PHOQ_SALTU
ID PHOQ_SALTU Reviewed; 487 AA.
AC F5ZP94;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Virulence sensor histidine kinase PhoQ;
DE EC=2.7.13.3;
DE EC=3.1.3.-;
DE AltName: Full=Sensor histidine protein kinase/phosphatase PhoQ;
GN Name=phoQ; OrderedLocusNames=STMUK_1198;
OS Salmonella typhimurium (strain ATCC 68169 / UK-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=990282;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 68169 / UK-1;
RX PubMed=21622747; DOI=10.1128/jb.05224-11;
RA Luo Y., Kong Q., Yang J., Golden G., Wanda S.Y., Jensen R.V., Ernst P.B.,
RA Curtiss R. III;
RT "Complete genome sequence of the universal killer Salmonella enterica
RT serovar typhimurium UK-1 (ATCC 68169).";
RL J. Bacteriol. 193:4035-4036(2011).
RN [2]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 68169 / UK-1;
RX PubMed=9573193; DOI=10.1128/jb.180.9.2409-2417.1998;
RA Bearson B.L., Wilson L., Foster J.W.;
RT "A low pH-inducible, PhoPQ-dependent acid tolerance response protects
RT Salmonella typhimurium against inorganic acid stress.";
RL J. Bacteriol. 180:2409-2417(1998).
CC -!- FUNCTION: Member of the two-component regulatory system PhoP/PhoQ which
CC regulates the expression of genes involved in virulence, adaptation to
CC acidic and low Mg(2+) environments and resistance to host defense
CC antimicrobial peptides. Essential for intramacrophage survival of
CC S.typhimurium. In low periplasmic Mg(2+), PhoQ functions as a membrane-
CC associated protein kinase that undergoes autophosphorylation and
CC subsequently transfers the phosphate to PhoP, resulting in the
CC expression of PhoP-activated genes (PAG) and repression of PhoP-
CC repressed genes (PRG). In high periplasmic Mg(2+), acts as a protein
CC phosphatase that dephosphorylates phospho-PhoP, resulting in the
CC repression of PAG and may lead to expression of some PRG. Essential for
CC transcription of spiC inside macrophages by controlling the expression
CC of the two-component regulatory system SsrB/SpiR (SsrA) and Pir at
CC transcriptional and post-transcriptional levels respectively. Promotes
CC expression of the two-component regulatory system PmrA/PmrB via
CC activation of pmrD gene. Is required to attenuate bacterial growth
CC within fibroblast cells and to enhance bacterial resistance to bile in
CC intestinal cells. Negatively regulates prgH, which is required for
CC invasion of epithelial cells (Probable). Involved in acid tolerance.
CC {ECO:0000269|PubMed:9573193, ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250};
CC Note=Binds up to 3 divalent metal cations. {ECO:0000250};
CC -!- SUBUNIT: Homodimer; probably dimerizes via the cytoplasmic domain.
CC Interacts with MgrB in the periplasm, altering its activity and that of
CC downstream effector PhoP (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- INDUCTION: The phoP/phoQ operon is positively autoregulated by both
CC PhoP and PhoQ in a Mg(2+)-dependent manner. Induced by low pH.
CC {ECO:0000269|PubMed:9573193}.
CC -!- DISRUPTION PHENOTYPE: Decreased tolerance to acid stress.
CC {ECO:0000269|PubMed:9573193}.
CC -!- MISCELLANEOUS: Substitutions experiments show that amino acid Thr-48
CC may be involved in the conformational changes responsible for the
CC balance between kinase-dominant state and phosphatase-dominant state.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: The PhoP/PhoQ-signaling cascade, which activates
CC virulence membrane genes (pagC, pagO, pagD, pagK, pgtE and phoN), is
CC induced by cationic antimicrobial peptides (CAMP) (polymyxin, alpha-
CC helical peptide C18G and sheet peptide protegrin-1) at sublethal
CC concentrations. {ECO:0000305}.
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DR EMBL; CP002614; AEF07104.1; -; Genomic_DNA.
DR RefSeq; WP_001031687.1; NC_016863.1.
DR AlphaFoldDB; F5ZP94; -.
DR SMR; F5ZP94; -.
DR KEGG; sej:STMUK_1198; -.
DR PATRIC; fig|990282.4.peg.1249; -.
DR HOGENOM; CLU_000445_42_0_6; -.
DR Proteomes; UP000008278; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR Gene3D; 3.30.450.140; -; 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; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR015014; PhoQ_Sensor.
DR InterPro; IPR038429; PhoQ_Sensor_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF08918; PhoQ_Sensor; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell inner membrane; Cell membrane; Growth regulation;
KW Hydrolase; Kinase; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Protein phosphatase; Transferase; Transmembrane;
KW Transmembrane helix; Two-component regulatory system; Virulence.
FT CHAIN 1..487
FT /note="Virulence sensor histidine kinase PhoQ"
FT /id="PRO_0000424538"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 215..266
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 274..481
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT BINDING 151
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 152
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 386..394
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 386
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 416..421
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 435..447
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 443
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT SITE 202
FT /note="Plays a critical role in the switching between
FT kinase and phosphatase states"
FT /evidence="ECO:0000250"
FT MOD_RES 277
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ SEQUENCE 487 AA; 55467 MW; BDCFEFC56F4CA058 CRC64;
MNKFARHFLP LSLRVRFLLA TAGVVLVLSL AYGIVALVGY SVSFDKTTFR LLRGESNLFY
TLAKWENNKI SVELPENLDM QSPTMTLIYD ETGKLLWTQR NIPWLIKSIQ PEWLKTNGFH
EIETNVDATS TLLSEDHSAQ EKLKEVREDD DDAEMTHSVA VNIYPATARM PQLTIVVVDT
IPIELKRSYM VWSWFVYVLA ANLLLVIPLL WIAAWWSLRP IEALAREVRE LEDHHREMLN
PETTRELTSL VRNLNQLLKS ERERYNKYRT TLTDLTHSLK TPLAVLQSTL RSLRNEKMSV
SKAEPVMLEQ ISRISQQIGY YLHRASMRGS GVLLSRELHP VAPLLDNLIS ALNKVYQRKG
VNISMDISPE ISFVGEQNDF VEVMGNVLDN ACKYCLEFVE ISARQTDDHL HIFVEDDGPG
IPHSKRSLVF DRGQRADTLR PGQGVGLAVA REITEQYAGQ IIASDSLLGG ARMEVVFGRQ
HPTQKEE
