PHOQ_PSEAE
ID PHOQ_PSEAE Reviewed; 448 AA.
AC Q9I4F8;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Two-component sensor PhoQ {ECO:0000303|PubMed:10564474};
DE EC=2.7.13.3 {ECO:0000250|UniProtKB:Q8Z7H3};
DE Flags: Precursor;
GN Name=phoQ; OrderedLocusNames=PA1180;
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.
RX PubMed=10564474; DOI=10.1046/j.1365-2958.1999.01600.x;
RA Macfarlane E.L., Kwasnicka A., Ochs M.M., Hancock R.E.;
RT "PhoP-PhoQ homologues in Pseudomonas aeruginosa regulate expression of the
RT outer-membrane protein OprH and polymyxin B resistance.";
RL Mol. Microbiol. 34:305-316(1999).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11021929; DOI=10.1099/00221287-146-10-2543;
RA Macfarlane E.L.A., Kwasnicka A., Hancock R.E.W.;
RT "Role of Pseudomonas aeruginosa PhoP-phoQ in resistance to antimicrobial
RT cationic peptides and aminoglycosides.";
RL Microbiology 146:2543-2554(2000).
RN [4]
RP FUNCTION.
RX PubMed=16707691; DOI=10.1128/jb.00053-06;
RA McPhee J.B., Bains M., Winsor G., Lewenza S., Kwasnicka A., Brazas M.D.,
RA Brinkman F.S., Hancock R.E.;
RT "Contribution of the PhoP-PhoQ and PmrA-PmrB two-component regulatory
RT systems to Mg2+-induced gene regulation in Pseudomonas aeruginosa.";
RL J. Bacteriol. 188:3995-4006(2006).
CC -!- FUNCTION: Member of the two-component regulatory system PhoP/PhoQ that
CC plays a role in the regulation of resistance towards polymyxin B and
CC cationic antimicrobial peptides in response to limiting concentrations
CC of Mg(2+) (PubMed:10564474, PubMed:11021929, PubMed:16707691). May
CC function as a membrane-associated protein kinase that phosphorylates
CC PhoP in response to environmental signals leading to activation of
CC specific gene promoters (Probable). {ECO:0000269|PubMed:10564474,
CC ECO:0000269|PubMed:11021929, ECO:0000269|PubMed:16707691,
CC ECO:0000305|PubMed:10564474}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000250|UniProtKB:Q8Z7H3};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant displays significantly lower
CC virulence than the wild-type strain (PubMed:10564474). Also exhibits a
CC constitutive polymyxin B resistance (PubMed:11021929).
CC {ECO:0000269|PubMed:10564474, ECO:0000269|PubMed:11021929}.
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DR EMBL; AE004091; AAG04569.1; -; Genomic_DNA.
DR PIR; A83498; A83498.
DR RefSeq; NP_249871.1; NC_002516.2.
DR RefSeq; WP_003082438.1; NZ_QZGE01000006.1.
DR AlphaFoldDB; Q9I4F8; -.
DR SMR; Q9I4F8; -.
DR STRING; 287.DR97_754; -.
DR PaxDb; Q9I4F8; -.
DR PRIDE; Q9I4F8; -.
DR DNASU; 879187; -.
DR EnsemblBacteria; AAG04569; AAG04569; PA1180.
DR GeneID; 879187; -.
DR KEGG; pae:PA1180; -.
DR PATRIC; fig|208964.12.peg.1225; -.
DR PseudoCAP; PA1180; -.
DR HOGENOM; CLU_000445_42_2_6; -.
DR InParanoid; Q9I4F8; -.
DR OMA; FFVYDVE; -.
DR PhylomeDB; Q9I4F8; -.
DR BioCyc; PAER208964:G1FZ6-1205-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IBA:GO_Central.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR Pfam; PF02518; HATPase_c; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Membrane; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Signal; Transferase; Transmembrane;
KW Transmembrane helix; Two-component regulatory system.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..448
FT /note="Two-component sensor PhoQ"
FT /evidence="ECO:0000255"
FT /id="PRO_0000449421"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 186..237
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 245..448
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 248
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ SEQUENCE 448 AA; 50280 MW; 91FD3363282DFB24 CRC64;
MIRSLRIRLM LGAAALAVLF MLALLPALQR AFGIALENTI EQRLAADVAT LVSAARVEKG
RLVMPEHLPV EEFNLPEAKV LGYIYDQNGD LLWRSTSAAD ESINYTPRYD GRGNEFHTTR
DAKGEEFFVF DVEIDLLRGK QAAYSIVTMQ SVSEFESLLK GFREQLYLWL GGALLVLLGL
LWLGLTWGFR AMRGLSSELD QIESGERESL SEEHPRELLR LTHSLNRLLR SEHKQRERYR
HSLGDLAHSL KTPLAVLQGV GDQLAEEPGN REQVRVLQGQ IERMSQQIGY QLQRASLRKS
GLVRHREQLA PLVETLCDAL DKVYRDKRVS LQRDFSPSFS VPVERGALLE LLGNLLENAY
RLCLGRVRVG ARLGPGYSEL WVEDDGPGVP AEQRARIIRR GERADTQHPG QGIGLAVALD
IIESYDGELS LDDSELGGAC FRIRFATV
