ID   PHOP_SALPA              Reviewed;         224 AA.
AC   Q5PMJ1;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Virulence transcriptional regulatory protein PhoP;
GN   Name=phoP; OrderedLocusNames=SPA1619;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA   Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA   Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA   Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA   Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA   Warren W., Florea L., Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(2004).
CC   -!- FUNCTION: Member of the two-component regulatory system PhoQ/PhoP which
CC       regulates the expression of genes involved in virulence and resistance
CC       to host defense antimicrobial peptides. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- PTM: Phosphorylated by PhoQ. {ECO:0000305}.
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DR   EMBL; CP000026; AAV77546.1; -; Genomic_DNA.
DR   RefSeq; WP_000986522.1; NC_006511.1.
DR   AlphaFoldDB; Q5PMJ1; -.
DR   SMR; Q5PMJ1; -.
DR   PRIDE; Q5PMJ1; -.
DR   EnsemblBacteria; AAV77546; AAV77546; SPA1619.
DR   KEGG; spt:SPA1619; -.
DR   HOGENOM; CLU_000445_30_1_6; -.
DR   OMA; QLWGYPP; -.
DR   Proteomes; UP000008185; 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   3: Inferred from homology;
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_0000081199"
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