ID A0A6M0QD05_9BACI Unreviewed; 481 AA.
AC A0A6M0QD05;
DT 07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 1.
DT 02-APR-2025, entry version 19.
DE RecName: Full=ATP-dependent RNA helicase DbpA {ECO:0000256|HAMAP-Rule:MF_00965};
DE EC=3.6.4.13 {ECO:0000256|HAMAP-Rule:MF_00965};
GN Name=dbpA {ECO:0000256|HAMAP-Rule:MF_00965};
GN ORFNames=G4D63_20865 {ECO:0000313|EMBL:NEY74155.1};
OS Bacillus mesophilus.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1808955 {ECO:0000313|EMBL:NEY74155.1, ECO:0000313|Proteomes:UP000481043};
RN [1] {ECO:0000313|EMBL:NEY74155.1, ECO:0000313|Proteomes:UP000481043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA4 {ECO:0000313|EMBL:NEY74155.1,
RC ECO:0000313|Proteomes:UP000481043};
RA Xie J.;
RT "Bacillus aquiflavi sp. nov., isolated from yellow water of strong flavor
RT Chinese baijiu in Yibin region of China.";
RL Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: DEAD-box RNA helicase involved in the assembly of the 50S
CC ribosomal subunit. Has an RNA-dependent ATPase activity, which is
CC specific for 23S rRNA, and a 3' to 5' RNA helicase activity that uses
CC the energy of ATP hydrolysis to destabilize and unwind short rRNA
CC duplexes. {ECO:0000256|HAMAP-Rule:MF_00965}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + phosphate + H(+); Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00965};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00965}.
CC -!- DOMAIN: Contains an N-terminal domain that binds non-specifically to
CC RNA and a C-terminal domain that binds specifically and tightly to
CC hairpin 92 of 23S rRNA. {ECO:0000256|HAMAP-Rule:MF_00965}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DbpA subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00965}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:NEY74155.1}.
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DR EMBL; JAAIWM010000015; NEY74155.1; -; Genomic_DNA.
DR RefSeq; WP_163182021.1; NZ_JAAIWM010000015.1.
DR AlphaFoldDB; A0A6M0QD05; -.
DR Proteomes; UP000481043; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0005840; C:ribosome; IEA:TreeGrafter.
DR GO; GO:0034458; F:3'-5' RNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0033592; F:RNA strand annealing activity; IEA:TreeGrafter.
DR GO; GO:0009409; P:response to cold; IEA:TreeGrafter.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IEA:UniProtKB-UniRule.
DR CDD; cd00268; DEADc; 1.
DR CDD; cd12500; RRM_BsYxiN_like; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR HAMAP; MF_00965; DEAD_helicase_DbpA; 1.
DR InterPro; IPR005580; DbpA/CsdA_RNA-bd_dom.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR050547; DEAD_box_RNA_helicases.
DR InterPro; IPR028619; DEAD_helicase_DbpA.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C-like.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR PANTHER; PTHR47963:SF2; ATP-DEPENDENT RNA HELICASE DBPA; 1.
DR PANTHER; PTHR47963; DEAD-BOX ATP-DEPENDENT RNA HELICASE 47, MITOCHONDRIAL; 1.
DR Pfam; PF03880; DbpA; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00965}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00965};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_00965};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00965};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00965}; Reference proteome {ECO:0000313|Proteomes:UP000481043};
KW Ribosome biogenesis {ECO:0000256|HAMAP-Rule:MF_00965};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_00965}.
FT DOMAIN 4..32
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 35..205
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 216..376
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 406..481
FT /note="Involved in 23S rRNA binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00965"
FT MOTIF 4..32
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
SQ SEQUENCE 481 AA; 54030 MW; A469CD178EB06DBB CRC64;
MTETSFEAYQ LSDEIKRALD LLKYETPTEV QTEVIPKALN NQDLVVKSQT GSGKTASFGI
PICEKLDWEE KKPQALILTP TRELAVQVRD DITNIGRFKR IKAMAVYGKE PFAKQKDELK
QKTHVVVGTP GRVKDHIDRE TLVLDEIKYL IIDEADEMLN MGFIEEVEAI INQLPTDRIT
MVFSATLPKD VEKLCHQYMN EPVHVEIEST GVTTSSIEHL VIKLREEEKL SVLKDVTVVE
NPHSCIIFCN TKEHVENVYS ELEESNYASE RLHGGLVQED RFAVMDGFKR GNFRYLVATD
VAARGIDVDN VTLILNYDVP MEKASYVHRT GRTGRAGNKG KAITLVTENE EKYLRAIERY
IGFEIPTVDE PSQGQVAGNQ GAFDEKVGGR RVVRNNKTER INRDIMKLHF SGGKKKKLRA
VDFVGTISNL PGVSAEDIGI ITILDHLTYV DILNGKGSVV LQAMEEKTIK GKKLKVSVAN
K
//
