -.
DR PaxDb; P32670; -.
DR PRIDE; P32670; -.
DR EnsemblBacteria; AAT48236; AAT48236; b3947.
DR EnsemblBacteria; BAE77363; BAE77363; BAE77363.
DR GeneID; 948437; -.
DR KEGG; ecj:JW5555; -.
DR KEGG; eco:b3947; -.
DR PATRIC; fig|511145.12.peg.4069; -.
DR EchoBASE; EB1851; -.
DR eggNOG; COG1080; Bacteria.
DR eggNOG; COG1762; Bacteria.
DR eggNOG; COG1925; Bacteria.
DR HOGENOM; CLU_007308_5_0_6; -.
DR InParanoid; P32670; -.
DR OMA; QHIYGEQ; -.
DR PhylomeDB; P32670; -.
DR BioCyc; EcoCyc:EG11906-MON; -.
DR PRO; PR:P32670; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:1902495; C:transmembrane transporter complex; IC:ComplexPortal.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008965; F:phosphoenolpyruvate-protein phosphotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IC:ComplexPortal.
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; 1.10.274.10; -; 1.
DR Gene3D; 3.20.20.60; -; 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; IPR008279; PEP-util_enz_mobile_dom.
DR InterPro; IPR018274; PEP_util_AS.
DR InterPro; IPR000121; PEP_util_C.
DR InterPro; IPR023151; PEP_util_CS.
DR InterPro; IPR036637; Phosphohistidine_dom_sf.
DR InterPro; IPR016152; PTrfase/Anion_transptr.
DR InterPro; IPR006318; PTS_EI-like.
DR InterPro; IPR002178; PTS_EIIA_type-2_dom.
DR InterPro; IPR008731; PTS_EIN.
DR InterPro; IPR001020; PTS_HPr_His_P_site.
DR InterPro; IPR036618; PtsI_HPr-bd_sf.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR Pfam; PF05524; PEP-utilisers_N; 1.
DR Pfam; PF00391; PEP-utilizers; 1.
DR Pfam; PF02896; PEP-utilizers_C; 1.
DR Pfam; PF00381; PTS-HPr; 1.
DR Pfam; PF00359; PTS_EIIA_2; 1.
DR SUPFAM; SSF47831; SSF47831; 1.
DR SUPFAM; SSF51621; SSF51621; 1.
DR SUPFAM; SSF52009; SSF52009; 1.
DR SUPFAM; SSF55594; SSF55594; 1.
DR SUPFAM; SSF55804; SSF55804; 1.
DR TIGRFAMs; TIGR01417; PTS_I_fam; 1.
DR PROSITE; PS00742; PEP_ENZYMES_2; 1.
DR PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
DR PROSITE; PS51094; PTS_EIIA_TYPE_2; 1.
DR PROSITE; PS51350; PTS_HPR_DOM; 1.
DR PROSITE; PS00369; PTS_HPR_HIS; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Kinase; Magnesium; Metal-binding; Phosphoprotein;
KW Phosphotransferase system; Reference proteome; Sugar transport;
KW Transferase; Transport.
FT CHAIN 1..833
FT /note="Multiphosphoryl transfer protein 2"
FT /id="PRO_0000147094"
FT DOMAIN 2..91
FT /note="HPr"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00681"
FT DOMAIN 688..830
FT /note="PTS EIIA type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00417"
FT REGION 143..653
FT /note="PTS EI"
FT /evidence="ECO:0000305|PubMed:7773398"
FT ACT_SITE 16
FT /note="Tele-phosphohistidine intermediate; for HPr
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00417"
FT ACT_SITE 301
FT /note="Tele-phosphohistidine intermediate; for PTS EI
FT activity"
FT /evidence="ECO:0000250|UniProtKB:P08839,
FT ECO:0000255|PROSITE-ProRule:PRU00417"
FT ACT_SITE 614
FT /note="Proton donor; for EI activity"
FT /evidence="ECO:0000250|UniProtKB:P08839"
FT ACT_SITE 750
FT /note="Tele-phosphohistidine intermediate; for PTS EIIA
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00417"
FT BINDING 408
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000250|UniProtKB:P23533"
FT BINDING 444
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000250|UniProtKB:P08839"
FT BINDING 543
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P08839"
FT BINDING 566..567
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000250|UniProtKB:P08839"
FT BINDING 567
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P08839"
FT BINDING 577
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000250|UniProtKB:P23533"
FT MOD_RES 16
FT /note="Phosphohistidine; by EI"
FT /evidence="ECO:0000305"
FT MOD_RES 301
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000305"
FT MOD_RES 750
FT /note="Phosphohistidine; by HPr"
FT /evidence="ECO:0000305"
SQ SEQUENCE 833 AA; 91774 MW; 8E667F44D29CC732 CRC64;
MALIVEFICE LPNGVHARPA SHVETLCNTF SSQIEWHNLR TDRKGNAKSA LALIGTDTLA
GDNCQLLISG ADEQEAHQRL SQWLRDEFPH CDAPLAEVKS DELEPLPVSL TNLNPQIIRA
RTVCSGSAGG ILTPISSLDL NALGNLPAAK GVDAEQSALE NGLTLVLKNI EFRLLDSDGA
TSAILEAHRS LAGDTSLREH LLAGVSAGLS CAEAIVASAN HFCEEFSRSS SSYLQERALD
VRDVCFQLLQ QIYGEQRFPA PGKLTQPAIC MADELTPSQF LELDKNHLKG LLLKSGGTTS
HTVILARSFN IPTLVGVDID ALTPWQQQTI YIDGNAGAIV VEPGEAVARY YQQEARVQDA
LREQQRVWLT QQARTADGIR IEIAANIAHS VEAQAAFGNG AEGVGLFRTE MLYMDRTSAP
GESELYNIFC QALESANGRS IIVRTMDIGG DKPVDYLNIP AEANPFLGYR AVRIYEEYAS
LFTTQLRSIL RASAHGSLKI MIPMISSMEE ILWVKEKLAE AKQQLRNEHI PFDEKIQLGI
MLEVPSVMFI IDQCCEEIDF FSIGSNDLTQ YLLAVDRDNA KVTRHYNSLN PAFLRALDYA
VQAVHRQGKW IGLCGELGAK GSVLPLLVGL GLDELSMSAP SIPAAKARMA QLDSRECRKL
LNQAMACRTS LEVEHLLAQF RMTQQDAPLV TAECITLESD WRSKEEVLKG MTDNLLLAGR
CRYPRKLEAD LWAREAVFST GLGFSFAIPH SKSEHIEQST ISVARLQAPV RWGDDEAQFI
IMLTLNKHAA GDQHMRIFSR LARRIMHEEF RNALVNAASA DAIASLLQHE LEL
