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Database: UniProt
Entry: Q737M8_BACC1
LinkDB: Q737M8_BACC1
Original site: Q737M8_BACC1 
ID   Q737M8_BACC1            Unreviewed;       542 AA.
AC   Q737M8;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   24-JAN-2024, entry version 105.
DE   RecName: Full=Ribosome protection protein VmlR {ECO:0000256|HAMAP-Rule:MF_00846};
GN   Name=vmlR {ECO:0000256|HAMAP-Rule:MF_00846};
GN   OrderedLocusNames=BCE_2620 {ECO:0000313|EMBL:AAS41534.1};
OS   Bacillus cereus (strain ATCC 10987 / NRS 248).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=222523 {ECO:0000313|EMBL:AAS41534.1, ECO:0000313|Proteomes:UP000002527};
RN   [1] {ECO:0000313|EMBL:AAS41534.1, ECO:0000313|Proteomes:UP000002527}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10987 / NRS 248 {ECO:0000313|Proteomes:UP000002527};
RX   PubMed=14960714; DOI=10.1093/nar/gkh258;
RA   Rasko D.A., Ravel J., Okstad O.A., Helgason E., Cer R.Z., Jiang L.,
RA   Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.,
RA   Nelson W.C., Kolsto A.-B., Fraser C.M., Read T.D.;
RT   "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic
RT   adaptations and a large plasmid related to Bacillus anthracis pXO1.";
RL   Nucleic Acids Res. 32:977-988(2004).
CC   -!- FUNCTION: Recognizes and binds in the vacant E-site of ribosomes
CC       stalled by some peptidyltransferase center (PTC)-targeting antibiotics.
CC       Makes contact with the PTC and both ribosomal subunits. Induces
CC       conformational changes in the P-site, which allows it to dislodge the
CC       antibiotic from its PTC binding site. {ECO:0000256|HAMAP-
CC       Rule:MF_00846}.
CC   -!- SUBUNIT: Binds within the E-site of the 70S ribosome, where it contacts
CC       ribosomal proteins of the large and small subunit, the 16 and 23S rRNAs
CC       and the acceptor arm of the P-site tRNA. {ECO:0000256|HAMAP-
CC       Rule:MF_00846}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00846}.
CC       Note=Does not stably associate with ribosomes. {ECO:0000256|HAMAP-
CC       Rule:MF_00846}.
CC   -!- DOMAIN: The antibiotic resistance domain (ARD) is packed between the
CC       23S rRNA and the acceptor arm of the P-site tRNA and inserts into the
CC       peptidyltransferase center (PTC). The C-terminal extension (CTE)
CC       contacts the small ribosomal subunit, positioned in the Shine-Dalgarno-
CC       anti-Shine-Dalgarno cavity. {ECO:0000256|HAMAP-Rule:MF_00846}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCF family.
CC       ARE2 subfamily. {ECO:0000256|HAMAP-Rule:MF_00846}.
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DR   EMBL; AE017194; AAS41534.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q737M8; -.
DR   KEGG; bca:BCE_2620; -.
DR   HOGENOM; CLU_000604_36_0_9; -.
DR   OMA; FKEYHRV; -.
DR   Proteomes; UP000002527; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0072344; P:rescue of stalled ribosome; IEA:UniProtKB-UniRule.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   CDD; cd03221; ABCF_EF-3; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   HAMAP; MF_00846; VmlR; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR032781; ABC_tran_Xtn.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR043684; VmlR.
DR   PANTHER; PTHR42855:SF2; ABC TRANSPORTER ATP-BINDING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR42855; ABC TRANSPORTER ATP-BINDING SUBUNIT; 1.
DR   Pfam; PF00005; ABC_tran; 2.
DR   Pfam; PF12848; ABC_tran_Xtn; 1.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   3: Inferred from homology;
KW   Antibiotic resistance {ECO:0000256|HAMAP-Rule:MF_00846};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00846}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00846};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00846}; Repeat {ECO:0000256|HAMAP-Rule:MF_00846};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00846};
KW   rRNA-binding {ECO:0000256|HAMAP-Rule:MF_00846};
KW   tRNA-binding {ECO:0000256|HAMAP-Rule:MF_00846}.
FT   DOMAIN          5..202
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          294..505
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   REGION          185..291
FT                   /note="Antibiotic resistance domain (ARD)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00846"
FT   BINDING         37..44
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00846"
FT   BINDING         326..333
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00846"
SQ   SEQUENCE   542 AA;  62965 MW;  722909D8D1FB1075 CRC64;
     MKELLKLNDV YVEIKENMLL EKMNVTVKQG DVIGLIGKNG AGKSTLLQLI NGKIEPSKGT
     VEWMQMNMTT AYVEQEKESF VNKDIIAKEA ELLAKWGVPT NDFFTLSGGE KLKVRLAKGF
     AENPNVLILD EPTNHLDEMS TEFLIKQIKN MKGTVIVVSH DRYFLDVVAT RIWSIEDKKL
     IDHSGNYTSY MKAREHKRMT QQREYEKQQK KIEQVETHIK ELSSWSQKAH AQSTKQEGVK
     EFYRVKAKRM DAQVKSKRKR LEKELEKTKV ERVKEDYSVE FSIQANKKVG KRFLEVKQLR
     KEFNNRLLFE NVNFTIQHGE KIAIVGPNGS GKTTLLKMIM GAETAQGEIW ISPSANIGYL
     TQEVFDLPLD KTPEDLFYKE TFEERGKVQN LMKHLGFESS QWTEPIRYMS MGERVKCKLM
     AYILDEKDVL ILDEPTNHLD LPSREQLENT LAEYNGTLVI VSHDRYFLEK TTNTKLVFVN
     NTIQKQLEEP TKTRDEIEEL RLTLETERQE VLGKLSFLTS KDKEYKALDE RFKELTKQIK
     EL
//
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