ID A0A0W0XN57_9GAMM Unreviewed; 765 AA.
AC A0A0W0XN57;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
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:KTD45992.1};
GN ORFNames=Lrub_2789 {ECO:0000313|EMBL:KTD45992.1};
OS Legionella rubrilucens.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=458 {ECO:0000313|EMBL:KTD45992.1, ECO:0000313|Proteomes:UP000054608};
RN [1] {ECO:0000313|EMBL:KTD45992.1, ECO:0000313|Proteomes:UP000054608}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WA-270A-C2 {ECO:0000313|EMBL:KTD45992.1,
RC ECO:0000313|Proteomes:UP000054608};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KTD45992.1}.
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DR EMBL; LNYT01000022; KTD45992.1; -; Genomic_DNA.
DR RefSeq; WP_058532734.1; NZ_LNYT01000022.1.
DR AlphaFoldDB; A0A0W0XN57; -.
DR STRING; 458.Lrub_2789; -.
DR PATRIC; fig|458.5.peg.2909; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000054608; Unassembled WGS sequence.
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 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:KTD45992.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054608};
KW Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KTD45992.1};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 17..164
FT /note="GAF"
FT /evidence="ECO:0000259|SMART:SM00065"
SQ SEQUENCE 765 AA; 84766 MW; CC2A0E6396F5A181 CRC64;
MLKILKRIVQ DVTTANHLTE ALDILVQRVR KAVDTDAVSV YLIDSKHAEY VLIATDGLNK
QAQFRVRVGL DNGIIGLVGR REEPINVEDA PNHPDFHHDP LLEEEQFKAF LGVPIIQHRK
LYGVITVQQS ERRCFDDAEE AFLITLAAQL GGIIAHAEAT GELAELTQPK PIGAQKADVV
QTSLSGIGSV PGIGIGSAVV VYPPADIDAV PRIPVEEADV DEEVTTFYDA LQVAREDMQR
LSRRMKSNVA EEEHALFDVY VRILDDESLG AEVEEVIRQE KLSAQAALSV VIKKHVQQFE
SMEDEYLRER ASDFRDLGRR VLAELQRGQR EEITYPRRTV LIGEEIPASA LAEVPKGQLV
GVVSARGANN SHVAILARAL DVPTVMGVRG LKVEQLSGRA IIVDGFLGHI YLSPSKSVLA
EFKKLAKEEE ALNQSLVSLR DKPAETLDNY RISLQVNTGL AMDAGLSMSV GAEGVGLYRS
EIPFMSRDRF PSEDEQYIIY RQILKAFAPR YVTMRTLDIG GDKTLPYFPV EEDNPYLGWR
GIRITLDHPD VFLMQIRAMM RASEELNNLK IMLPMVTTLG EVEEAILLIE QAYRELLEEG
CNIEKPRLGV MVEVPAAVYL ARELAKRVDF LSVGSNDLTQ YLLAVDRNNA RVAGLYDAFH
PAMLQTLMKV VEGGHAAGVE VSICGEMASD PLAVILLMAM GFDILSMNSV SLPRVKWVIR
NFSLANARKI LAEVLEFEHP QAIRLHLQRA LEAEGLGGLI RAGRS
//
