HPRR_ECOLI
ID HPRR_ECOLI Reviewed; 223 AA.
AC P76340; P97172;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Transcriptional regulatory protein HprR {ECO:0000305};
DE AltName: Full=Hydrogen peroxide response regulator {ECO:0000303|PubMed:27983483};
GN Name=hprR {ECO:0000303|PubMed:27983483}; Synonyms=yedW;
GN OrderedLocusNames=b1969, JW5322;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [2]
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 [3]
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 [4]
RP PHOSPHORYLATION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=15522865; DOI=10.1074/jbc.m410104200;
RA Yamamoto K., Hirao K., Oshima T., Aiba H., Utsumi R., Ishihama A.;
RT "Functional characterization in vitro of all two-component signal
RT transduction systems from Escherichia coli.";
RL J. Biol. Chem. 280:1448-1456(2005).
RN [5]
RP FUNCTION, DNA-BINDING, AND INTERPLAY BETWEEN HPRSR AND CUSSR.
RX PubMed=25568260; DOI=10.1099/mic.0.000026;
RA Urano H., Umezawa Y., Yamamoto K., Ishihama A., Ogasawara H.;
RT "Cooperative regulation of the common target genes between H(2)O(2)-sensing
RT YedVW and Cu2+-sensing CusSR in Escherichia coli.";
RL Microbiology 161:729-738(2015).
RN [6]
RP FUNCTION, DNA-BINDING, AND INTERPLAY BETWEEN HPRSR AND CUSSR.
RX PubMed=27983483; DOI=10.1099/mic.0.000410;
RA Urano H., Yoshida M., Ogawa A., Yamamoto K., Ishihama A., Ogasawara H.;
RT "Cross-regulation between two common ancestral response regulators, HprR
RT and CusR, in Escherichia coli.";
RL Microbiology 163:243-252(2017).
CC -!- FUNCTION: Member of a two-component regulatory system HprR/HprS
CC involved in response to hydrogen peroxide (PubMed:25568260,
CC PubMed:27983483). Regulates the expression of at least 5 operons,
CC cyoABCDE, hprRS, hiuH, cusRS and cusCFBA. Bifunctional regulator that
CC acts as an activator and a repressor (PubMed:25568260).
CC {ECO:0000269|PubMed:25568260, ECO:0000269|PubMed:27983483}.
CC -!- INTERACTION:
CC P76340; P76092: ynbC; NbExp=2; IntAct=EBI-560799, EBI-544837;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- PTM: Phosphorylated by HprS. {ECO:0000269|PubMed:15522865}.
CC -!- MISCELLANEOUS: HprSR and CusSR form a unique regulation system, where
CC both two-component systems recognize and regulate the same set of
CC genes, but under different environmental conditions. HprSR plays a role
CC in H(2)O(2) response regulation, while CusSR plays a role in Cu(2+)
CC response regulation (PubMed:25568260, PubMed:27983483). Under low
CC protein concentrations, the two regulators recognize and transcribe
CC both hiuH and cusC promoters, albeit at different efficiency,
CC apparently in a collaborative fashion (PubMed:27983483).
CC {ECO:0000269|PubMed:25568260, ECO:0000269|PubMed:27983483}.
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DR EMBL; U00096; AAC75035.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA15796.2; -; Genomic_DNA.
DR PIR; E64961; E64961.
DR RefSeq; NP_416478.2; NC_000913.3.
DR RefSeq; WP_001395354.1; NZ_LN832404.1.
DR AlphaFoldDB; P76340; -.
DR SMR; P76340; -.
DR BioGRID; 4260386; 5.
DR BioGRID; 850837; 1.
DR DIP; DIP-11853N; -.
DR IntAct; P76340; 2.
DR STRING; 511145.b1969; -.
DR iPTMnet; P76340; -.
DR jPOST; P76340; -.
DR PaxDb; P76340; -.
DR PRIDE; P76340; -.
DR EnsemblBacteria; AAC75035; AAC75035; b1969.
DR EnsemblBacteria; BAA15796; BAA15796; BAA15796.
DR GeneID; 946486; -.
DR KEGG; ecj:JW5322; -.
DR KEGG; eco:b1969; -.
DR PATRIC; fig|511145.12.peg.2049; -.
DR EchoBASE; EB3798; -.
DR eggNOG; COG0745; Bacteria.
DR HOGENOM; CLU_000445_30_1_6; -.
DR InParanoid; P76340; -.
DR OMA; NYEFFGD; -.
DR PhylomeDB; P76340; -.
DR BioCyc; EcoCyc:G7057-MON; -.
DR PRO; PR:P76340; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0032993; C:protein-DNA complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IDA:EcoCyc.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; IBA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:EcoCyc.
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:0045892; P:negative regulation of transcription, DNA-templated; IDA:EcoCyc.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:EcoCyc.
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; IPR006291; PcoR.
DR InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor.
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; SSF46894; SSF46894; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR TIGRFAMs; TIGR01387; cztR_silR_copR; 1.
DR PROSITE; PS51755; OMPR_PHOB; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW Activator; Cytoplasm; DNA-binding; Phosphoprotein; Reference proteome;
KW Repressor; Transcription; Transcription regulation;
KW Two-component regulatory system.
FT CHAIN 1..223
FT /note="Transcriptional regulatory protein HprR"
FT /id="PRO_0000081360"
FT DOMAIN 2..115
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DNA_BIND 122..220
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"
SQ SEQUENCE 223 AA; 25018 MW; 4A595D7430C2E2B5 CRC64;
MKILLIEDNQ RTQEWVTQGL SEAGYVIDAV SDGRDGLYLA LKDDYALIIL DIMLPGMDGW
QILQTLRTAK QTPVICLTAR DSVDDRVRGL DSGANDYLVK PFSFSELLAR VRAQLRQHHA
LNSTLEISGL RMDSVSHSVS RDNISITLTR KEFQLLWLLA SRAGEIIPRT VIASEIWGIN
FDSDTNTVDV AIRRLRAKVD DPFPEKLIAT IRGMGYSFVA VKK
