ID   DBPA_LISMO              Reviewed;         470 AA.
AC   Q8Y7M8;
DT   03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 126.
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}; OrderedLocusNames=lmo1246;
OS   Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=169963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-679 / EGD-e;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA   Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA   Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA   Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA   Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA   Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA   Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
RN   [2]
RP   FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC BAA-679 / EGD-e;
RX   PubMed=22820328; DOI=10.1128/aem.01526-12;
RA   Markkula A., Lindstrom M., Johansson P., Bjorkroth J., Korkeala H.;
RT   "Roles of four putative DEAD-box RNA helicase genes in growth of Listeria
RT   monocytogenes EGD-e under heat, pH, osmotic, ethanol, and oxidative stress
RT   conditions.";
RL   Appl. Environ. Microbiol. 78:6875-6882(2012).
RN   [3]
RP   FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC BAA-679 / EGD-e;
RX   PubMed=22564273; DOI=10.1111/j.1462-2920.2012.02761.x;
RA   Markkula A., Mattila M., Lindstrom M., Korkeala H.;
RT   "Genes encoding putative DEAD-box RNA helicases in Listeria monocytogenes
RT   EGD-e are needed for growth and motility at 3 degrees C.";
RL   Environ. Microbiol. 14:2223-2232(2012).
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       ECO:0000269|PubMed:22564273, ECO:0000269|PubMed:22820328}.
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: By growth at 3 degrees Celsius (PubMed:22564273), and 3.5%
CC       ethanol, repressed by 6% NaCl (PubMed:22820328).
CC       {ECO:0000269|PubMed:22564273, ECO:0000269|PubMed:22820328}.
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: Growth rate decreased at 37 and 25 degrees
CC       Celsius, slightly slower and to lower optical density at 3 degrees
CC       Celsius. No effect on motility at 25 or 3 degrees Celsius
CC       (PubMed:22564273). {ECO:0000269|PubMed:22564273,
CC       ECO:0000269|PubMed:22820328}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DbpA subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00965}.
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DR   EMBL; AL591978; CAC99324.1; -; Genomic_DNA.
DR   PIR; AF1230; AF1230.
DR   RefSeq; NP_464771.1; NC_003210.1.
DR   RefSeq; WP_010989717.1; NZ_CP023861.1.
DR   AlphaFoldDB; Q8Y7M8; -.
DR   SMR; Q8Y7M8; -.
DR   STRING; 169963.lmo1246; -.
DR   PaxDb; Q8Y7M8; -.
DR   EnsemblBacteria; CAC99324; CAC99324; CAC99324.
DR   GeneID; 986011; -.
DR   KEGG; lmo:lmo1246; -.
DR   PATRIC; fig|169963.11.peg.1278; -.
DR   eggNOG; COG0513; Bacteria.
DR   HOGENOM; CLU_003041_21_1_9; -.
DR   OMA; YDIELYQ; -.
DR   PhylomeDB; Q8Y7M8; -.
DR   BioCyc; LMON169963:LMO1246-MON; -.
DR   PHI-base; PHI:7618; -.
DR   Proteomes; UP000000817; 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; 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; 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..470
FT                   /note="ATP-dependent RNA helicase DbpA"
FT                   /id="PRO_0000430108"
FT   DOMAIN          30..200
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00965"
FT   DOMAIN          223..365
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00965"
FT   REGION          394..470
FT                   /note="Involved in 23S rRNA binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00965"
FT   MOTIF           1..27
FT                   /note="Q motif"
FT   MOTIF           148..151
FT                   /note="DEAD box"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00965"
FT   BINDING         43..50
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00965"
SQ   SEQUENCE   470 AA;  52986 MW;  03AD77C834D06372 CRC64;
     MNNLKLSEEI KRAINELGYT EATPVQKAVI PVALTGEDIV AKSQTGSGKT AAFAIPIAEQ
     VEWEENKPQA LIIVPTRELA MQVKTECTNI GRFKRVKAAA IYGQSPFAKQ KLELSQKNHI
     VVGTPGRLLD HIEKGSLNVD KVAHLVLDEV DEMLSMGFID QVEDILSRLP KQRQNLFFSA
     TMPEEMQDLI KRYQDNPMVI EMASEKTNPI FHVEMQTDNK EKTLKDVLIT ENPDSAIIFC
     NTKNQVDELT DLLDVKASKI HGGLRQEDRF RAMDDFKSGK SRFLIATDVA GRGIDVDNVS
     LVINYDLPIE KENYVHRIGR TGRAGKSGKA ISFVKTNENP LLRDIEEMLD VTIEKKRKPT
     VIEVKVNEDA FRKKQQKRPT IKKARGEKLN KNIMKLYFNG GKKKKIRAVD FVGTISKLEG
     ITAEDIGIIT IEDHVSFVEI LNGKGPAVLE MMRSRKVKGR RLKVNEARKR