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
//