ID Q5ZRL0_LEGPH Unreviewed; 764 AA.
AC Q5ZRL0;
DT 23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT 23-NOV-2004, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE RecName: Full=phosphoenolpyruvate--protein phosphotransferase {ECO:0000256|ARBA:ARBA00012232};
DE EC=2.7.3.9 {ECO:0000256|ARBA:ARBA00012232};
GN Name=ptsP {ECO:0000313|EMBL:AAU28918.1};
GN OrderedLocusNames=lpg2871 {ECO:0000313|EMBL:AAU28918.1};
OS Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC
OS 33152 / DSM 7513).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=272624 {ECO:0000313|EMBL:AAU28918.1, ECO:0000313|Proteomes:UP000000609};
RN [1] {ECO:0000313|EMBL:AAU28918.1, ECO:0000313|Proteomes:UP000000609}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513
RC {ECO:0000313|Proteomes:UP000000609};
RX PubMed=15448271; DOI=10.1126/science.1099776;
RA Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G.,
RA Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V.,
RA Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A.,
RA Chou I.C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A.,
RA Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A.,
RA Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A.,
RA Russo J.J.;
RT "The genomic sequence of the accidental pathogen Legionella pneumophila.";
RL Science 305:1966-1968(2004).
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC {ECO:0000256|ARBA:ARBA00007837}.
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DR EMBL; AE017354; AAU28918.1; -; Genomic_DNA.
DR RefSeq; WP_010948557.1; NC_002942.5.
DR RefSeq; YP_096865.1; NC_002942.5.
DR AlphaFoldDB; Q5ZRL0; -.
DR STRING; 272624.lpg2871; -.
DR PaxDb; 272624-lpg2871; -.
DR GeneID; 66492043; -.
DR KEGG; lpn:lpg2871; -.
DR PATRIC; fig|272624.6.peg.3058; -.
DR eggNOG; COG3605; Bacteria.
DR HOGENOM; CLU_007308_7_1_6; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000000609; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:InterPro.
DR Gene3D; 3.30.450.40; -; 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; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR InterPro; IPR000121; PEP_util_C.
DR InterPro; IPR023151; PEP_util_CS.
DR InterPro; IPR036637; Phosphohistidine_dom_sf.
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:SF1; PHOSPHOENOLPYRUVATE-DEPENDENT PHOSPHOTRANSFERASE SYSTEM; 1.
DR PANTHER; PTHR46244; PHOSPHOENOLPYRUVATE-PROTEIN PHOSPHOTRANSFERASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF05524; PEP-utilisers_N; 1.
DR Pfam; PF00391; PEP-utilizers; 1.
DR Pfam; PF02896; PEP-utilizers_C; 1.
DR PRINTS; PR01736; PHPHTRNFRASE.
DR SMART; SM00065; GAF; 1.
DR SUPFAM; SSF47831; Enzyme I of the PEP:sugar phosphotransferase system HPr-binding (sub)domain; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR SUPFAM; SSF52009; Phosphohistidine domain; 1.
DR PROSITE; PS00742; PEP_ENZYMES_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphotransferase system {ECO:0000256|ARBA:ARBA00022683};
KW Pyruvate {ECO:0000313|EMBL:AAU28918.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000609};
KW Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AAU28918.1};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 17..164
FT /note="GAF"
FT /evidence="ECO:0000259|SMART:SM00065"
FT COILED 216..250
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 414..441
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 764 AA; 84540 MW; EB3D7F770150730B CRC64;
MLKILKRIVQ DVTAASDLKE ALGILVQRIN TAINAEAVSV YLIDNKNAEY VLIATEGLNK
QAEFRVRIAL DCGLIGLIGR REEPINIENA PSHPDFYHNP LIGEDHLNAF LGVPIIQHRK
LYGVLVVQQL EQRYFDDAEE SFLITLAAQL GGIIAHAEAT GELAELTQPK KGIGVDKVEA
TYTALTGIGS VPGIGIGTAV VVYPPADIDA VPRNPVEELE DEINAFYEAL ETTRDDIRRL
SKRMKETVAE EEHALFDVYL RILDRDSLGA EVEHVIREEK ISAQAALATV IKKHVQQFES
MGDDYLRERA SDFRDLGRRV LAELQRTQRE EIVYPKRTIL IGEEITAAAL AEVPEGQLAG
VVSAKGSNNS HVAILARALG VPTVMGLRGL KVELVSRRAL IVDGYYGHVY ISPSKSLLAE
FKQLAQEEQE LNQSLVSLRD KPAETTDNYR VSLQVNTGLA MDAGLSMSVG AEGVGLYRSE
VPFMSRDRFP SEDEQTIIYR QTLKAFAPRL VTMRTLDIGG DKILPYFPVE EENPYLGWRG
IRITLDHPDV FLIQVRAMMR ASEELDNLRI MLPMVTTLSE VEEAVYLIEQ AFEELVEEGC
EIVKPKIGVM IEVPAAAYLA REMAKRVDFI SVGSNDLTQY LLAVDRNNAR VAALYDPLHP
AMLRTLLKIV EGGHAAGVEV SICGEMASDP LAVILLIAMG FDTLSMNSAS LPRVKWVIRN
FAIANARKIL AEVLEFEHPA EIRFHLQKAL EEEGLGGLIR AGKS
//
