PHOP_SALTY
ID PHOP_SALTY Reviewed; 224 AA.
AC P0DM78; P14146;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2013, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Virulence transcriptional regulatory protein PhoP;
DE AltName: Full=Acid shock protein 29;
DE Short=ASP29;
GN Name=phoP; OrderedLocusNames=STM1231;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN VIRULENCE, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=ATCC 14028 / SGSC 2980 / CDC 6516-60 / NCTC 12023, and
RC LT2 / SGSC1412 / ATCC 700720;
RX PubMed=2544889; DOI=10.1073/pnas.86.13.5054;
RA Miller S.I., Kukral A.M., Mekalanos J.J.;
RT "A two-component regulatory system (phoP phoQ) controls Salmonella
RT typhimurium virulence.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:5054-5058(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2674945; DOI=10.1073/pnas.86.18.7077;
RA Groisman E.A., Chiao E., Lipps C.J., Heffron F.;
RT "Salmonella typhimurium phoP virulence gene is a transcriptional
RT regulator.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:7077-7081(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [4]
RP FUNCTION IN ACID TOLERANCE, AND DISRUPTION PHENOTYPE.
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
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).
RN [5]
RP EFFECT OF PHOP OVEREXPRESSION, AND MUTAGENESIS OF ASP-52.
RC STRAIN=ATCC 14028 / SGSC 2980 / CDC 6516-60 / NCTC 12023;
RX PubMed=15060051; DOI=10.1128/jb.186.8.2476-2480.2004;
RA Lejona S., Castelli M.E., Cabeza M.L., Kenney L.J., Garcia Vescovi E.,
RA Soncini F.C.;
RT "PhoP can activate its target genes in a PhoQ-independent manner.";
RL J. Bacteriol. 186:2476-2480(2004).
RN [6]
RP ANALYSIS OF PHOP REGULATORY NETWORK.
RX PubMed=15703297; DOI=10.1073/pnas.0408238102;
RA Zwir I., Shin D., Kato A., Nishino K., Latifi T., Solomon F., Hare J.M.,
RA Huang H., Groisman E.A.;
RT "Dissecting the PhoP regulatory network of Escherichia coli and Salmonella
RT enterica.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:2862-2867(2005).
RN [7]
RP FUNCTION.
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=25972862; DOI=10.3389/fmicb.2015.00396;
RA Baison-Olmo F., Galindo-Moreno M., Ramos-Morales F.;
RT "Host cell type-dependent translocation and PhoP-mediated positive
RT regulation of the effector SseK1 of Salmonella enterica.";
RL Front. Microbiol. 6:396-396(2015).
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 (PubMed:2544889, PubMed:9573193,
CC PubMed:25972862). 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 (Probable). Involved in acid tolerance. {ECO:0000269|PubMed:2544889,
CC ECO:0000269|PubMed:25972862, ECO:0000269|PubMed:9573193, ECO:0000305}.
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.
CC -!- PTM: Phosphorylated and dephosphorylated by PhoQ. {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: 10,000-fold reduction in virulence in male BALB/c
CC mice (for strain ATCC 14028). Decreased tolerance to acid stress.
CC {ECO:0000269|PubMed:2544889, ECO:0000269|PubMed:9573193}.
CC -!- MISCELLANEOUS: PhoP/PhoQ-signaling cascade, which activates 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. {ECO:0000305}.
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DR EMBL; M24424; AAA27188.1; -; Genomic_DNA.
DR EMBL; M25241; AAA27187.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20160.1; -; Genomic_DNA.
DR PIR; A32932; RGEBFT.
DR RefSeq; NP_460201.1; NC_003197.2.
DR RefSeq; WP_000986522.1; NC_003197.2.
DR AlphaFoldDB; P0DM78; -.
DR SMR; P0DM78; -.
DR STRING; 99287.STM1231; -.
DR PaxDb; P0DM78; -.
DR EnsemblBacteria; AAL20160; AAL20160; STM1231.
DR GeneID; 1252749; -.
DR KEGG; stm:STM1231; -.
DR PATRIC; fig|99287.12.peg.1302; -.
DR HOGENOM; CLU_000445_30_1_6; -.
DR OMA; QLWGYPP; -.
DR PhylomeDB; P0DM78; -.
DR BioCyc; SENT99287:STM1231-MON; -.
DR PHI-base; PHI:2674; -.
DR PHI-base; PHI:6591; -.
DR Proteomes; UP000001014; Chromosome.
DR CollecTF; EXPREG_000008e0; -.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0032993; C:protein-DNA complex; IBA:GO_Central.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; IDA:UniProtKB.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
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 Reference proteome; Repressor; Transcription; Transcription regulation;
KW Two-component regulatory system; Virulence.
FT CHAIN 1..224
FT /note="Virulence transcriptional regulatory protein PhoP"
FT /id="PRO_0000081201"
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"
FT MUTAGEN 52
FT /note="D->A: Expression at concentrations above 30 uM
FT retains a protein-protein interaction and PhoQ-independent
FT induction of PAG. Yields insoluble purified protein above 7
FT uM."
FT /evidence="ECO:0000269|PubMed:15060051"
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
