ID Q630F0_BACCZ Unreviewed; 481 AA.
AC Q630F0;
DT 25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 125.
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=deaD {ECO:0000313|EMBL:AAU20279.1};
GN Synonyms=dbpA {ECO:0000256|HAMAP-Rule:MF_00965};
GN OrderedLocusNames=BCE33L5149 {ECO:0000313|EMBL:AAU20279.1};
OS Bacillus cereus (strain ZK / E33L).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=288681 {ECO:0000313|EMBL:AAU20279.1, ECO:0000313|Proteomes:UP000002612};
RN [1] {ECO:0000313|Proteomes:UP000002612}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZK / E33L {ECO:0000313|Proteomes:UP000002612};
RX PubMed=16621833; DOI=10.1128/JB.188.9.3382-3390.2006;
RA Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Brown N.,
RA Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA Green L.D., Hill K.K., Hitchcock P., Jackson P.J., Keim P.,
RA Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K.,
RA Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., Okinaka R.T.,
RA Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Rubin E.,
RA Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Ticknor L.O., Wills P.L., Brettin T.S., Gilna P.;
RT "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT thuringiensis isolates closely related to Bacillus anthracis.";
RL J. Bacteriol. 188:3382-3390(2006).
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; CP000001; AAU20279.1; -; Genomic_DNA.
DR RefSeq; WP_000039359.1; NZ_CP009968.1.
DR AlphaFoldDB; Q630F0; -.
DR KEGG; bcz:BCE33L5149; -.
DR PATRIC; fig|288681.22.peg.192; -.
DR Proteomes; UP000002612; 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 216..378
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; 54073 MW; F10709AD6F5FF5F9 CRC64;
MSKKSFSNYA LSKEVRRALT GLGYEHPTEV QGEVIPVALQ KKDLVVKSQT GSGKTASFGI
PLCEMVEWEE NKPQALVLTP TRELAVQVKE DITNIGRFKR IKAAAIYGKS PFARQKLELK
QKTHIVVGTP GRVLDHIEKG TLSLERLKYL VIDEADEMLN MGFIDQVEAI IDELPTKRMT
MLFSATLPED VERLSRTYMN APTHIEIKAA GITTDKIEHT LFEVREEEKL SLLKDVTTIE
NPDSCIIFCR TQENVDHVYR QLDRVNYPCD KIHGGMVQED RFGVMDDFRK GKFRYLVATD
VAARGIDIDN ITHVINYDIP LEKESYVHRT GRTGRAGNSG KAITFITPYE DRFLEEIEAY
IGFAIPKANA PSKEEVMKGK AAFEEKIQAK PTIKKDKSAD INKGIMKLYF NGGKKKKIRA
VDFVGTIAKI QGVSAEDIGI ITIQDNVSYV EILNGKGPLV LKIMRNTTIK GKQLKVHEAN
K
//
