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Entry: A0A078LXQ9_9PSED
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ID   A0A078LXQ9_9PSED        Unreviewed;       757 AA.
AC   A0A078LXQ9;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 43.
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:CDZ95087.1};
GN   ORFNames=BN1079_02419 {ECO:0000313|EMBL:CDZ95087.1};
OS   Pseudomonas saudiphocaensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1499686 {ECO:0000313|EMBL:CDZ95087.1, ECO:0000313|Proteomes:UP000053902};
RN   [1] {ECO:0000313|EMBL:CDZ95087.1, ECO:0000313|Proteomes:UP000053902}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=20_BN {ECO:0000313|EMBL:CDZ95087.1,
RC   ECO:0000313|Proteomes:UP000053902};
RA   Urmite Genomes Urmite Genomes;
RL   Submitted (JUL-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; CCSF01000001; CDZ95087.1; -; Genomic_DNA.
DR   RefSeq; WP_037024616.1; NZ_CCSF01000001.1.
DR   AlphaFoldDB; A0A078LXQ9; -.
DR   STRING; 1499686.BN1079_02419; -.
DR   eggNOG; COG3605; Bacteria.
DR   HOGENOM; CLU_007308_7_1_6; -.
DR   OrthoDB; 9765468at2; -.
DR   Proteomes; UP000053902; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Phosphotransferase system {ECO:0000256|ARBA:ARBA00022683};
KW   Pyruvate {ECO:0000313|EMBL:CDZ95087.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053902};
KW   Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CDZ95087.1};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          17..164
FT                   /note="GAF"
FT                   /evidence="ECO:0000259|SMART:SM00065"
FT   COILED          216..243
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   757 AA;  83340 MW;  4D81458847241B69 CRC64;
     MLGTLRKIVQ EVNAAKDLKA ALGIIVLRVR EAMGSQVCSV YLLDPESDRF VLMATEGLNK
     KAIGKVSMAH NEGLVGLVGS REEPLNLEHA SEHPRYRYFA ETGEERYASF LGAPIIHHRR
     VMGVLVIQQK ERRQFDEGEE AFLVTMSAQL AGVIAHAEAT GSIRGFGRQG KGIQETRFLG
     IAGAPGAAVG SAVVVLPPAD LDVVPDKHIE DIPAELALFE AALEAVRADM RALSQKLSSQ
     MRKEELALFD VYLMMLDDSA LGGEVAAVIR TGQWAQGALR QVVSNHIARF EMMDDDYLRE
     RASDIKDIGR RLLGNLQKAH KQALTYPERT ILVSEELTPA MLGEVPEGRL AGMVSVLGSS
     NSHVAILARA MGIPTVMGAV DLPYSKVDGI ELIVDGTRGE IITNPGKVLR EQYLQLAEQE
     RQLSAGLDVL RELPCETTDG HRIPLWVNTG LLADVVRAQE RGAEGVGLYR TEVPFMIKER
     FPSEKEQMAI YREQLQAFHP LPVTMRTLDI GGDKSLPYFP IKEENPFLGW RGIRVTLDHP
     EIFLLQIRAM LKASVGLNNL RILLPMISGT RELEESLHLI HRAIGEVRDE GMDVQVPPVG
     VMIEVPAAVY LTRELARQVD FISVGSNDLT QYLLAVDRNN PRVADLYDYL HPAVLEALQR
     IVKEAHEEGR PVSICGEMAG DPAAAMLLLA MGFDSLSMNA TNLPRVKWLL RQISMQTAKD
     LLARVMTIDS PEVTHATVQL TLRNLGLDKL TNPSAAV
//
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