ID C4L036_EXISA Unreviewed; 481 AA.
AC C4L036;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 86.
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 OrderedLocusNames=EAT1b_1773 {ECO:0000313|EMBL:ACQ70699.1};
OS Exiguobacterium sp. (strain ATCC BAA-1283 / AT1b).
OC Bacteria; Bacillota; Bacilli; Bacillales;
OC Bacillales Family XII. Incertae Sedis; Exiguobacterium.
OX NCBI_TaxID=360911 {ECO:0000313|EMBL:ACQ70699.1, ECO:0000313|Proteomes:UP000000716};
RN [1] {ECO:0000313|EMBL:ACQ70699.1, ECO:0000313|Proteomes:UP000000716}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1283 / AT1b {ECO:0000313|Proteomes:UP000000716};
RX PubMed=21460088; DOI=10.1128/JB.00303-11;
RA Vishnivetskaya T.A., Lucas S., Copeland A., Lapidus A., Glavina Del Rio T.,
RA Dalin E., Tice H., Bruce D.C., Goodwin L.A., Pitluck S., Saunders E.,
RA Brettin T., Detter C., Han C., Larimer F., Land M.L., Hauser L.J.,
RA Kyrpides N.C., Ovchinnikova G., Kathariou S., Ramaley R.F., Rodrigues D.F.,
RA Hendrix C., Richardson P., Tiedje J.M.;
RT "Complete genome sequence of the Thermophilic Bacterium Exiguobacterium sp.
RT AT1b.";
RL J. Bacteriol. 193:2880-2881(2011).
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 + H(+) + phosphate; 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}.
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DR EMBL; CP001615; ACQ70699.1; -; Genomic_DNA.
DR RefSeq; WP_015880258.1; NC_012673.1.
DR AlphaFoldDB; C4L036; -.
DR STRING; 360911.EAT1b_1773; -.
DR KEGG; eat:EAT1b_1773; -.
DR eggNOG; COG0513; Bacteria.
DR HOGENOM; CLU_003041_28_3_9; -.
DR OrthoDB; 9805696at2; -.
DR Proteomes; UP000000716; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
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; IPR028619; DEAD_helicase_DbpA.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
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}; 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 231..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; 54075 MW; 709FF05726C5AF3B CRC64;
MNKQQFTDYR LSDEITRALG IMKYESPTEV QQQVIPRALE REDLVVKAQT GSGKTAAFGI
PVIELIDWAE NKPQVLVLTP TRELAVQVRE DMTNIGRFKR IKATAVYGKE PFSKQREELK
QKTHIVVGTP GRVMDHIERE TLSLDRIEYL IIDEADEMLN RGFLADVEKI LQQLPKDRVT
MVFSATFPQD IERLCQKHMN APARVAIEST GMTASTIEHR LLPVHRNEKL AVLQDITVVE
NPDSCMIFCR TKENVDTVYA ELDKAGYSAE RLHGGLEQED RFAVMNGFKM GNFRYLVATD
VAARGIDVDN VELVINYDVP VEKESYVHRT GRTGRAGKQG TAITLMTRQE ERLIGAIESY
VQFEIPMIDA PTEAEVAANQ DAFEQKLSGR RVVRNNKTAR INQDIMKLHF SGGKKKKLRA
VDFVGTIAKI PGVSADDIGI ITINDQMTYV DILNGKGSIV LQAMETTPVK GKKLKVSKAR
K
//
