BCRR_ENTFL
ID BCRR_ENTFL Reviewed; 204 AA.
AC Q5WNW9;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 25-MAY-2022, entry version 54.
DE RecName: Full=HTH-type transcriptional activator BcrR {ECO:0000305};
GN Name=bcrR {ECO:0000303|PubMed:15388429};
OS Enterococcus faecalis (Streptococcus faecalis).
OG Plasmid pJM01.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1351;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=AR01/DGVS;
RX PubMed=15388429; DOI=10.1128/aac.48.10.3743-3748.2004;
RA Manson J.M., Keis S., Smith J.M.B., Cook G.M.;
RT "Acquired bacitracin resistance in Enterococcus faecalis is mediated by an
RT ABC transporter and a novel regulatory protein, BcrR.";
RL Antimicrob. Agents Chemother. 48:3743-3748(2004).
RN [2]
RP PROTEIN SEQUENCE OF 1-10, FUNCTION, DNA-BINDING, ACTIVITY REGULATION,
RP SUBCELLULAR LOCATION, AND DOMAIN.
RC STRAIN=AR01/DGVS;
RX PubMed=18227063; DOI=10.1074/jbc.m709503200;
RA Gauntlett J.C., Gebhard S., Keis S., Manson J.M., Pos K.M., Cook G.M.;
RT "Molecular analysis of BcrR, a membrane-bound bacitracin sensor and DNA-
RT binding protein from Enterococcus faecalis.";
RL J. Biol. Chem. 283:8591-8600(2008).
RN [3]
RP FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, DOMAIN, AND
RP MUTAGENESIS OF ARG-11; SER-33; GLY-64; GLU-179 AND THR-183.
RX PubMed=30777814; DOI=10.1099/mic.0.000781;
RA Darnell R.L., Nakatani Y., Knottenbelt M.K., Gebhard S., Cook G.M.;
RT "Functional characterization of BcrR: a one-component transmembrane signal
RT transduction system for bacitracin resistance.";
RL Microbiology 165:475-487(2019).
CC -!- FUNCTION: Functions as both a membrane-bound sensor and transducer of
CC bacitracin availability to activates transcription of the bcrABD operon
CC in the presence of bacitracin (PubMed:15388429, PubMed:18227063,
CC PubMed:30777814). Binds specifically to two inverted repeat sequences
CC on the bcrABD promoter, irrespective of bacitracin concentration
CC (PubMed:18227063). {ECO:0000269|PubMed:15388429,
CC ECO:0000269|PubMed:18227063, ECO:0000269|PubMed:30777814}.
CC -!- ACTIVITY REGULATION: Constitutively bound to the bcrABD promoter
CC (PubMed:18227063, PubMed:30777814). Requires bacitracin for activation,
CC probably through a conformational change, such as the oligomerization
CC of inactive dimers to form active tetramers (PubMed:30777814).
CC {ECO:0000269|PubMed:18227063, ECO:0000269|PubMed:30777814}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18227063,
CC ECO:0000269|PubMed:30777814}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DOMAIN: Contains an N-terminal helix-turn-helix DNA-binding domain, an
CC intermediate oligomerization domain and a C-terminal transmembrane
CC domain. {ECO:0000269|PubMed:18227063, ECO:0000269|PubMed:30777814}.
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DR EMBL; AY496968; AAS78452.1; -; Genomic_DNA.
DR RefSeq; WP_002367752.1; NZ_QPZR01000029.1.
DR AlphaFoldDB; Q5WNW9; -.
DR SMR; Q5WNW9; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR CDD; cd00093; HTH_XRE; 1.
DR Gene3D; 1.10.260.40; -; 1.
DR InterPro; IPR001387; Cro/C1-type_HTH.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR Pfam; PF01381; HTH_3; 1.
DR SMART; SM00530; HTH_XRE; 1.
DR SUPFAM; SSF47413; SSF47413; 1.
DR PROSITE; PS50943; HTH_CROC1; 1.
PE 1: Evidence at protein level;
KW Activator; Antibiotic resistance; Cell membrane; Direct protein sequencing;
KW DNA-binding; Membrane; Plasmid; Transcription; Transcription regulation;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..204
FT /note="HTH-type transcriptional activator BcrR"
FT /id="PRO_0000447368"
FT TOPO_DOM 1..81
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:30777814"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 103..126
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:30777814"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 148..154
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:30777814"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 176..181
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:30777814"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 203..204
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:30777814"
FT DOMAIN 7..61
FT /note="HTH cro/C1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00257"
FT DNA_BIND 18..37
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00257"
FT MUTAGEN 11
FT /note="R->K: Loss of activity. Does not affect DNA-binding
FT and cellular localization."
FT /evidence="ECO:0000269|PubMed:30777814"
FT MUTAGEN 33
FT /note="S->L: Loss of activity. Does not affect DNA-binding
FT and cellular localization."
FT /evidence="ECO:0000269|PubMed:30777814"
FT MUTAGEN 64
FT /note="G->D: Constitutively active. Does not affect DNA-
FT binding and cellular localization."
FT /evidence="ECO:0000269|PubMed:30777814"
FT MUTAGEN 64
FT /note="G->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:30777814"
FT MUTAGEN 179
FT /note="E->K: Loss of activity. Does not affect DNA-binding
FT and cellular localization."
FT /evidence="ECO:0000269|PubMed:30777814"
FT MUTAGEN 183
FT /note="T->M: Loss of activity. Does not affect DNA-binding
FT and cellular localization."
FT /evidence="ECO:0000269|PubMed:30777814"
SQ SEQUENCE 204 AA; 22887 MW; DD35639F9581CD17 CRC64;
MEFNEKLQQL RTGKNLTQEQ LAEQLYVSRT AISKWESGKG YPNMESLKCI SKFFSVTIDE
LLSGEELITL AETENRSNLK KIYNYIYGIL DMMAVAFIFL PLYGNSVGGY VYAVNLLSFT
ATTPFNLAVY WSAFAALIII GIGKIISTHL DKEKWGGIAT KCSLTITALA VCFFAAAREP
YITVLVFLLL IGKIFVWIKQ MGMK
