ID   CSHA_GEOKA              Reviewed;         467 AA.
AC   Q5L3G9;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=DEAD-box ATP-dependent RNA helicase CshA {ECO:0000255|HAMAP-Rule:MF_01493};
DE            EC=3.6.4.13 {ECO:0000255|HAMAP-Rule:MF_01493};
GN   Name=cshA {ECO:0000255|HAMAP-Rule:MF_01493}; OrderedLocusNames=GK0226;
OS   Geobacillus kaustophilus (strain HTA426).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   Geobacillus thermoleovorans group.
OX   NCBI_TaxID=235909;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTA426;
RX   PubMed=15576355; DOI=10.1093/nar/gkh970;
RA   Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA   Matsui S., Uchiyama I.;
RT   "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT   Geobacillus kaustophilus.";
RL   Nucleic Acids Res. 32:6292-6303(2004).
CC   -!- FUNCTION: DEAD-box RNA helicase possibly involved in RNA degradation.
CC       Unwinds dsRNA in both 5'- and 3'-directions, has RNA-dependent ATPase
CC       activity. {ECO:0000255|HAMAP-Rule:MF_01493}.
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_01493};
CC   -!- SUBUNIT: Oligomerizes, may be a member of the RNA degradosome.
CC       {ECO:0000255|HAMAP-Rule:MF_01493}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01493}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. CshA subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01493}.
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DR   EMBL; BA000043; BAD74511.1; -; Genomic_DNA.
DR   RefSeq; WP_011229736.1; NC_006510.1.
DR   AlphaFoldDB; Q5L3G9; -.
DR   SMR; Q5L3G9; -.
DR   STRING; 235909.GK0226; -.
DR   EnsemblBacteria; BAD74511; BAD74511; GK0226.
DR   KEGG; gka:GK0226; -.
DR   eggNOG; COG0513; Bacteria.
DR   HOGENOM; CLU_003041_21_0_9; -.
DR   OMA; EHKDGQR; -.
DR   Proteomes; UP000001172; Chromosome.
DR   GO; GO:0043590; C:bacterial nucleoid; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR   GO; GO:0003724; F:RNA helicase activity; ISS:UniProtKB.
DR   GO; GO:0006401; P:RNA catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0010501; P:RNA secondary structure unwinding; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 2.
DR   HAMAP; MF_01493; DEAD_helicase_CshA; 1.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR030880; DEAD_helicase_CshA.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
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..467
FT                   /note="DEAD-box ATP-dependent RNA helicase CshA"
FT                   /id="PRO_0000280057"
FT   DOMAIN          33..203
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01493"
FT   DOMAIN          214..374
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01493"
FT   REGION          428..467
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           2..30
FT                   /note="Q motif"
FT   MOTIF           151..154
FT                   /note="DEAD box"
FT   COMPBIAS        438..459
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         46..53
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01493"
SQ   SEQUENCE   467 AA;  52449 MW;  84EF44ADB0463C97 CRC64;
     MTTFQELGLS QEVMKAIERM GFEETTPIQA KTIPLSLQNK DVIGQAQTGT GKTAAFGIPI
     VEKVNVKNSA VQALVVAPTR ELAIQVSEEL YKIGAVKRVR VLPIYGGQDI ERQIRALKKH
     PHVIVGTPGR IIDHINRGTL RLEHVHTVVL DEADEMLNMG FIEDIEAILS HVPAERQTLL
     FSATMPDPIR RIAERFMNEP ELVKVKAKEM TVPNIQQYYL EVHEKKKFDI LTRLLDIQAP
     ELAIVFGRTK RRVDELAEAL NLRGYAAEGI HGDLSQAKRL SVLRKFKEGA IEILVATDVA
     ARGLDISGVT HVYNFDIPQD PESYVHRIGR TGRAGKTGVA MTFVTPREIG QLHHIERTTK
     RKMERMKPPT LDEALEGQQR IAIEKLLNVV ETENLSFYKR AAEELLEEHD SVTIVAACLK
     MLTREPDTTP VQLTEEPPLA VKREKKRGGR PDGSARSRTK KRRITAH