PHOP_SALT1
ID PHOP_SALT1 Reviewed; 224 AA.
AC D0ZV90;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Virulence transcriptional regulatory protein PhoP;
GN Name=phoP; OrderedLocusNames=STM14_1409;
OS Salmonella typhimurium (strain 14028s / SGSC 2262).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=588858;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=14028s / SGSC 2262;
RX PubMed=19897643; DOI=10.1128/jb.01233-09;
RA Jarvik T., Smillie C., Groisman E.A., Ochman H.;
RT "Short-term signatures of evolutionary change in the Salmonella enterica
RT serovar typhimurium 14028 genome.";
RL J. Bacteriol. 192:560-567(2010).
RN [2]
RP FUNCTION.
RC STRAIN=14028s / SGSC 2262;
RX PubMed=8392513; DOI=10.1128/jb.175.14.4475-4484.1993;
RA Behlau I., Miller S.I.;
RT "A PhoP-repressed gene promotes Salmonella typhimurium invasion of
RT epithelial cells.";
RL J. Bacteriol. 175:4475-4484(1993).
RN [3]
RP AUTOREGULATION.
RC STRAIN=14028s / SGSC 2262;
RX PubMed=7543474; DOI=10.1128/jb.177.15.4364-4371.1995;
RA Soncini F.C., Garcia Vescovi E., Groisman E.A.;
RT "Transcriptional autoregulation of the Salmonella typhimurium phoPQ
RT operon.";
RL J. Bacteriol. 177:4364-4371(1995).
RN [4]
RP REGULATION BY MG(2+).
RC STRAIN=14028s / SGSC 2262;
RX PubMed=8548821; DOI=10.1016/s0092-8674(00)81003-x;
RA Garcia Vescovi E., Soncini F.C., Groisman E.A.;
RT "Mg2+ as an extracellular signal: environmental regulation of Salmonella
RT virulence.";
RL Cell 84:165-174(1996).
RN [5]
RP FUNCTION.
RC STRAIN=14028s / SGSC 2262;
RX PubMed=10084994; DOI=10.1128/iai.67.4.1614-1622.1999;
RA van Velkinburgh J.C., Gunn J.S.;
RT "PhoP-PhoQ-regulated loci are required for enhanced bile resistance in
RT Salmonella spp.";
RL Infect. Immun. 67:1614-1622(1999).
RN [6]
RP FUNCTION.
RC STRAIN=14028s / SGSC 2262;
RX PubMed=10775270; DOI=10.1093/emboj/19.8.1861;
RA Kox L.F.F., Woesten M.M.S.M., Groisman E.A.;
RT "A small protein that mediates the activation of a two-component system by
RT another two-component system.";
RL EMBO J. 19:1861-1872(2000).
RN [7]
RP FUNCTION, AND INDUCTION BY CATIONIC ANTIMICROBIAL PEPTIDES (CAMP).
RC STRAIN=14028s / SGSC 2262;
RX PubMed=14507376; DOI=10.1046/j.1365-2958.2003.03675.x;
RA Bader M.W., Navarre W.W., Shiau W., Nikaido H., Frye J.G., McClelland M.,
RA Fang F.C., Miller S.I.;
RT "Regulation of Salmonella typhimurium virulence gene expression by cationic
RT antimicrobial peptides.";
RL Mol. Microbiol. 50:219-230(2003).
RN [8]
RP INDUCTION, AND PHOSPHORYLATION BY PHOQ.
RC STRAIN=14028s / SGSC 2262;
RX PubMed=16096064; DOI=10.1016/j.cell.2005.05.030;
RA Bader M.W., Sanowar S., Daley M.E., Schneider A.R., Cho U., Xu W.,
RA Klevit R.E., Le Moual H., Miller S.I.;
RT "Recognition of antimicrobial peptides by a bacterial sensor kinase.";
RL Cell 122:461-472(2005).
RN [9]
RP FUNCTION.
RC STRAIN=14028s / SGSC 2262;
RX PubMed=15948951; DOI=10.1111/j.1365-2958.2005.04668.x;
RA Bijlsma J.J.E., Groisman E.A.;
RT "The PhoP/PhoQ system controls the intramacrophage type three secretion
RT system of Salmonella enterica.";
RL Mol. Microbiol. 57:85-96(2005).
