ID A0A098GAC1_9GAMM Unreviewed; 764 AA.
AC A0A098GAC1;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
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:CEG58932.1};
GN ORFNames=LFA_3603 {ECO:0000313|EMBL:CEG58932.1};
OS Legionella fallonii LLAP-10.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=1212491 {ECO:0000313|EMBL:CEG58932.1, ECO:0000313|Proteomes:UP000032430};
RN [1] {ECO:0000313|Proteomes:UP000032430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC700992 {ECO:0000313|Proteomes:UP000032430};
RA Gomez-Valero L.;
RL Submitted (SEP-2014) 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}.
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DR EMBL; LN614827; CEG58932.1; -; Genomic_DNA.
DR RefSeq; WP_045097153.1; NZ_LN614827.1.
DR AlphaFoldDB; A0A098GAC1; -.
DR STRING; 1212491.LFA_3603; -.
DR KEGG; lfa:LFA_3603; -.
DR HOGENOM; CLU_007308_7_1_6; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000032430; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000032430};
KW Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CEG58932.1};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 17..164
FT /note="GAF"
FT /evidence="ECO:0000259|SMART:SM00065"
SQ SEQUENCE 764 AA; 83899 MW; 1B644BCD66FA82EF CRC64;
MLKVLKRIVQ DVTAAKHLKD ALGILVQHIN KAINAEAVSV YLIDNKHAEY VLIATEGLNK
QAEFRVRIAL DNGLVGLIGR REEPINLEDA PSHPDFYHNS LLGEEHLNAF LGVPIIQHRK
LYGVLIVQQV EQRCFDDAEE SFLITLAAQL GGIIAHAEAT GELAELTQPK PLGVAKVEVT
PTALTGIGSV PGIGIGTAVV VYPSADIDAV PRAPAEDLDS EIVAFYQALE AARDDMRRLS
KRMKATVAEE EHALFDVYLR ILDKDSLGAE VEQVIRAEEI SAQAALATVI KKHVAQFEGM
EDDYLRERAS DFRDLGRRVL AELQWSQREE ISYPKKTVLI GEEVTAAALA EVPEGQLAGV
VSAKGSNNSH VAILARALGV PTVMGLRGLK VENIAKRALI VDGYYGHVYV SPSRALLSEF
KVLAQEEQDL NQSLVSLRDK PAETTDSYRV SLQVNTGLAM DAGMSMSVGA EGVGLYRSEV
PFMSRDRFPS EDEQTIIYRQ TLKAFAPRFV TMRTLDIGGD KILPYFPIAE DNPYLGWRGI
RVTLDHPDVF LVQVRAMMRA SEELNNLRIM LPMVTNLSEV EEAAYLIEQA FEELLEEGCV
IEKPKIGVMI EVPAAAYLAR EIAKRVDFIS VGSNDLTQYL LAVDRNNARV AGLYDALHPA
MLRVLLKIVE GGHAAGVEVS ICGEIASDPL AVILLIAMGF DTLSMNSSSL PRVKWVIRNF
AIANARKILA EVLEYEHPAE IRFHLQKALE DEGLGSLIRA GKSS
//
