BTSR_ECOLI
ID BTSR_ECOLI Reviewed; 239 AA.
AC P0AFT5; P33356; P76432; P76433; Q2MAV5; Q9ALR8;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Transcriptional regulatory protein BtsR {ECO:0000305};
GN Name=btsR {ECO:0000303|PubMed:28469239}; Synonyms=yehT;
GN OrderedLocusNames=b2125, JW5352;
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 / BHB2600;
RA Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K.,
RA Church G.M.;
RT "Automated multiplex sequencing of the E.coli genome.";
RL Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
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 FUNCTION, AND 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, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ASP-54.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=22685278; DOI=10.1128/jb.00409-12;
RA Kraxenberger T., Fried L., Behr S., Jung K.;
RT "First insights into the unexplored two-component system YehU/YehT in
RT Escherichia coli.";
RL J. Bacteriol. 194:4272-4284(2012).
RN [6]
RP FUNCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=24659770; DOI=10.1128/jb.01554-14;
RA Behr S., Fried L., Jung K.;
RT "Identification of a novel nutrient-sensing histidine kinase/response
RT regulator network in Escherichia coli.";
RL J. Bacteriol. 196:2023-2029(2014).
RN [7]
RP FUNCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=28469239; DOI=10.1038/s41598-017-01410-2;
RA Behr S., Kristoficova I., Witting M., Breland E.J., Eberly A.R., Sachs C.,
RA Schmitt-Kopplin P., Hadjifrangiskou M., Jung K.;
RT "Identification of a high-affinity pyruvate receptor in Escherichia coli.";
RL Sci. Rep. 7:1388-1388(2017).
CC -!- FUNCTION: Member of the two-component regulatory system BtsS/BtsR,
CC which is part of a nutrient-sensing regulatory network composed of
CC BtsS/BtsR, the low-affinity pyruvate signaling system YpdA/YpdB and
CC their respective target proteins, BtsT and YhjX. Responds to depletion
CC of nutrients, specifically serine, and the concomitant presence of
CC extracellular pyruvate. BtsR regulates expression of btsT by binding to
CC its promoter region. Activation of the BtsS/BtsR signaling cascade also
CC suppresses YpdA/YpdB-mediated yhjX induction.
CC {ECO:0000269|PubMed:15522865, ECO:0000269|PubMed:22685278,
CC ECO:0000269|PubMed:24659770, ECO:0000269|PubMed:28469239}.
CC -!- INTERACTION:
CC P0AFT5; P07004: proA; NbExp=4; IntAct=EBI-556431, EBI-548584;
CC P0AFT5; P0A823: sfsA; NbExp=2; IntAct=EBI-556431, EBI-556413;
CC -!- PTM: Phosphorylated by BtsS. {ECO:0000269|PubMed:15522865}.
CC -!- DISRUPTION PHENOTYPE: Deletion of btsSR has no obvious phenotypic
CC effect under the conditions tested. {ECO:0000269|PubMed:22685278}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA60488.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U00007; AAA60488.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC75186.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE76601.1; -; Genomic_DNA.
DR PIR; D64980; D64980.
DR RefSeq; NP_416629.4; NC_000913.3.
DR RefSeq; WP_000598641.1; NZ_STEB01000002.1.
DR AlphaFoldDB; P0AFT5; -.
DR SMR; P0AFT5; -.
DR BioGRID; 4261849; 319.
DR BioGRID; 853268; 4.
DR DIP; DIP-48085N; -.
DR IntAct; P0AFT5; 3.
DR STRING; 511145.b2125; -.
DR jPOST; P0AFT5; -.
DR PaxDb; P0AFT5; -.
DR PRIDE; P0AFT5; -.
DR EnsemblBacteria; AAC75186; AAC75186; b2125.
DR EnsemblBacteria; BAE76601; BAE76601; BAE76601.
DR GeneID; 66673980; -.
DR GeneID; 949024; -.
DR KEGG; ecj:JW5352; -.
DR KEGG; eco:b2125; -.
DR PATRIC; fig|1411691.4.peg.120; -.
DR EchoBASE; EB1944; -.
DR eggNOG; COG3279; Bacteria.
DR HOGENOM; CLU_000445_14_1_6; -.
DR InParanoid; P0AFT5; -.
DR OMA; ENKGTYA; -.
DR PhylomeDB; P0AFT5; -.
DR BioCyc; EcoCyc:EG12006-MON; -.
DR PRO; PR:P0AFT5; -.
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:0001216; F:DNA-binding transcription activator activity; IBA:GO_Central.
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:0000160; P:phosphorelay signal transduction system; IDA:EcoCyc.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:EcoCyc.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR007492; LytTR_DNA-bd_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR039420; WalR-like.
DR PANTHER; PTHR48111; PTHR48111; 1.
DR Pfam; PF04397; LytTR; 1.
DR Pfam; PF00072; Response_reg; 1.
DR SMART; SM00850; LytTR; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR PROSITE; PS50930; HTH_LYTTR; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Two-component regulatory system.
FT CHAIN 1..239
FT /note="Transcriptional regulatory protein BtsR"
FT /id="PRO_0000081361"
FT DOMAIN 3..116
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DOMAIN 137..239
FT /note="HTH LytTR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00112"
FT MOD_RES 54
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT MUTAGEN 54
FT /note="D->E: 2-fold increase in btsT induction."
FT /evidence="ECO:0000269|PubMed:22685278"
FT MUTAGEN 54
FT /note="D->N: 10-fold decrease in btsT induction."
FT /evidence="ECO:0000269|PubMed:22685278"
SQ SEQUENCE 239 AA; 27400 MW; 5665AAE782B7FBA3 CRC64;
MIKVLIVDDE PLARENLRVF LQEQSDIEIV GECSNAVEGI GAVHKLRPDV LFLDIQMPRI
SGLEMVGMLD PEHRPYIVFL TAFDEYAIKA FEEHAFDYLL KPIDEARLEK TLARLRQERS
KQDVSLLPEN QQALKFIPCT GHSRIYLLQM KDVAFVSSRM SGVYVTSHEG KEGFTELTLR
TLESRTPLLR CHRQYLVNLA HLQEIRLEDN GQAELILRNG LTVPVSRRYL KSLKEAIGL
