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Database: UniProt
Entry: Q73EU1
LinkDB: Q73EU1
Original site: Q73EU1 
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   16-OCT-2019, entry version 96.
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};
GN   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
CC       degradation. Unwinds dsRNA in both 5'- and 3'-directions, has RNA-
CC       dependent ATPase 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
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01493}.
DR   EMBL; AE017194; AAS39203.1; -; Genomic_DNA.
DR   RefSeq; WP_000206582.1; NC_003909.8.
DR   SMR; Q73EU1; -.
DR   DNASU; 2752637; -.
DR   EnsemblBacteria; AAS39203; AAS39203; BCE_0267.
DR   KEGG; bca:BCE_0267; -.
DR   HOGENOM; HOG000268810; -.
DR   KO; K05592; -.
DR   OMA; RNPIRIL; -.
DR   BioCyc; BCER222523:G1G0J-296-MONOMER; -.
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: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   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; Complete proteome; Cytoplasm; Helicase; Hydrolase;
KW   Nucleotide-binding; RNA-binding; Stress response.
FT   CHAIN         1    525       DEAD-box ATP-dependent RNA helicase CshA.
FT                                /FTId=PRO_0000280050.
FT   DOMAIN       33    203       Helicase ATP-binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01493}.
FT   DOMAIN      214    374       Helicase C-terminal. {ECO:0000255|HAMAP-
FT                                Rule:MF_01493}.
FT   NP_BIND      46     53       ATP. {ECO:0000255|HAMAP-Rule:MF_01493}.
FT   MOTIF         2     30       Q motif.
FT   MOTIF       151    154       DEAD box.
FT   COMPBIAS    457    521       Arg/Gly-rich.
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
//
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