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PHOQ_SALTS
ID   PHOQ_SALTS              Reviewed;         487 AA.
AC   E1WFA0; P14147; Q9L3L1;
DT   13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 1.
DT   03-AUG-2022, entry version 60.
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=SL1344_1168;
OS   Salmonella typhimurium (strain SL1344).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=216597;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF ARG-313.
RC   STRAIN=SL1344;
RX   PubMed=11553591; DOI=10.1128/iai.69.10.6463-6474.2001;
RA   Cano D.A., Martinez-Moya M., Pucciarelli M.G., Groisman E.A., Casadesus J.,
RA   Garcia-del Portillo F.;
RT   "Salmonella enterica serovar Typhimurium response involved in attenuation
RT   of pathogen intracellular proliferation.";
RL   Infect. Immun. 69:6463-6474(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SL1344;
RX   PubMed=22538806; DOI=10.1073/pnas.1201061109;
RA   Kroger C., Dillon S.C., Cameron A.D., Papenfort K., Sivasankaran S.K.,
RA   Hokamp K., Chao Y., Sittka A., Hebrard M., Handler K., Colgan A.,
RA   Leekitcharoenphon P., Langridge G.C., Lohan A.J., Loftus B., Lucchini S.,
RA   Ussery D.W., Dorman C.J., Thomson N.R., Vogel J., Hinton J.C.;
RT   "The transcriptional landscape and small RNAs of Salmonella enterica
RT   serovar Typhimurium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:E1277-E1286(2012).
RN   [3]
RP   REGULATION BY RCSB.
RC   STRAIN=SL1344;
RX   PubMed=15516559; DOI=10.1128/jb.186.22.7481-7489.2004;
RA   Tierrez A., Garcia-del Portillo F.;
RT   "The Salmonella membrane protein IgaA modulates the activity of the RcsC-
RT   YojN-RcsB and PhoP-PhoQ regulons.";
RL   J. Bacteriol. 186:7481-7489(2004).
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. Involved in acid tolerance (Probable).
CC       {ECO:0000305}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3;
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. Repressed by RcsB via sigma
CC       factor RpoS.
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; AJ272210; CAB75592.1; -; Genomic_DNA.
DR   EMBL; FQ312003; CBW17264.1; -; Genomic_DNA.
DR   RefSeq; WP_001031687.1; NZ_QASL01000001.1.
DR   AlphaFoldDB; E1WFA0; -.
DR   SMR; E1WFA0; -.
DR   EnsemblBacteria; CBW17264; CBW17264; SL1344_1168.
DR   KEGG; sey:SL1344_1168; -.
DR   PATRIC; fig|216597.6.peg.1297; -.
DR   HOGENOM; CLU_000445_42_0_6; -.
DR   OMA; TLVFIYD; -.
DR   BioCyc; SENT216597:SL1344_RS06075-MON; -.
DR   Proteomes; UP000008962; 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   1: Evidence at protein 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_0000424537"
FT   TOPO_DOM        1..16
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        17..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        38..193
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        194..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        215..487
FT                   /note="Cytoplasmic"
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"
FT   MUTAGEN         313
FT                   /note="R->W: Increased ability to proliferate within
FT                   fibroblasts."
FT                   /evidence="ECO:0000269|PubMed:11553591"
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
 
 
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