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Database: UniProt
Entry: Q63GX5
LinkDB: Q63GX5
Original site: Q63GX5 
ID   CSHA_BACCZ              Reviewed;         528 AA.
AC   Q63GX5;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   16-OCT-2019, entry version 100.
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=BCE33L0221;
OS   Bacillus cereus (strain ZK / E33L).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=288681;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZK / E33L;
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.,
RA   Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O.,
RA   Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T.,
RA   Goodwin L.A., Hill K.K., Hitchcock P., Jackson P.J., Keim P.,
RA   Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K.,
RA   Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C.,
RA   Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P.,
RA   Robinson D.L., Rubin E., Saunders E., Tapia R., Tesmer J.G.,
RA   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
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; CP000001; AAU20012.1; -; Genomic_DNA.
DR   RefSeq; WP_000206583.1; NZ_CP009968.1.
DR   SMR; Q63GX5; -.
DR   EnsemblBacteria; AAU20012; AAU20012; BCE33L0221.
DR   KEGG; bcz:BCE33L0221; -.
DR   PATRIC; fig|288681.22.peg.5390; -.
DR   KO; K05592; -.
DR   OMA; RNPIRIL; -.
DR   Proteomes; UP000002612; 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    528       DEAD-box ATP-dependent RNA helicase CshA.
FT                                /FTId=PRO_0000280052.
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    524       Arg/Gly-rich.
SQ   SEQUENCE   528 AA;  58928 MW;  B6CC3E249CDFF58A 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 ARGGGSKKRG GNGGGYRDGN RNRSRDGRGG DGRNRDRNRD
     GRNRDGNRDR NREGSRDGNR GRRGEGQGRP GSSNGRGERK HHSRKPQA
//
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