ID   DEAD_BUCBP              Reviewed;         602 AA.
AC   Q89AF9;
DT   30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2003, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=ATP-dependent RNA helicase DeaD {ECO:0000255|HAMAP-Rule:MF_00964};
DE            EC=3.6.4.13 {ECO:0000255|HAMAP-Rule:MF_00964};
DE   AltName: Full=Cold-shock DEAD box protein A {ECO:0000255|HAMAP-Rule:MF_00964};
GN   Name=deaD {ECO:0000255|HAMAP-Rule:MF_00964};
GN   Synonyms=csdA {ECO:0000255|HAMAP-Rule:MF_00964}; OrderedLocusNames=bbp_335;
OS   Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=224915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bp;
RX   PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
CC   -!- FUNCTION: DEAD-box RNA helicase involved in various cellular processes
CC       at low temperature, including ribosome biogenesis, mRNA degradation and
CC       translation initiation. {ECO:0000255|HAMAP-Rule:MF_00964}.
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_00964};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00964}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DeaD/CsdA
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00964}.
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DR   EMBL; AE016826; AAO27056.1; -; Genomic_DNA.
DR   RefSeq; WP_011091457.1; NC_004545.1.
DR   AlphaFoldDB; Q89AF9; -.
DR   SMR; Q89AF9; -.
DR   STRING; 224915.bbp_335; -.
DR   EnsemblBacteria; AAO27056; AAO27056; bbp_335.
DR   GeneID; 56470874; -.
DR   KEGG; bab:bbp_335; -.
DR   eggNOG; COG0513; Bacteria.
DR   HOGENOM; CLU_003041_21_1_6; -.
DR   OMA; LPQGMPK; -.
DR   OrthoDB; 626183at2; -.
DR   Proteomes; UP000000601; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0003724; F:RNA helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0070417; P:cellular response to cold; IEA:InterPro.
DR   GO; GO:0000027; P:ribosomal large subunit assembly; IEA:UniProtKB-UniRule.
DR   GO; GO:0006401; P:RNA catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd12499; RRM_EcCsdA_like; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   HAMAP; MF_00964; DEAD_helicase_DeaD; 1.
DR   InterPro; IPR034415; CsdA_RRM.
DR   InterPro; IPR005580; DbpA/CsdA_RNA-bd_dom.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR028618; DEAD_helicase_DeaD.
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   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Helicase; Hydrolase; Nucleotide-binding;
KW   Reference proteome; RNA-binding; Stress response.
FT   CHAIN           1..602
FT                   /note="ATP-dependent RNA helicase DeaD"
FT                   /id="PRO_0000055100"
FT   DOMAIN          37..208
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00964"
FT   DOMAIN          231..378
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00964"
FT   MOTIF           6..34
FT                   /note="Q motif"
FT   MOTIF           156..159
FT                   /note="DEAD box"
FT   BINDING         50..57
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00964"
SQ   SEQUENCE   602 AA;  68490 MW;  F1508E82CBB4D69B CRC64;
     MTHTNMTFSS FGLNSCIITA LNDIGYVQPS PIQAACIPYL IKGKDVLGMA QTGSGKTAAF
     ALPLLHNIKL DVRVPQILVL TPTRELAVQV AEAFSNFSKK LIGVHVLALY GGQRYDLQLK
     SLRKGPQIIV GTPGRLLDHL KRRTLSLSNL HSLVLDEADE MLRMGFIEDV ETIMTEIPDR
     HQTALFSATM PEAIRRISRR FMKNPKEIRI QSNITTRPDI QQSYWMVYGK KTDALIRFLE
     AEDFSATIIF VRTKNATLEV SEVLERYGYN SAALNGDMNQ SLREQTLEKL KDGRLDILIA
     TDVAARGLDV DRISFVINYD IPMDSESYVH RIGRTGRAGR KGKALLFVEN RERRLLRNIE
     RAMNISISEV NLPKSDFLSK RRLEKFAQKV QIQLDSKDLH EYRGLLPKLQ PNNNSLDIES
     LAAALLKMAQ GERSLIVKPE SIVRARHLKI KDTYRNNNYK SLNYVSRYNR DKNVDLYRID
     VGRNDGVEVR HIVGAIANEG DISSRKIGNV RLFSNYSTIE LPKGLSNTLP KTFIRTKILN
     KFINIKLLYN SNFKGNYNDI KDVKVYNSNK LRSKKMNNKK FVSSGVRKKI KTNISCNRRR
     SV