ID PT1_STRMU Reviewed; 577 AA. AC P45595; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 28-NOV-2002, sequence version 2. DT 04-NOV-2026, entry version 152. DE RecName: Full=Phosphoenolpyruvate-protein phosphotransferase {ECO:0000250|UniProtKB:P08839}; DE EC=2.7.3.9 {ECO:0000250|UniProtKB:P08839}; DE AltName: Full=Phosphotransferase system, enzyme I {ECO:0000250|UniProtKB:P08839}; GN Name=ptsI; OrderedLocusNames=SMU_675; OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159). OC Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=210007; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=NG5 / Serotype c; RX PubMed=8132321; DOI=10.1128/iai.62.4.1156-1165.1994; RA Boyd D.A., Cvitkovitch D.G., Hamilton I.R.; RT "Sequence and expression of the genes for HPr (ptsH) and enzyme I (ptsI) of RT the phosphoenolpyruvate-dependent phosphotransferase transport system from RT Streptococcus mutans."; RL Infect. Immun. 62:1156-1165(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700610 / UA159; RX PubMed=12397186; DOI=10.1073/pnas.172501299; RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B., RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S., RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.; RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental RT pathogen."; RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002). CC -!- FUNCTION: General (non sugar-specific) component of the CC phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar CC PTS). This major carbohydrate active-transport system catalyzes the CC phosphorylation of incoming sugar substrates concomitantly with their CC translocation across the cell membrane. Enzyme I transfers the CC phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl CC carrier protein (HPr). {ECO:0000250|UniProtKB:P08839}. 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 -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P08839}; CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P08839}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- DOMAIN: The N-terminal domain contains the HPr binding site, the CC central domain the pyrophosphate/phosphate carrier histidine, and the CC C-terminal domain the pyruvate binding site. CC {ECO:0000250|UniProtKB:P08839}. CC -!- MISCELLANEOUS: The reaction takes place in three steps, mediated by a CC phosphocarrier histidine residue located on the surface of the central CC domain. The two first partial reactions are catalyzed at an active site CC located on the N-terminal domain, and the third partial reaction is CC catalyzed at an active site located on the C-terminal domain. For CC catalytic turnover, the central domain swivels from the concave surface CC of the N-terminal domain to that of the C-terminal domain. CC {ECO:0000250|UniProtKB:P08839}. CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L15191; AAA91093.1; -; Genomic_DNA. DR EMBL; AE014133; AAN58409.1; -; Genomic_DNA. DR RefSeq; WP_002262985.1; NC_004350.2. DR AlphaFoldDB; P45595; -. DR SMR; P45595; -. DR STRING; 210007.SMU_675; -. DR KEGG; smu:SMU_675; -. DR PATRIC; fig|210007.7.peg.600; -. DR eggNOG; COG1080; Bacteria. DR HOGENOM; CLU_007308_7_0_9; -. DR OMA; AADPLMI; -. DR OrthoDB; 9765468at2; -. DR PhylomeDB; P45595; -. DR Proteomes; UP000002512; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008965; F:phosphoenolpyruvate-protein