PHOP_SALTU
ID PHOP_SALTU Reviewed; 224 AA.
AC F5ZP95;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 1.
DT 25-MAY-2022, entry version 56.
DE RecName: Full=Virulence transcriptional regulatory protein PhoP;
GN Name=phoP; OrderedLocusNames=STMUK_1199;
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 PROTEIN SEQUENCE OF 1-20, 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 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:9573193,
CC 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. Induced at pH 4.4 (at
CC protein level). {ECO:0000269|PubMed:9573193}.
CC -!- PTM: Phosphorylated by PhoQ. {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Decreased tolerance to acid stress.
CC {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; CP002614; AEF07105.1; -; Genomic_DNA.
DR AlphaFoldDB; F5ZP95; -.
DR SMR; F5ZP95; -.
DR KEGG; sej:STMUK_1199; -.
DR PATRIC; fig|990282.4.peg.1250; -.
DR HOGENOM; CLU_000445_30_1_6; -.
DR Proteomes; UP000008278; 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; Direct protein sequencing; DNA-binding;
KW Growth regulation; Phosphoprotein; Repressor; Transcription;
KW Transcription regulation; Two-component regulatory system; Virulence.
FT CHAIN 1..224
FT /note="Virulence transcriptional regulatory protein PhoP"
FT /id="PRO_0000424529"
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
