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Database: UniProt
Entry: Q81DF9
LinkDB: Q81DF9
Original site: Q81DF9 
ID   CSHE_BACCR              Reviewed;         458 AA.
AC   Q81DF9;
DT   03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   16-OCT-2019, entry version 110.
DE   RecName: Full=DEAD-box ATP-dependent RNA helicase CshE;
DE            EC=3.6.4.13;
GN   Name=cshE; OrderedLocusNames=BC_2408;
OS   Bacillus cereus (strain ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 /
OS   NCIMB 9373 / NRRL B-3711).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL
RC   B-3711;
RX   PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B.,
RA   Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A.,
RA   Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T.,
RA   Grechkin Y., Pusch G., Haselkorn R., Fonstein M., Ehrlich S.D.,
RA   Overbeek R., Kyrpides N.C.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with
RT   Bacillus anthracis.";
RL   Nature 423:87-91(2003).
RN   [2]
RP   INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL
RC   B-3711;
RX   PubMed=20709848; DOI=10.1128/aem.00782-10;
RA   Pandiani F., Brillard J., Bornard I., Michaud C., Chamot S.,
RA   Nguyen-the C., Broussolle V.;
RT   "Differential involvement of the five RNA helicases in adaptation of
RT   Bacillus cereus ATCC 14579 to low growth temperatures.";
RL   Appl. Environ. Microbiol. 76:6692-6697(2010).
RN   [3]
RP   INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL
RC   B-3711;
RX   PubMed=21705526; DOI=10.1128/aem.02974-10;
RA   Pandiani F., Chamot S., Brillard J., Carlin F., Nguyen-the C.,
RA   Broussolle V.;
RT   "Role of the five RNA helicases in the adaptive response of Bacillus
RT   cereus ATCC 14579 cells to temperature, pH, and oxidative stresses.";
RL   Appl. Environ. Microbiol. 77:5604-5609(2011).
CC   -!- FUNCTION: DEAD-box RNA helicase. Probably has an RNA-dependent
CC       ATPase activity and a 3' to 5' RNA helicase activity that uses the
CC       energy of ATP hydrolysis to destabilize and unwind short RNA
CC       duplexes (By similarity). {ECO:0000250}.
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   -!- INDUCTION: Induced at 10 degrees Celsius.
CC       {ECO:0000269|PubMed:20709848, ECO:0000269|PubMed:21705526}.
CC   -!- DISRUPTION PHENOTYPE: Wild-type growth rate at 10 and 30 degrees
CC       Celsius, no change upon exposure to H(2)O(2) or diamide.
CC       {ECO:0000269|PubMed:20709848, ECO:0000269|PubMed:21705526}.
DR   EMBL; AE016877; AAP09371.1; -; Genomic_DNA.
DR   RefSeq; NP_832170.1; NC_004722.1.
DR   RefSeq; WP_002195506.1; NZ_CP034551.1.
DR   SMR; Q81DF9; -.
DR   EnsemblBacteria; AAP09371; AAP09371; BC_2408.
DR   GeneID; 1204757; -.
DR   KEGG; bce:BC2408; -.
DR   PATRIC; fig|226900.8.peg.2436; -.
DR   eggNOG; ENOG4105C1J; Bacteria.
DR   eggNOG; COG0513; LUCA.
DR   KO; K05592; -.
DR   OMA; TRFHDFK; -.
DR   Proteomes; UP000001417; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0033592; F:RNA strand annealing activity; IBA:GO_Central.
DR   GO; GO:0000027; P:ribosomal large subunit assembly; IBA:GO_Central.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
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; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Complete proteome; Helicase; Hydrolase;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN         1    458       DEAD-box ATP-dependent RNA helicase CshE.
FT                                /FTId=PRO_0000430104.
FT   DOMAIN       36    207       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      218    379       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND      49     56       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF         5     33       Q motif.
FT   MOTIF       155    158       DEAD box.
SQ   SEQUENCE   458 AA;  51573 MW;  3658721717B36EB6 CRC64;
     MVYLKNFLEL GISETFNHTL RENGITEATP IQEKAIPVIL SGKDIIGQAK TGTGKTLAFV
     LPILEKIDPE CSDVQALIVA PTRELALQIT TEIKKMLVQR EDINVLAIYG GQDVAQQLRK
     LKGNTHIVVA TPGRLLDHIR RETIDLSNLS TIVLDEADQM LYFGFLYDIE DILDETPGSK
     QTMLFSATMP KDIKKLAKRY MDEPQMIQVQ SEEVTVDTIE QRVIETTDRA KPDALRFVMD
     RDQPFLAVIF CRTKVRASKL YDNLKGLGYN CAELHGDIPQ AKRERVMKSF REAKIQYLIA
     TDVAARGLDV DGVTHVFNYD IPEDVESYIH RIGRTGRAGG SGLAITFVAA KDEKHLEEIE
     KTLGAPIQRE IIEQPKIKRV DENGKPVPKP APKKSGQNRQ RDSREGSRSD SRRDSRNSSR
     SDSRNSSRNS SRNENNRSFN KPSNKKGSTK QGQQRRGR
//
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