CSHA_BACC1
ID CSHA_BACC1 Reviewed; 525 AA.
AC Q73EU1;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=BCE_0267;
OS Bacillus cereus (strain ATCC 10987 / NRS 248).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=222523;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10987 / NRS 248;
RX PubMed=14960714; DOI=10.1093/nar/gkh258;
RA Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L.,
RA Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F.,
RA Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.;
RT "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic
RT adaptations and a large plasmid related to Bacillus anthracis pXO1.";
RL Nucleic Acids Res. 32:977-988(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; AE017194; AAS39203.1; -; Genomic_DNA.
DR RefSeq; WP_000206582.1; NC_003909.8.
DR AlphaFoldDB; Q73EU1; -.
DR SMR; Q73EU1; -.
DR DNASU; 2752637; -.
DR EnsemblBacteria; AAS39203; AAS39203; BCE_0267.
DR GeneID; 59156618; -.
DR GeneID; 64201247; -.
DR KEGG; bca:BCE_0267; -.
DR HOGENOM; CLU_003041_21_0_9; -.
DR OMA; EHKDGQR; -.
DR Proteomes; UP000002527; 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 RNA-binding; Stress response.
FT CHAIN 1..525
FT /note="DEAD-box ATP-dependent RNA helicase CshA"
FT /id="PRO_0000280050"
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..525
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 459..500
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 525 AA; 58583 MW; 1E3A8A3DB343AB11 CRC64;
MTTFRELGLS DSLLQSVESM GFEEATPIQA ETIPHALQGK DIIGQAQTGT GKTAAFGLPL
LDKVDTHKES VQGIVIAPTR ELAIQVGEEL YKIGKHKRVR ILPIYGGQDI NRQIRALKKH
PHIIVGTPGR ILDHINRKTL RLQNVETVVL DEADEMLNMG FIEDIEAILT DVPETHQTLL
FSATMPDPIR RIAERFMTEP QHIKVKAKEV TMPNIQQFYL EVQEKKKFDV LTRLLDIQSP
ELAIVFGRTK RRVDELSEAL NLRGYAAEGI HGDLTQAKRM SVLRKFKEGS IEVLVATDVA
ARGLDISGVT HVYNFDIPQD PESYVHRIGR TGRAGKKGIA MLFVTPRESG QLKNIERTTK
RKMDRMDAPT LDEALEGQQR LIAEKLQNTI ENENLAYYKR IAEEMLEEND SVTVVAAALK
MMTKEPDTTP IALTSEPPVV ARGGGSKKRG GNGGGYRDGN RNRSRDGRGG DGRNRDRNRD
GRNRDGNRDR NRDGGNRGRR GEGQGRPGSS NGRGERKHHS RKPQA