PT1_STREI
ID PT1_STREI Reviewed; 577 AA.
AC Q9WXK9;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 100.
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;
OS Streptococcus equinus (Streptococcus bovis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1335;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 700410 / JB1;
RX PubMed=12610726; DOI=10.1007/s00203-003-0516-9;
RA Asanuma N., Hino T.;
RT "Molecular characterization of HPr and related enzymes, and regulation of
RT HPr phosphorylation in the ruminal bacterium Streptococcus bovis.";
RL Arch. Microbiol. 179:205-213(2003).
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 -!- INDUCTION: Transcription of ptsI appears to be regulated in response to
CC sugars supplied, i.e. is four-fold lower when cells were grown on
CC lactose than when grown on glucose.
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}.
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DR EMBL; AB027569; BAA78049.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9WXK9; -.
DR SMR; Q9WXK9; -.
DR STRING; 1335.A6J79_06895; -.
DR PRIDE; Q9WXK9; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.274.10; -; 1.
DR Gene3D; 3.20.20.60; -; 1.
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; 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 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 SUPFAM; SSF47831; SSF47831; 1.
DR SUPFAM; SSF51621; SSF51621; 1.
DR SUPFAM; SSF52009; SSF52009; 1.
DR TIGRFAMs; TIGR01417; PTS_I_fam; 1.
DR PROSITE; PS00742; PEP_ENZYMES_2; 1.
DR PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Kinase; Magnesium; Metal-binding; Phosphotransferase system;
KW Sugar transport; Transferase; Transport.
FT CHAIN 1..577
FT /note="Phosphoenolpyruvate-protein phosphotransferase"
FT /id="PRO_0000147090"
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"
SQ SEQUENCE 577 AA; 63219 MW; 989FF58D1B6DDD12 CRC64;
MTEMLKGIAA SDGVAVAKAY LLVQPDLSFE TVTVEDTSAE EARLDAALKA SQDELSIIRE
KAVETLGEEA AAVFDAHLMV LADPEMISQI KETIRAKQTN AEAGLKEVTD MFITIFEGME
DNPYMQERAA DIRDVAKRVL AHLLGAKLPN PATIDEESIV IAHDLTPSDT AQLNKQFVKA
FVTNIGGRTS HSAIMARTLE IAAVLGTNDI TSRVKDGDIV AVNGITGEVI INPTDEQVAE
FKAAGEAYAK QKAEWALLKD AKTVTADGKH FELAANIGTP KDVEGVNANG AEAVGLYRTE
FLYMDSQDFP TEDEQYEAYK AVLEGMNGKP VVVRTMDIGG DKELPYLDLP KEMNPFLGFR
ALRISISETG NAMFRTQIRA LLRASVHGQL RIMFPMVALL KEFRAAKAIF DEEKANLKAE
GVAVSDDIQV GIMIEIPAAA MLADQFAKEV DFFSIGTNDL IQYTMAADRM NEQVSYLYQP
YNPSILRLIN NVIKAAHAEG KWVGMCGEMA GDQKAVPLLV EMGLDEFSMS ATSILRTRSL
MKKLDTAKMQ EYANRALTEC STMEEVLELS KEYVNVD
