ID   FLER_PSEAE              Reviewed;         473 AA.
AC   Q9I4N3;
DT   13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 151.
DE   RecName: Full=Response regulator protein FleR {ECO:0000303|PubMed:7591148};
GN   Name=fleR {ECO:0000303|PubMed:7591148}; OrderedLocusNames=PA1099;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=PAK;
RX   PubMed=7591148; DOI=10.1128/iai.63.12.4868-4876.1995;
RA   Ritchings B.W., Almira E.C., Lory S., Ramphal R.;
RT   "Cloning and phenotypic characterization of fleS and fleR, new response
RT   regulators of Pseudomonas aeruginosa which regulate motility and adhesion
RT   to mucin.";
RL   Infect. Immun. 63:4868-4876(1995).
RN   [3]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=8876537; DOI=10.1164/ajrccm/154.4_pt_2.s170;
RA   Ramphal R., Arora S.K., Ritchings B.W.;
RT   "Recognition of mucin by the adhesin-flagellar system of Pseudomonas
RT   aeruginosa.";
RL   Am. J. Respir. Crit. Care Med. 154:S170-S174(1996).
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=30877999; DOI=10.1016/j.isci.2019.02.028;
RA   Kollaran A.M., Joge S., Kotian H.S., Badal D., Prakash D., Mishra A.,
RA   Varma M., Singh V.;
RT   "Context-Specific Requirement of Forty-Four Two-Component Loci in
RT   Pseudomonas aeruginosa Swarming.";
RL   IScience 13:305-317(2019).
CC   -!- FUNCTION: Member of the two-component regulatory system FleS/FleR that
CC       regulates the expression of multiple genes involved in flagellar
CC       synthesis, adhesion, swarming, motility and antibiotic resistance
CC       (PubMed:7591148, PubMed:30877999, PubMed:8876537). May function as a
CC       transcriptional activator by direct binding to a cis-acting sequence
CC       upstream of the target genes (Probable). {ECO:0000269|PubMed:30877999,
CC       ECO:0000269|PubMed:7591148, ECO:0000269|PubMed:8876537,
CC       ECO:0000305|PubMed:7591148}.
CC   -!- DISRUPTION PHENOTYPE: Deletion leads to loss of motility due to the
CC       absence of flagella as well as swimming defect (PubMed:7591148,
CC       PubMed:30877999). In addition, mutant possessing pili adheres poorly to
CC       mucins (PubMed:8876537). {ECO:0000269|PubMed:30877999,
CC       ECO:0000269|PubMed:7591148, ECO:0000269|PubMed:8876537}.
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DR   EMBL; AE004091; AAG04488.1; -; Genomic_DNA.
DR   PIR; D83508; D83508.
DR   RefSeq; NP_249790.1; NC_002516.2.
DR   RefSeq; WP_003082202.1; NZ_QZGE01000006.1.
DR   AlphaFoldDB; Q9I4N3; -.
DR   SMR; Q9I4N3; -.
DR   STRING; 287.DR97_838; -.
DR   PaxDb; Q9I4N3; -.
DR   PRIDE; Q9I4N3; -.
DR   EnsemblBacteria; AAG04488; AAG04488; PA1099.
DR   GeneID; 882087; -.
DR   KEGG; pae:PA1099; -.
DR   PATRIC; fig|208964.12.peg.1138; -.
DR   PseudoCAP; PA1099; -.
DR   HOGENOM; CLU_000445_0_0_6; -.
DR   InParanoid; Q9I4N3; -.
DR   OMA; ARYIHQQ; -.
DR   PhylomeDB; Q9I4N3; -.
DR   BioCyc; PAER208964:G1FZ6-1122-MON; -.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:1900191; P:negative regulation of single-species biofilm formation; IMP:PseudoCAP.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR   GO; GO:0045785; P:positive regulation of cell adhesion; IMP:PseudoCAP.
DR   GO; GO:2000155; P:positive regulation of cilium-dependent cell motility; IMP:PseudoCAP.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 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   InterPro; IPR029995; TR_FlbD/FleR/FlgR.
DR   PANTHER; PTHR32071:SF21; PTHR32071:SF21; 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; SSF46689; SSF46689; 1.
DR   SUPFAM; SSF52172; SSF52172; 1.
DR   SUPFAM; SSF52540; SSF52540; 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   3: Inferred from homology;
KW   ATP-binding; DNA-binding; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation;
KW   Two-component regulatory system.
FT   CHAIN           1..473
FT                   /note="Response regulator protein FleR"
FT                   /id="PRO_0000448538"
FT   DOMAIN          4..118
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   DOMAIN          130..359
FT                   /note="Sigma-54 factor interaction"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT   BINDING         158..165
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT   BINDING         221..230
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT   MOD_RES         53
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   473 AA;  51234 MW;  BCD508ECD7D0B244 CRC64;
     MAAKVLLVED DRALREALSD TLLLGGHEFV AVDSAEAALP VLAREAFSLV ISDVNMPGMD
     GHQLLGLIRT RYPHLPVLLM TAYGAVDRAV EAMRQGAADY LVKPFEARAL LDLVARHALG
     QLPGSEEDGP VALEPASRQL LELAARVARS DSTVLISGES GTGKEVLANY IHQQSPRAGK
     PFIAINCAAI PDNMLEATLF GHEKGSFTGA IAAQPGKFEL ADGGTILLDE ISEMPLGLQA
     KLLRVLQERE VERVGARKPI NLDIRVLATT NRDLAAEVAA GRFREDLYYR LSVFPLAWRP
     LRERPADILP LAERLLRKHS RKMNLGAVAL GPEAAQCLVR HAWPGNVREL DNAIQRALIL
     QQGGLIQPAD LCLTAPIGMP LAAPVPVPMP AMPPATPPSV EIPSPAAGQD ASGALGDDLR
     RREFQVIIDT LRTERGRRKE AAERLGISPR TLRYKLAQMR DAGMDVEAYL YAI