DBPA_BACCR
ID DBPA_BACCR Reviewed; 481 AA.
AC Q814I2;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=ATP-dependent RNA helicase DbpA {ECO:0000255|HAMAP-Rule:MF_00965};
DE EC=3.6.4.13 {ECO:0000255|HAMAP-Rule:MF_00965};
GN Name=dbpA {ECO:0000255|HAMAP-Rule:MF_00965}; Synonyms=cshD;
GN OrderedLocusNames=BC_5451;
OS Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=226900;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC / NCTC 2599 / NRRL B-3711;
RX PubMed=12721630; DOI=10.1038/nature01582;
RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT anthracis.";
RL Nature 423:87-91(2003).
RN [2]
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC / NCTC 2599 / NRRL B-3711;
RX PubMed=20709848; DOI=10.1128/aem.00782-10;
RA Pandiani F., Brillard J., Bornard I., Michaud C., Chamot S., Nguyen-the C.,
RA Broussolle V.;
RT "Differential involvement of the five RNA helicases in adaptation of
RT Bacillus cereus ATCC 14579 to low growth temperatures.";
RL Appl. Environ. Microbiol. 76:6692-6697(2010).
RN [3]
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC / NCTC 2599 / NRRL B-3711;
RX PubMed=21705526; DOI=10.1128/aem.02974-10;
RA Pandiani F., Chamot S., Brillard J., Carlin F., Nguyen-the C.,
RA Broussolle V.;
RT "Role of the five RNA helicases in the adaptive response of Bacillus cereus
RT ATCC 14579 cells to temperature, pH, and oxidative stresses.";
RL Appl. Environ. Microbiol. 77:5604-5609(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:0000255|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:0000255|HAMAP-Rule:MF_00965};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00965}.
CC -!- INDUCTION: Induced at 10 degrees Celsius. {ECO:0000269|PubMed:20709848,
CC ECO:0000269|PubMed:21705526}.
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:0000255|HAMAP-Rule:MF_00965}.
CC -!- DISRUPTION PHENOTYPE: Wild-type growth rate at 10 and 30 degrees
CC Celsius, no change upon exposure to H(2)O(2) or diamide.
CC {ECO:0000269|PubMed:20709848, ECO:0000269|PubMed:21705526}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DbpA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00965}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE016877; AAP12312.1; -; Genomic_DNA.
DR RefSeq; NP_835111.1; NC_004722.1.
DR RefSeq; WP_000039351.1; NZ_CP034551.1.
DR AlphaFoldDB; Q814I2; -.
DR SMR; Q814I2; -.
DR STRING; 226900.BC_5451; -.
DR EnsemblBacteria; AAP12312; AAP12312; BC_5451.
DR KEGG; bce:BC5451; -.
DR PATRIC; fig|226900.8.peg.5632; -.
DR HOGENOM; CLU_003041_21_1_9; -.
DR OMA; YDIELYQ; -.
DR Proteomes; UP000001417; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR GO; GO:0033592; F:RNA strand annealing activity; IBA:GO_Central.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IBA:GO_Central.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 3.40.50.300; -; 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 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; SSF52540; 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 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Helicase; Hydrolase; Nucleotide-binding;
KW Reference proteome; Ribosome biogenesis; RNA-binding.
FT CHAIN 1..481
FT /note="ATP-dependent RNA helicase DbpA"
FT /id="PRO_0000430107"
FT DOMAIN 35..205
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00965"
FT DOMAIN 231..377
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00965"
FT REGION 406..481
FT /note="Involved in 23S rRNA binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00965"
FT MOTIF 4..32
FT /note="Q motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00965"
FT MOTIF 153..156
FT /note="DEAD box"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00965"
FT BINDING 48..55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00965"
SQ SEQUENCE 481 AA; 54174 MW; BCAFAD3CE35CE7B9 CRC64;
MSKKSFSDYK LSKEIVRALT GLGYDHPTEV QGEVIPVALQ KKDLVVKSQT GSGKTASFGI
PLCEMVEWEE NKPQALVLTP TRELAVQVKE DITNIGRFKR IKAAAVYGKS PFARQKLELK
QKTHIVVGTP GRVLDHIEKG TLSLECLKYL VIDEADEMLN MGFIDQVEAI IDELPTKRMT
MLFSATLPED VEKLSRTYMN SPTHIEIKAA GITTDKIEHT LFEVIEDEKL SLLKDVTTIE
NPDSCIIFCR TQENVDHVYR QLKRANYPCD KIHGGMVQED RFEVMDDFRK GKFRYLVATD
VAARGIDIDN ITHVINYDIP LEKESYVHRT GRTGRAGNSG KAITFITPYE NRFLEEIEEY
IGFEIPKAIG PSKEEVMKEK AAFEEKLHAK PIIKKDKNAD INKGIMKLYF NGGKKKKIRA
VDFVGTIAKI KGVTAEDIGI ITIQDNVSYV EILNGKGPLV LKVMKTTTIK GKQLKVHEAI
K