ID Q99Z66_STRP1 Unreviewed; 577 AA.
AC Q99Z66; Q48Y34;
DT 01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2001, sequence version 1.
DT 27-MAR-2024, entry version 159.
DE RecName: Full=Phosphoenolpyruvate-protein phosphotransferase {ECO:0000256|ARBA:ARBA00016544, ECO:0000256|PIRNR:PIRNR000732};
DE EC=2.7.3.9 {ECO:0000256|ARBA:ARBA00012232, ECO:0000256|PIRNR:PIRNR000732};
DE AltName: Full=Phosphotransferase system, enzyme I {ECO:0000256|ARBA:ARBA00033235, ECO:0000256|PIRNR:PIRNR000732};
GN Name=pstI {ECO:0000313|EMBL:AAK34199.1};
GN OrderedLocusNames=SPy_1372 {ECO:0000313|EMBL:AAK34199.1};
OS Streptococcus pyogenes serotype M1.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=301447 {ECO:0000313|EMBL:AAK34199.1, ECO:0000313|Proteomes:UP000000750};
RN [1] {ECO:0000313|EMBL:AAK34199.1, ECO:0000313|Proteomes:UP000000750}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700294 / SF370 / Serotype M1
RC {ECO:0000313|Proteomes:UP000000750};
RX PubMed=11296296; DOI=10.1073/pnas.071559398;
RA Ferretti J.J., McShan W.M., Adjic D., Savic D., Savic G., Lyon K.,
RA Primeaux C., Sezate S.S., Surorov A.N., Kenton S., Lai H., Lin S., Qian Y.,
RA Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J., Yuan X.,
RA Clifton S.W., Roe B.A., McLaughlin R.E.;
RT "Complete genome sequence of an M1 strain of Streptococcus pyogenes.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001).
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:0000256|ARBA:ARBA00002728,
CC ECO:0000256|PIRNR:PIRNR000732}.
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:0000256|ARBA:ARBA00000683,
CC ECO:0000256|PIRNR:PIRNR000732};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|PIRNR:PIRNR000732, ECO:0000256|PIRSR:PIRSR000732-3};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|PIRNR:PIRNR000732}.
CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC {ECO:0000256|ARBA:ARBA00007837, ECO:0000256|PIRNR:PIRNR000732}.
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DR EMBL; AE004092; AAK34199.1; -; Genomic_DNA.
DR RefSeq; NP_269478.1; NC_002737.2.
DR AlphaFoldDB; Q99Z66; -.
DR PaxDb; 1314-HKU360_01153; -.
DR KEGG; spy:SPy_1372; -.
DR PATRIC; fig|160490.10.peg.1198; -.
DR HOGENOM; CLU_007308_7_0_9; -.
DR OMA; DLMINAG; -.
DR PHI-base; PHI:8022; -.
DR Proteomes; UP000000750; Chromosome.
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; 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; 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 {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR000732};
KW Kinase {ECO:0000256|PIRNR:PIRNR000732};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRNR:PIRNR000732};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR000732};
KW Phosphotransferase system {ECO:0000256|ARBA:ARBA00022683,
KW ECO:0000256|PIRNR:PIRNR000732};
KW Reference proteome {ECO:0000313|Proteomes:UP000000750};
KW Sugar transport {ECO:0000256|ARBA:ARBA00022597,
KW ECO:0000256|PIRNR:PIRNR000732};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000732};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR000732}.
FT DOMAIN 6..128
FT /note="Phosphotransferase system enzyme I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF05524"
FT DOMAIN 154..227
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 252..545
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT ACT_SITE 191
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000732-1"
FT ACT_SITE 506
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000732-1"
FT BINDING 298
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|PIRSR:PIRSR000732-2"
FT BINDING 334
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|PIRSR:PIRSR000732-2"
FT BINDING 435
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000732-3"
FT BINDING 458..459
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|PIRSR:PIRSR000732-2"
FT BINDING 459
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000732-3"
FT BINDING 469
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|PIRSR:PIRSR000732-2"
SQ SEQUENCE 577 AA; 63136 MW; D2311F94C26BB7C9 CRC64;
MTEMLKGIAA SDGVAVAKAY LLVQPDLSFE TVTVADTNAE EARLDVALQA AQDELSVIRE
NAVESLGEEA AAVFDAHLMV LADPEMISQV KETIRAKQTN AETGLKEVTD MFITIFEGME
DNPYMQERAA DIRDVAKRVL AHLLGVKLPN PATINEESIV IAHDLTPSDT AQLNKQFVKA
FVTNIGGRTS HSAIMARTLE IAAVLGTNDI TKRVKDGDVI AVNGITGEVI IDPSEDQVLA
FKEAGAAYAK QKAEWSLLKD AHTETADGKH FELAANIGTP KDVEGVNDNG AEAVGLYRTE
FLYMDSQDFP TEDEQYEAYK AVLEGMNGKP VVVRTMDIGG DKELPYFDLP KEMNPFLGFR
ALRISISETG DAMFRTQMRA LLRASVHGQL RIMFPMVALL KEFRAAKAVF DEEKANLLAE
GVAVADDIQV GIMIEIPAAA MLADQFAKEV DFFSIGTNDL IQYTMAADRM NEQVSYLYQP
YNPSILRLIN NVIKAAHAEG KWAGMCGEMA GDQQAVPLLV GMGLDEFSMS ATSVLRTRSL
MKKLDSAKME EYANRALTEC STAEEVLELS KEYVSED
//
