CSHA_BACHK
ID CSHA_BACHK Reviewed; 528 AA.
AC Q6HPE6;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-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=BT9727_0219;
OS Bacillus thuringiensis subsp. konkukian (strain 97-27).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=281309;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=97-27;
RX PubMed=16621833; DOI=10.1128/jb.188.9.3382-3390.2006;
RA Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D.,
RA Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA Hill K.K., Hitchcock P., Jackson P.J., Keim P., Kewalramani A.R.,
RA Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M.,
RA Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B.,
RA Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R.,
RA Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L.,
RA Brettin T.S., Gilna P.;
RT "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT thuringiensis isolates closely related to Bacillus anthracis.";
RL J. Bacteriol. 188:3382-3390(2006).
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; AE017355; AAT61332.1; -; Genomic_DNA.
DR RefSeq; WP_000206587.1; NC_005957.1.
DR RefSeq; YP_034574.1; NC_005957.1.
DR AlphaFoldDB; Q6HPE6; -.
DR SMR; Q6HPE6; -.
DR EnsemblBacteria; AAT61332; AAT61332; BT9727_0219.
DR GeneID; 45020285; -.
DR GeneID; 56655489; -.
DR KEGG; btk:BT9727_0219; -.
DR PATRIC; fig|281309.8.peg.235; -.
DR HOGENOM; CLU_003041_21_0_9; -.
DR OMA; EHKDGQR; -.
DR Proteomes; UP000001301; 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..528
FT /note="DEAD-box ATP-dependent RNA helicase CshA"
FT /id="PRO_0000280056"
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..528
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..504
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 528 AA; 58944 MW; A4DF1F168FEDF594 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 LIAEKLQSTI ENENLAYYKR IAEEMLEEND SVTVVAAALK
MMTKEPDTTP IALTSEPPVV SRGGGSKKRG GNGGGYRDGN RNRSRDGRGG DGRNRDRNRD
GRNRDGNRDR NREGSRDGNR GRRGEGQGRP GSSNGRGERK HHSRKPQA
