PHOP_ECOLI
ID PHOP_ECOLI Reviewed; 223 AA.
AC P23836;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Transcriptional regulatory protein PhoP;
GN Name=phoP; OrderedLocusNames=b1130, JW1116;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1729240; DOI=10.1128/jb.174.2.492-498.1992;
RA Kasahara M., Nakata A., Shinagawa H.;
RT "Molecular analysis of the Escherichia coli phoP-phoQ operon.";
RL J. Bacteriol. 174:492-498(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1530848; DOI=10.1128/jb.174.2.486-491.1992;
RA Groisman E.A., Heffron F., Solomon F.;
RT "Molecular genetic analysis of the Escherichia coli phoP locus.";
RL J. Bacteriol. 174:486-491(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-50.
RC STRAIN=K12;
RX PubMed=1729205; DOI=10.1128/jb.174.1.130-136.1992;
RA He B., Smith J.M., Zalkin H.;
RT "Escherichia coli purB gene: cloning, nucleotide sequence, and regulation
RT by purR.";
RL J. Bacteriol. 174:130-136(1992).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-24.
RC STRAIN=K12;
RA Green S.M., Drabble W.T.;
RL Submitted (MAY-1991) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP PROTEIN SEQUENCE OF 1-7 AND 119-125.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=12123454; DOI=10.1046/j.1365-2958.2002.03017.x;
RA Yamamoto K., Ogasawara H., Fujita N., Utsumi R., Ishihama A.;
RT "Novel mode of transcription regulation of divergently overlapping
RT promoters by PhoP, the regulator of two-component system sensing external
RT magnesium availability.";
RL Mol. Microbiol. 45:423-438(2002).
RN [9]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [10]
RP FUNCTION, AND INDUCTION BY LOW MG(2+).
RC STRAIN=K12 / MC4100 / JA176;
RX PubMed=10464230; DOI=10.1128/jb.181.17.5516-5520.1999;
RA Kato A., Tanabe H., Utsumi R.;
RT "Molecular characterization of the PhoP-PhoQ two-component system in
RT Escherichia coli K-12: identification of extracellular Mg2+-responsive
RT promoters.";
RL J. Bacteriol. 181:5516-5520(1999).
RN [11]
RP GENOME-WIDE ANALYSIS, AND REGULATION BY MG(2+).
RC STRAIN=K12 / MC4100 / JA176;
RX PubMed=12813061; DOI=10.1128/jb.185.13.3696-3702.2003;
RA Minagawa S., Ogasawara H., Kato A., Yamamoto K., Eguchi Y., Oshima T.,
RA Mori H., Ishihama A., Utsumi R.;
RT "Identification and molecular characterization of the Mg2+ stimulon of
RT Escherichia coli.";
RL J. Bacteriol. 185:3696-3702(2003).
RN [12]
RP GENOME-WIDE ANALYSIS.
RC STRAIN=K12 / ST001;
RX PubMed=13129944; DOI=10.1128/jb.185.19.5735-5746.2003;
RA Hagiwara D., Sugiura M., Oshima T., Mori H., Aiba H., Yamashino T.,
RA Mizuno T.;
RT "Genome-wide analyses revealing a signaling network of the RcsC-YojN-RcsB
RT phosphorelay system in Escherichia coli.";
RL J. Bacteriol. 185:5735-5746(2003).
RN [13]
RP INTERACTION WITH EVGA/EVGS.
RC STRAIN=K12 / MC4100 / JA176;
RX PubMed=15126461; DOI=10.1128/jb.186.10.3006-3014.2004;
RA Eguchi Y., Okada T., Minagawa S., Oshima T., Mori H., Yamamoto K.,
RA Ishihama A., Utsumi R.;
RT "Signal transduction cascade between EvgA/EvgS and PhoP/PhoQ two-component
RT systems of Escherichia coli.";
RL J. Bacteriol. 186:3006-3014(2004).
RN [14]
RP ANALYSIS OF PHOP REGULATORY NETWORK, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
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 [15]
RP ACTIVITY REGULATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=20041203; DOI=10.1371/journal.pgen.1000788;
RA Lippa A.M., Goulian M.;
RT "Feedback inhibition in the PhoQ/PhoP signaling system by a membrane
RT peptide.";
RL PLoS Genet. 5:E1000788-E1000788(2009).
RN [16]
RP ACTIVITY REGULATION, AND INDUCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=22267510; DOI=10.1128/jb.06055-11;
RA Lippa A.M., Goulian M.;
RT "Perturbation of the oxidizing environment of the periplasm stimulates the
RT PhoQ/PhoP system in Escherichia coli.";
RL J. Bacteriol. 194:1457-1463(2012).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-120 IN THE PRESENCE AND LACK OF
RP PHOSPHORYLATION ANALOG, AND SUBUNIT.
RX PubMed=17545283; DOI=10.1128/jb.00049-07;
RA Bachhawat P., Stock A.M.;
RT "Crystal structures of the receiver domain of the response regulator PhoP
RT from Escherichia coli in the absence and presence of the phosphoryl analog
RT beryllofluoride.";
RL J. Bacteriol. 189:5987-5995(2007).
CC -!- FUNCTION: Member of the two-component regulatory system PhoP/PhoQ
CC involved in adaptation to low Mg(2+) environments and the control of
CC acid resistance genes. In low periplasmic Mg(2+), PhoQ phosphorylates
CC PhoP, 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 (By similarity). Mediates
CC magnesium influx to the cytosol by activation of MgtA. Promotes
CC expression of the two-component regulatory system rstA/rstB and
CC transcription of the hemL, mgrB, nagA, slyB, vboR and yrbL genes.
