BAER_ECOLI
ID BAER_ECOLI Reviewed; 240 AA.
AC P69228; P30846;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Transcriptional regulatory protein BaeR;
GN Name=baeR {ECO:0000303|PubMed:8282725}; OrderedLocusNames=b2079, JW2064;
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=8282725; DOI=10.1093/oxfordjournals.jbchem.a124180;
RA Nagasawa S., Ishige K., Mizuno T.;
RT "Novel members of the two-component signal transduction genes in
RT Escherichia coli.";
RL J. Biochem. 114:350-357(1993).
RN [2]
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 [3]
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 [4]
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 [5]
RP REGULATES THE MDTABCD OPERON.
RC STRAIN=K12 / W3104 / ATCC 19020;
RX PubMed=12107133; DOI=10.1128/jb.184.15.4161-4167.2002;
RA Nagakubo S., Nishino K., Hirata T., Yamaguchi A.;
RT "The putative response regulator BaeR stimulates multidrug resistance of
RT Escherichia coli via a novel multidrug exporter system, MdtABC.";
RL J. Bacteriol. 184:4161-4167(2002).
RN [6]
RP REGULATES THE MDTABCD OPERON.
RC STRAIN=K12;
RX PubMed=12107134; DOI=10.1128/jb.184.15.4168-4176.2002;
RA Baranova N., Nikaido H.;
RT "The baeSR two-component regulatory system activates transcription of the
RT yegMNOB (mdtABCD) transporter gene cluster in Escherichia coli and
RT increases its resistance to novobiocin and deoxycholate.";
RL J. Bacteriol. 184:4168-4176(2002).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC4100;
RX PubMed=12354228; DOI=10.1046/j.1365-2958.2002.03112.x;
RA Raffa R.G., Raivio T.L.;
RT "A third envelope stress signal transduction pathway in Escherichia coli.";
RL Mol. Microbiol. 45:1599-1611(2002).
RN [8]
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 [9]
RP REGULATES THE CASABCDE-YGBT-YGBF OPERON, DNA-BINDING, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=K12 / BW25113;
RX PubMed=21255106; DOI=10.1111/j.1365-2958.2010.07482.x;
RA Perez-Rodriguez R., Haitjema C., Huang Q., Nam K.H., Bernardis S., Ke A.,
RA DeLisa M.P.;
RT "Envelope stress is a trigger of CRISPR RNA-mediated DNA silencing in
RT Escherichia coli.";
RL Mol. Microbiol. 79:584-599(2011).
CC -!- FUNCTION: Member of the two-component regulatory system BaeS/BaeR which
CC responds to envelope stress (PubMed:12354228). Activates expression of
CC periplasmic chaperone spy in response to spheroplast formation, indole
CC and P pili protein PapG overexpression (PubMed:12354228). Activates the
CC mdtABCD (PubMed:12107133, PubMed:12107134) and probably the CRISPR-Cas
CC casABCDE-ygbT-ygbF operon (PubMed:21255106).
CC {ECO:0000269|PubMed:12107133, ECO:0000269|PubMed:12107134,
CC ECO:0000269|PubMed:12354228, ECO:0000269|PubMed:21255106}.
CC -!- INTERACTION:
CC P69228; P69228: baeR; NbExp=3; IntAct=EBI-1119567, EBI-1119567;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- PTM: Phosphorylated by BaeS. {ECO:0000269|PubMed:15522865}.
CC -!- DISRUPTION PHENOTYPE: Increased sensitivity to membrane stress caused
CC by indole or by overexpression of P pili protein PapG; double baeR-cpxR
CC mutants are more sensitive yet (PubMed:12354228). Loss of induction of
CC the CRISPR-Cas casABCDE-ygbT-ygbF operon (PubMed:21255106).
CC {ECO:0000269|PubMed:12354228, ECO:0000269|PubMed:21255106}.
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DR EMBL; D14054; BAA03141.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75140.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15935.1; -; Genomic_DNA.
DR PIR; JX0283; JX0283.
DR RefSeq; NP_416583.1; NC_000913.3.
DR RefSeq; WP_000137877.1; NZ_SSZK01000011.1.
DR PDB; 4B09; X-ray; 3.30 A; A/B/C/D/E/F/G/H/I/J/K/L=1-240.
DR PDBsum; 4B09; -.
DR AlphaFoldDB; P69228; -.
DR SMR; P69228; -.
DR BioGRID; 4260427; 15.
DR BioGRID; 850951; 3.
DR DIP; DIP-9198N; -.
DR IntAct; P69228; 8.
DR STRING; 511145.b2079; -.
DR ChEMBL; CHEMBL3309029; -.
DR jPOST; P69228; -.
DR PaxDb; P69228; -.
DR PRIDE; P69228; -.
DR EnsemblBacteria; AAC75140; AAC75140; b2079.
DR EnsemblBacteria; BAA15935; BAA15935; BAA15935.
DR GeneID; 946605; -.
DR KEGG; ecj:JW2064; -.
DR KEGG; eco:b2079; -.
DR PATRIC; fig|1411691.4.peg.171; -.
DR EchoBASE; EB1575; -.
DR eggNOG; COG0745; Bacteria.
DR HOGENOM; CLU_000445_30_4_6; -.
DR InParanoid; P69228; -.
DR OMA; EFNILHF; -.
DR PhylomeDB; P69228; -.
DR BioCyc; EcoCyc:BAER-MON; -.
DR PRO; PR:P69228; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0032993; C:protein-DNA complex; IBA:GO_Central.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:EcoCyc.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:2000144; P:positive regulation of DNA-templated transcription, initiation; IDA:EcoCyc.
DR GO; GO:2001023; P:regulation of response to drug; IMP:EcoCyc.
DR GO; GO:0006351; P: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; 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 PROSITE; PS51755; OMPR_PHOB; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Cytoplasm; DNA-binding; Phosphoprotein;
KW Reference proteome; Stress response; Transcription;
KW Transcription regulation; Two-component regulatory system.
FT CHAIN 1..240
FT /note="Transcriptional regulatory protein BaeR"
FT /id="PRO_0000081021"
FT DOMAIN 12..125
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DNA_BIND 131..234
FT /note="OmpR/PhoB-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01091"
FT MOD_RES 61
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 240 AA; 27656 MW; 8E2F6C9EB911C9CC CRC64;
MTELPIDENT PRILIVEDEP KLGQLLIDYL RAASYAPTLI SHGDQVLPYV RQTPPDLILL
DLMLPGTDGL TLCREIRRFS DIPIVMVTAK IEEIDRLLGL EIGADDYICK PYSPREVVAR
VKTILRRCKP QRELQQQDAE SPLIIDEGRF QASWRGKMLD LTPAEFRLLK TLSHEPGKVF
SREQLLNHLY DDYRVVTDRT IDSHIKNLRR KLESLDAEQS FIRAVYGVGY RWEADACRIV
