BCRA_ENTFL
ID BCRA_ENTFL Reviewed; 308 AA.
AC Q5WNX0;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Bacitracin transport ATP-binding protein BcrA {ECO:0000305};
GN Name=bcrA {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], FUNCTION, INDUCTION, AND DISRUPTION
RP PHENOTYPE.
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 INDUCTION.
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).
CC -!- FUNCTION: Essential for high-level bacitracin resistance
CC (PubMed:15388429). Part of the ABC transporter complex BcrAB. Probably
CC responsible for energy coupling to the transport system (Probable).
CC {ECO:0000269|PubMed:15388429, ECO:0000305|PubMed:15388429}.
CC -!- SUBUNIT: The complex is probably composed of two ATP-binding proteins
CC (BcrA) and two transmembrane proteins (BcrB). {ECO:0000305}.
CC -!- INDUCTION: Transcription is activated by the regulatory protein BcrR in
CC the presence of bacitracin. {ECO:0000269|PubMed:15388429,
CC ECO:0000269|PubMed:18227063}.
CC -!- DISRUPTION PHENOTYPE: Disruption mutant is sensitive to bacitracin.
CC {ECO:0000269|PubMed:15388429}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR EMBL; AY496968; AAS78451.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5WNX0; -.
DR SMR; Q5WNX0; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:UniProt.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 2: Evidence at transcript level;
KW Antibiotic resistance; ATP-binding; Nucleotide-binding; Plasmid; Transport.
FT CHAIN 1..308
FT /note="Bacitracin transport ATP-binding protein BcrA"
FT /id="PRO_0000447366"
FT DOMAIN 8..236
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 40..47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 308 AA; 34291 MW; ED194215F70E1FC6 CRC64;
MMIMEYVIET ENLTKQYGET TVVNKINLHV PKGKIYGLLG RNGAGKTTAM KMMLQLAFPT
DGTVRLFGTN YKENIHTLYS KVGSIIETPG FYSNLTGYEN LQILAKLRGG VSKSGVEKAL
EVVGLHKEKR KVFSDYSLGM KQRLGIAAAI MHEPELLILD EPINGLDPIG ISEIRSFLSK
LSHENGTTIF ISSHVLSEIE QIADVIGVMH EGHLVEEVNI SELHKRNRKY TEFDVSDGKI
AAKILESSYH MTDFTVQDGT IRIYDFSQSV GEINREFARN GLLITRINDS EENLEDYFSK
LIGGGGIA