CC {ECO:0000250, ECO:0000269|PubMed:10464230}.
CC -!- ACTIVITY REGULATION: Feedback inhibited by MgrB, which seems to bind
CC PhoQ, altering its activity and that of downstream effector PhoP. PhoP-
CC regulated transcription is redox-sensitive, being activated when the
CC periplasm becomes more reducing (deletion of dsbA/dsbB, or treatment
CC with dithiothreitol). MgrB acts between DsbA/DsbB and PhoP/PhoQ in this
CC pathway. {ECO:0000269|PubMed:20041203, ECO:0000269|PubMed:22267510}.
CC -!- SUBUNIT: Monomer in the inactive, unphosphorylated state and dimer in
CC the active, phosphorylated state. {ECO:0000305|PubMed:17545283}.
CC -!- INTERACTION:
CC P23836; P23836: phoP; NbExp=5; IntAct=EBI-1121453, EBI-1121453;
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, inhibited at high Mg(2+)
CC concentrations (PubMed:10464230). Induced by dsbA disruption and
CC dithiothreitol (PubMed:22267510). {ECO:0000269|PubMed:10464230,
CC ECO:0000269|PubMed:22267510}.
CC -!- PTM: Phosphorylated by PhoQ. {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Altered expression of 33 genes; 9 are down-
CC regulated, the rest up-regulated. {ECO:0000269|PubMed:15703297}.
CC -!- MISCELLANEOUS: There is a close linkage between the Rcs and PhoQ/P
CC signaling systems, and both signaling systems respond to certain
CC external divalent cations (zinc and magnesium).
CC -!- MISCELLANEOUS: Two-component regulatory system EvgA/EvgS interacts with
CC PhoP/PhoQ via signal transduction mediated by phospho-EvgA.
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DR EMBL; D90393; BAA14390.1; -; Genomic_DNA.
DR EMBL; M81433; AAA24377.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74214.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35952.1; -; Genomic_DNA.
DR EMBL; M74924; AAA92732.1; -; Genomic_DNA.
DR EMBL; X59307; CAA41997.1; -; Genomic_DNA.
DR PIR; A41965; A41965.
DR RefSeq; NP_415648.1; NC_000913.3.
DR RefSeq; WP_001265471.1; NZ_STEB01000016.1.
DR PDB; 2PKX; X-ray; 2.54 A; A/B=1-121.
DR PDB; 2PL1; X-ray; 1.90 A; A=1-121.
DR PDBsum; 2PKX; -.
DR PDBsum; 2PL1; -.
DR AlphaFoldDB; P23836; -.
DR SMR; P23836; -.
DR BioGRID; 4260094; 19.
DR BioGRID; 850069; 1.
DR DIP; DIP-10500N; -.
DR IntAct; P23836; 6.
DR STRING; 511145.b1130; -.
DR iPTMnet; P23836; -.
DR jPOST; P23836; -.
DR PaxDb; P23836; -.
DR PRIDE; P23836; -.
DR EnsemblBacteria; AAC74214; AAC74214; b1130.
DR EnsemblBacteria; BAA35952; BAA35952; BAA35952.
DR GeneID; 945697; -.
DR KEGG; ecj:JW1116; -.
DR KEGG; eco:b1130; -.
DR PATRIC; fig|1411691.4.peg.1136; -.
DR EchoBASE; EB0724; -.
DR eggNOG; COG0745; Bacteria.
DR HOGENOM; CLU_000445_30_1_6; -.
DR InParanoid; P23836; -.
DR OMA; QLWGYPP; -.
DR PhylomeDB; P23836; -.
DR BioCyc; EcoCyc:PHOP-MON; -.
DR EvolutionaryTrace; P23836; -.
DR PRO; PR:P23836; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR CollecTF; EXPREG_00000950; -.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0032993; C:protein-DNA complex; IPI:CollecTF.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; IPI:CollecTF.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:CollecTF.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; EXP:CollecTF.
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 3D-structure; Activator; Cytoplasm; Direct protein sequencing; DNA-binding;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Two-component regulatory system.
FT CHAIN 1..223
FT /note="Transcriptional regulatory protein PhoP"
FT /id="PRO_0000081195"
FT DOMAIN 2..116
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DNA_BIND 124..222
FT /note="OmpR/PhoB-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01091"
FT MOD_RES 51
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:2PL1"
FT HELIX 10..22
FT /evidence="ECO:0007829|PDB:2PL1"
FT STRAND 26..32
FT /evidence="ECO:0007829|PDB:2PL1"
FT HELIX 33..42
FT /evidence="ECO:0007829|PDB:2PL1"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:2PL1"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:2PL1"
FT HELIX 59..68
FT /evidence="ECO:0007829|PDB:2PL1"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:2PL1"
FT HELIX 84..92
FT /evidence="ECO:0007829|PDB:2PL1"
FT STRAND 96..102
FT /evidence="ECO:0007829|PDB:2PL1"
FT HELIX 105..119
FT /evidence="ECO:0007829|PDB:2PL1"
SQ SEQUENCE 223 AA; 25535 MW; 2EFF27E3923D43EF CRC64;
MRVLVVEDNA LLRHHLKVQI QDAGHQVDDA EDAKEADYYL NEHIPDIAIV DLGLPDEDGL
SLIRRWRSND VSLPILVLTA RESWQDKVEV LSAGADDYVT KPFHIEEVMA RMQALMRRNS
GLASQVISLP PFQVDLSRRE LSINDEVIKL TAFEYTIMET LIRNNGKVVS KDSLMLQLYP
DAELRESHTI DVLMGRLRKK IQAQYPQEVI TTVRGQGYLF ELR
