ID F2I5V4_AERUA Unreviewed; 574 AA.
AC F2I5V4; A0A9Q4DAQ0;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 71.
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=ptsP {ECO:0000313|EMBL:AEA01168.1};
GN OrderedLocusNames=HMPREF9243_1441 {ECO:0000313|EMBL:AEA01168.1};
OS Aerococcus urinae (strain CCUG 59500 / ACS-120-V-Col10a).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Aerococcus;
OC Aerococcus incertae sedis.
OX NCBI_TaxID=2976812 {ECO:0000313|EMBL:AEA01168.1, ECO:0000313|Proteomes:UP000008129};
RN [1] {ECO:0000313|Proteomes:UP000008129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACS-120-V-Col10a {ECO:0000313|Proteomes:UP000008129};
RA Durkin A.S., Madupu R., Radune D., Hostetler J., Torralba M., Gillis M.,
RA Methe B., Sutton G., Nelson K.E.;
RT "Complete genome sequence of Aerococcus urinae strain ACS-120-V-Col10a.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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; CP002512; AEA01168.1; -; Genomic_DNA.
DR RefSeq; WP_013669403.1; NZ_JAOTMI010000022.1.
DR AlphaFoldDB; F2I5V4; -.
DR STRING; 866775.HMPREF9243_1441; -.
DR KEGG; aur:HMPREF9243_1441; -.
DR PATRIC; fig|866775.3.peg.1348; -.
DR eggNOG; COG1080; Bacteria.
DR HOGENOM; CLU_007308_7_0_9; -.
DR Proteomes; UP000008129; 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 Coiled coil {ECO:0000256|SAM:Coils};
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}; Pyruvate {ECO:0000313|EMBL:AEA01168.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008129};
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 5..127
FT /note="Phosphotransferase system enzyme I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF05524"
FT DOMAIN 153..225
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 252..541
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT COILED 26..53
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 189
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000732-1"
FT ACT_SITE 502
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000732-1"
FT BINDING 296
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|PIRSR:PIRSR000732-2"
FT BINDING 332
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|PIRSR:PIRSR000732-2"
FT BINDING 431
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000732-3"
FT BINDING 454..455
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|PIRSR:PIRSR000732-2"
FT BINDING 455
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000732-3"
FT BINDING 465
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|PIRSR:PIRSR000732-2"
SQ SEQUENCE 574 AA; 63702 MW; 3997C30C0A10C086 CRC64;
MEKLKGIGAS DGYAIAKAFL LEQPDLSFEE GKVEDADAEI DRLTKAIDDS RIEIAKIKVI
AQERLSEEEA GVFDAHLQML DDPEMIATYQ QKIKDENLDA QTAVRQTADG FIAIFKAMED
NPYMQERAAD IKDVTDRLIA HLIGAKIPNL SLIDEDAIVI APDLTPSDTA QLNKYVKGFV
TDIGGRTSHS AIMARSLEVA AVVGTTSASE AVSDGDLVIV DGFEGEVLIN PDQATVDSYK
DKAKAYQKQK LEWESLKDAD SLTKDGKQFE IVANIGSPKD LPGVHENGAE GVGLYRTEFL
YMDSDHFPTE EEQFEAYKEV LESLNGKNVV IRTMDIGGDK KLPYLPLPEE LNPFLGYRAI
RICLRETDMF RTQLRALLRA SAYGKLSIMF PMVATLEEWR QAKALYEEER QKLIDEGVEV
ADNIQVGIMI EIPAAAVLAD QFAKEVDFFS IGTNDLIQYT MAADRMNNNI SYLYQPYNPA
VLRLINYVIQ ASHKEGKWTG MCGEVAGDQT AIPLLVGMGL DEFSMSATSI LKSRSLMARL
DSKECEELAH KAMNEKTSSE EVAEMVHDYV SKLD
//
