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Database: UniProt
Entry: Q3KG29_PSEPF
LinkDB: Q3KG29_PSEPF
Original site: Q3KG29_PSEPF 
ID   Q3KG29_PSEPF            Unreviewed;       463 AA.
AC   Q3KG29;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 140.
DE   SubName: Full=Two-component response regulator {ECO:0000313|EMBL:ABA73277.1};
GN   OrderedLocusNames=Pfl01_1534 {ECO:0000313|EMBL:ABA73277.1};
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922 {ECO:0000313|EMBL:ABA73277.1, ECO:0000313|Proteomes:UP000002704};
RN   [1] {ECO:0000313|EMBL:ABA73277.1, ECO:0000313|Proteomes:UP000002704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1 {ECO:0000313|EMBL:ABA73277.1,
RC   ECO:0000313|Proteomes:UP000002704};
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
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DR   EMBL; CP000094; ABA73277.1; -; Genomic_DNA.
DR   RefSeq; WP_011333047.1; NC_007492.2.
DR   AlphaFoldDB; Q3KG29; -.
DR   KEGG; pfo:Pfl01_1534; -.
DR   eggNOG; COG2204; Bacteria.
DR   HOGENOM; CLU_000445_0_0_6; -.
DR   Proteomes; UP000002704; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd00009; AAA; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR002197; HTH_Fis.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR002078; Sigma_54_int.
DR   InterPro; IPR025662; Sigma_54_int_dom_ATP-bd_1.
DR   InterPro; IPR025943; Sigma_54_int_dom_ATP-bd_2.
DR   InterPro; IPR025944; Sigma_54_int_dom_CS.
DR   PANTHER; PTHR32071:SF21; PROPIONATE CATABOLISM OPERON REGULATORY PROTEIN; 1.
DR   PANTHER; PTHR32071; TRANSCRIPTIONAL REGULATORY PROTEIN; 1.
DR   Pfam; PF02954; HTH_8; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   Pfam; PF00158; Sigma54_activat; 1.
DR   PRINTS; PR01590; HTHFIS.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
DR   PROSITE; PS00675; SIGMA54_INTERACT_1; 1.
DR   PROSITE; PS00676; SIGMA54_INTERACT_2; 1.
DR   PROSITE; PS00688; SIGMA54_INTERACT_3; 1.
DR   PROSITE; PS50045; SIGMA54_INTERACT_4; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          4..118
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          130..359
FT                   /note="Sigma-54 factor interaction"
FT                   /evidence="ECO:0000259|PROSITE:PS50045"
FT   MOD_RES         53
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   463 AA;  50398 MW;  A51C7FE0F1F06579 CRC64;
     MGIKVLLVED DRSLREALAD TLLLAGHDYH AVGSAEEALN AVEREAFSLV VSDVNMPGMD
     GHQLLGLLRA RQPQLPVLLM TAHGAVERAV DAMRQGAADY LVKPFEPKAL LDLVARHALG
     SLVASDAEGP VAVEPASAQL LDLAARVARS DSTVLISGES GTGKEVLARY IHQQSHRASQ
     PFIAINCAAI PDNMLEATLF GHEKGSFTGA IAAQAGKFEQ ADGGTILLDE ISEMPLGLQA
     KLLRVLQERE VERVGARKPI TLDIRVVATT NRDLAGEVAA GRFREDLYYR LSVFPLAWRP
     LRERTADILP LAERLLAKHV NKMKHAMAKF SSEAQACLIG YPWPGNVREL DNAVQRALIL
     QQGGLIQPQD FCLSGPALFA PLPAVVPVAP VIREVEIEVD SAGALGDDLR RREFQMIIDT
     LRTERGRRKE AAEKLGISPR TLRYKLAQMR DAGMDVEGYL FAT
//
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