CSHE_BACCR
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 03-AUG-2022, entry version 121.
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 / CCUG 7414 / JCM 2152 / NBRC
OS 15305 / NCIMB 9373 / NCTC 2599 / 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 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC / NCTC 2599 / NRRL B-3711;
RX PubMed=12721630; DOI=10.1038/nature01582;
RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT anthracis.";
RL Nature 423:87-91(2003).
RN [2]
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC / NCTC 2599 / NRRL B-3711;
RX PubMed=20709848; DOI=10.1128/aem.00782-10;
RA Pandiani F., Brillard J., Bornard I., Michaud C., Chamot S., Nguyen-the C.,
RA 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 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC / NCTC 2599 / NRRL 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 cereus
RT 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 ATPase
CC activity and a 3' to 5' RNA helicase activity that uses the energy of
CC ATP hydrolysis to destabilize and unwind short RNA duplexes (By
CC 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. {ECO:0000269|PubMed:20709848,
CC 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}.
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DR EMBL; AE016877; AAP09371.1; -; Genomic_DNA.
DR RefSeq; NP_832170.1; NC_004722.1.
DR RefSeq; WP_002195506.1; NZ_CP034551.1.
DR AlphaFoldDB; Q81DF9; -.
DR SMR; Q81DF9; -.
DR STRING; 226900.BC_2408; -.
DR EnsemblBacteria; AAP09371; AAP09371; BC_2408.
DR KEGG; bce:BC2408; -.
DR PATRIC; fig|226900.8.peg.2436; -.
DR HOGENOM; CLU_003041_28_3_9; -.
DR OMA; FGCQALV; -.
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:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
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 Gene3D; 3.40.50.300; -; 2.
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; Helicase; Hydrolase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..458
FT /note="DEAD-box ATP-dependent RNA helicase CshE"
FT /id="PRO_0000430104"
FT DOMAIN 36..207
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 218..379
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 374..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 5..33
FT /note="Q motif"
FT MOTIF 155..158
FT /note="DEAD box"
FT COMPBIAS 374..388
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..421
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 49..56
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
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