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 phosphorylates PhoP,
CC resulting in the expression of PhoP-activated genes (PAG) and
CC repression of PhoP-repressed genes (PRG). In high periplasmic Mg(2+),
CC PhoQ dephosphorylates phospho-PhoP, resulting in the repression of PAG
CC and may lead to expression of some PRG. Essential for transcription of
CC spiC inside macrophages by controlling the expression of the two-
CC component regulatory system SsrB/SpiR (SsrA) and Pir at transcriptional
CC and post-transcriptional levels respectively. Promotes expression of
CC the two-component regulatory system PmrA/PmrB via activation of pmrD
CC gene. Is required to attenuate bacterial growth within fibroblast cells
CC and to enhance bacterial resistance to bile in intestinal cells.
CC Negatively regulates prgH, which is required for invasion of epithelial
CC cells. PhoP uses multiple mechanisms to promote transcription and
CC activates promoters for PAG at low (uM range) Mg(2+) concentrations.
CC Probably involved in acid tolerance. {ECO:0000269|PubMed:10084994,
CC ECO:0000269|PubMed:10775270, ECO:0000269|PubMed:14507376,
CC ECO:0000269|PubMed:15948951, ECO:0000269|PubMed:8392513}.
CC -!- SUBUNIT: Monomer in the inactive, unphosphorylated state and dimer in
CC the active, phosphorylated state. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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. Induced by antimicrobial peptides (similar to those in
CC macrophages) and low Mg(2+) concentrations.
CC {ECO:0000269|PubMed:14507376, ECO:0000269|PubMed:16096064}.
CC -!- PTM: Phosphorylated by PhoQ. {ECO:0000269|PubMed:16096064}.
CC -!- MISCELLANEOUS: PhoP/PhoQ-signaling cascade, which activated virulence
CC membrane proteins (PagC, PagO, PagD, PagK, PgtE and PhoN), is induced
CC by cationic antimicrobial peptides (CAMP) (polymyxin, alpha-helical
CC peptide C18G and sheet peptide protegrin-1) at sublethal
CC concentrations.
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DR EMBL; CP001363; ACY87895.1; -; Genomic_DNA.
DR RefSeq; WP_000986522.1; NZ_CP043402.1.
DR AlphaFoldDB; D0ZV90; -.
DR SMR; D0ZV90; -.
DR IntAct; D0ZV90; 1.
DR EnsemblBacteria; ACY87895; ACY87895; STM14_1409.
DR KEGG; seo:STM14_1409; -.
DR PATRIC; fig|588858.6.peg.1379; -.
DR HOGENOM; CLU_000445_30_1_6; -.
DR OMA; QLWGYPP; -.
DR BioCyc; SENT588858:STM14_RS06665-MON; -.
DR PHI-base; PHI:6110; -.
DR Proteomes; UP000002695; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR CDD; cd00383; trans_reg_C; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR001867; OmpR/PhoB-type_DNA-bd.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR039420; WalR-like.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR48111; PTHR48111; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF00486; Trans_reg_C; 1.
DR SMART; SM00448; REC; 1.
DR SMART; SM00862; Trans_reg_C; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR PROSITE; PS51755; OMPR_PHOB; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW Activator; Cytoplasm; DNA-binding; Growth regulation; Phosphoprotein;
KW Repressor; Transcription; Transcription regulation;
KW Two-component regulatory system; Virulence.
FT CHAIN 1..224
FT /note="Virulence transcriptional regulatory protein PhoP"
FT /id="PRO_0000424530"
FT DOMAIN 3..117
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DNA_BIND 125..223
FT /note="OmpR/PhoB-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01091"
FT MOD_RES 52
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 224 AA; 25633 MW; 3A90B2FDC328C7B2 CRC64;
MMRVLVVEDN ALLRHHLKVQ LQDSGHQVDA AEDAREADYY LNEHLPDIAI VDLGLPDEDG
LSLIRRWRSS DVSLPVLVLT AREGWQDKVE VLSSGADDYV TKPFHIEEVM ARMQALMRRN
SGLASQVINI PPFQVDLSRR ELSVNEEVIK LTAFEYTIME TLIRNNGKVV SKDSLMLQLY
PDAELRESHT IDVLMGRLRK KIQAQYPHDV ITTVRGQGYL FELR