phosphotransferase activity; ISS:UniProtKB. DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:InterPro. DR FunFam; 1.10.274.10:FF:000001; Phosphoenolpyruvate-protein phosphotransferase; 1. DR FunFam; 3.20.20.60:FF:000007; Phosphoenolpyruvate-protein phosphotransferase; 1. DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1. DR Gene3D; 3.50.30.10; Phosphohistidine domain; 1. DR Gene3D; 1.10.274.10; PtsI, HPr-binding domain; 1. DR InterPro; IPR008279; PEP-util_enz_mobile_dom. DR InterPro; IPR050499; PEP-utilizing_PTS_enzyme. 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; IPR024692; PTS_EI. DR InterPro; IPR006318; PTS_EI-like. DR InterPro; IPR008731; PTS_EIN. DR InterPro; IPR036618; PtsI_HPr-bd_sf. DR InterPro; IPR015813; Pyrv/PenolPyrv_kinase-like_dom. DR InterPro; IPR040442; Pyrv_kinase-like_dom_sf. DR NCBIfam; TIGR01417; PTS_I_fam; 1. DR PANTHER; PTHR46244; PHOSPHOENOLPYRUVATE-PROTEIN PHOSPHOTRANSFERASE; 1. DR PANTHER; PTHR46244:SF3; PHOSPHOENOLPYRUVATE-PROTEIN PHOSPHOTRANSFERASE; 1. DR Pfam; PF05524; PEP-utilisers_N; 1. DR Pfam; PF00391; PEP-utilizers; 1. DR Pfam; PF02896; PEP-utilizers_C; 1. DR PIRSF; PIRSF000732; PTS_enzyme_I; 1. DR PRINTS; PR01736; PHPHTRNFRASE. DR SUPFAM; SSF47831; Enzyme I of the PEP:sugar phosphotransferase system HPr-binding (sub)domain; 1. DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1. DR SUPFAM; SSF52009; Phosphohistidine domain; 1. DR PROSITE; PS00742; PEP_ENZYMES_2; 1. DR PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1. PE 3: Inferred from homology; KW Cytoplasm; Kinase; Magnesium; Metal-binding; Phosphotransferase system; KW Reference proteome; Sugar transport; Transferase; Transport. FT CHAIN 1..577 FT /note="Phosphoenolpyruvate-protein phosphotransferase" FT /id="PRO_0000147092" FT ACT_SITE 191 FT /note="Tele-phosphohistidine intermediate" FT /evidence="ECO:0000250|UniProtKB:P08839" FT ACT_SITE 506 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:P08839" FT BINDING 298 FT /ligand="phosphoenolpyruvate" FT /ligand_id="ChEBI:CHEBI:58702" FT /evidence="ECO:0000250|UniProtKB:P23533" FT BINDING 334 FT /ligand="phosphoenolpyruvate" FT /ligand_id="ChEBI:CHEBI:58702" FT /evidence="ECO:0000250|UniProtKB:P08839" FT BINDING 435 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P08839" FT BINDING 458..459 FT /ligand="phosphoenolpyruvate" FT /ligand_id="ChEBI:CHEBI:58702" FT /evidence="ECO:0000250|UniProtKB:P08839" FT BINDING 459 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P08839" FT BINDING 469 FT /ligand="phosphoenolpyruvate" FT /ligand_id="ChEBI:CHEBI:58702" FT /evidence="ECO:0000250|UniProtKB:P23533" FT CONFLICT 547 FT /note="D -> A (in Ref. 1; AAA91093)" FT /evidence="ECO:0000305" SQ SEQUENCE 577 AA; 63398 MW; EE20E49B60FF8FE2 CRC64; MTEMLKGIAA SDGVAVAKAY LLVQPDLTFE TVSVTDTQAE EARLDAALEA SQNELSLIRQ KAVDTLGEEA AAVFDAHLMV LADPEMIGQI KETIRTKEVN AESALKEVTD MFVTLFENME DNPYMQERAA DIRDVAKRVL AHLLGVELPN PATISEESIV IAHDLTPSDT AQLDANYVKA FVTNIGGRTS HSAIMARTLE IAAVLGTNDI TERVKNGDIV AVNGITGQVI INPTEDQIAE FKAAGETYAK QKAEWALLKD AETVTADGKH FELAANIGTP KDVEGVNNNG AEAVGLYRTE FLYMDSQDFP TEDEQYEAYK AVLEGMNGKP VVVRTMDIGG DKELPYFDLP KEMNPFLGFR ALRISISETG NQMFRTQLRA LLRASVHGQL RIMFPMVALL NEFRKAKGIL EEEKANLKAE GVAVSDDIQV GIMIEIPAAA MLADQFAKEV DFFSIGTNDL IQYTMAADRM NEQVSYLYQP YNPSILRLVD HVVKAAHAEG KWAGMCGEMA GDQTAVPLLV GIGLDEFSMS ATSVLRTRSL MKKLDTDKMQ ELAQRALTEC ATMEEVLELE KEYIDFD //