PILR_PSEAE
ID PILR_PSEAE Reviewed; 445 AA.
AC Q00934; Q9HVN2;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Response regulator protein PilR {ECO:0000303|PubMed:30042200};
GN Name=pilR; OrderedLocusNames=PA4547;
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 [GENOMIC DNA].
RC STRAIN=PAK;
RX PubMed=1317379; DOI=10.1128/jb.174.11.3514-3521.1992;
RA Ishimoto K.S., Lory S.;
RT "Identification of pilR, which encodes a transcriptional activator of the
RT Pseudomonas aeruginosa pilin gene.";
RL J. Bacteriol. 174:3514-3521(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=8097014; DOI=10.1111/j.1365-2958.1993.tb01158.x;
RA Hobbs M., Collie E.S.R., Free P.D., Livingston S.P., Mattick J.S.;
RT "PilS and PilR, a two-component transcriptional regulatory system
RT controlling expression of type 4 fimbriae in Pseudomonas aeruginosa.";
RL Mol. Microbiol. 7:669-682(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=PAK;
RX PubMed=7911557; DOI=10.1007/bf00284205;
RA Boyd J.M., Koga T., Lory S.;
RT "Identification and characterization of PilS, an essential regulator of
RT pilin expression in Pseudomonas aeruginosa.";
RL Mol. Gen. Genet. 243:565-574(1994).
RN [4]
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 [5]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=7715443; DOI=10.1111/j.1365-2958.1994.tb01338.x;
RA Jin S., Ishimoto K.S., Lory S.;
RT "PilR, a transcriptional regulator of piliation in Pseudomonas aeruginosa,
RT binds to a cis-acting sequence upstream of the pilin gene promoter.";
RL Mol. Microbiol. 14:1049-1057(1994).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=PAK;
RX PubMed=30042200; DOI=10.1128/mbio.01310-18;
RA Kilmury S.L.N., Burrows L.L.;
RT "The Pseudomonas aeruginosa PilSR Two-Component System Regulates Both
RT Twitching and Swimming Motilities.";
RL MBio 9:0-0(2018).
CC -!- FUNCTION: Member of the two-component regulatory system PilS/PilR that
CC regulates the expression of multiple genes including the type IV pilus
CC (T4P) major subunit PilA (PubMed:8097014, PubMed:7911557). Thereby,
CC plays a major role in the regulation of multiple motility pathways
CC (PubMed:30042200). Upon appropriate environmental signals, the
CC histidine kinase PilS transfers the phosphoryl group onto PilR
CC (PubMed:8097014). In turn, PilR functions as a transcriptional
CC activator by direct binding to a cis-acting sequence upstream of the
CC pilin gene promoter leading to its activation (PubMed:1317379,
CC PubMed:7715443). {ECO:0000269|PubMed:1317379,
CC ECO:0000269|PubMed:30042200, ECO:0000269|PubMed:7715443,
CC ECO:0000269|PubMed:7911557, ECO:0000269|PubMed:8097014}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- PTM: Phosphorylated by PilS. {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant results in changes in swimming,
CC swarming and/or twitching motility associated with virulence in
CC specific hosts. {ECO:0000269|PubMed:30042200}.
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DR EMBL; M83311; AAA25956.1; -; Genomic_DNA.
DR EMBL; Z12154; CAA78139.1; -; Genomic_DNA.
DR EMBL; L22436; AAA20188.1; -; Unassigned_DNA.
DR EMBL; AE004091; AAG07935.1; -; Genomic_DNA.
DR PIR; A41896; A41896.
DR PIR; A83078; A83078.
DR RefSeq; NP_253237.1; NC_002516.2.
DR RefSeq; WP_003094694.1; NZ_QZGE01000004.1.
DR AlphaFoldDB; Q00934; -.
DR SMR; Q00934; -.
DR STRING; 287.DR97_1851; -.
DR PaxDb; Q00934; -.
DR PRIDE; Q00934; -.
DR EnsemblBacteria; AAG07935; AAG07935; PA4547.
DR GeneID; 877622; -.
DR KEGG; pae:PA4547; -.
DR PATRIC; fig|208964.12.peg.4759; -.
DR PseudoCAP; PA4547; -.
DR HOGENOM; CLU_000445_0_6_6; -.
DR InParanoid; Q00934; -.
DR OMA; QAPIYIS; -.
DR PhylomeDB; Q00934; -.
DR BioCyc; PAER208964:G1FZ6-4640-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR GO; GO:0060491; P:regulation of cell projection assembly; 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 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 1: Evidence at protein level;
KW Activator; ATP-binding; Cytoplasm; DNA-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Two-component regulatory system.
FT CHAIN 1..445
FT /note="Response regulator protein PilR"
FT /id="PRO_0000081205"
FT DOMAIN 5..119
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DOMAIN 135..364
FT /note="Sigma-54 factor interaction"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT DNA_BIND 418..437
FT /note="H-T-H motif"
FT /evidence="ECO:0000250"
FT BINDING 163..170
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT BINDING 226..235
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT MOD_RES 11
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT MOD_RES 54
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT VARIANT 108..109
FT /note="LG -> FDF (in strain: PAK)"
FT VARIANT 269
FT /note="V -> L (in strain: PAK)"
FT VARIANT 353
FT /note="R -> G (in strain: PAK)"
SQ SEQUENCE 445 AA; 49737 MW; 9F9A3382A4421FDE CRC64;
MSRQKALIVD DEPDIRELLE ITLGRMKLDT RSARNVKEAR ELLAREPFDL CLTDMRLPDG
SGLDLVQYIQ QRHPQTPVAM ITAYGSLDTA IQALKAGAFD FLTKPVDLGR LRELVATALR
LRNPEAEEAP VDNRLLGESP PMRALRNQIG KLARSQAPVY ISGESGSGKE LVARLIHEQG
PRIERPFVPV NCGAIPSELM ESEFFGHKKG SFTGAIEDKQ GLFQAASGGT LFLDEVADLP
MAMQVKLLRA IQEKAVRAVG GQQEVAVDVR ILCATHKDLA AEVGAGRFRQ DLYYRLNVIE
LRVPPLRERR EDIPLLAERI LKRLAGDTGL PAARLTGDAQ EKLKNYRFPG NVRELENMLE
RAYTLCEDDQ IQPHDLRLAD APGASQEGAA SLSEIDNLED YLEDIERKLI MQALEETRWN
RTAAAQRLGL TFRSMRYRLK KLGID
