CSHC_BACCR
ID CSHC_BACCR Reviewed; 389 AA.
AC Q81E85;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=DEAD-box ATP-dependent RNA helicase CshC;
DE EC=3.6.4.13;
GN Name=cshC; OrderedLocusNames=BC_2103;
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 FUNCTION, 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.
CC {ECO:0000269|PubMed:21705526}.
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: Longer lag phase at 20 degrees Celsius, wild-type
CC growth rate at 30 degrees Celsius, no growth at 10 degrees Celsius. At
CC 12 degrees Celsius cells were short and stocky, by transmission
CC electron microscopy the cytoplasm appears empty although cells are
CC viable. Decreased growth in the presence of H(2)O(2) and diamide.
CC {ECO:0000269|PubMed:20709848, ECO:0000269|PubMed:21705526}.
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DR EMBL; AE016877; AAP09072.1; -; Genomic_DNA.
DR RefSeq; NP_831871.1; NC_004722.1.
DR RefSeq; WP_000588613.1; NZ_CP034551.1.
DR AlphaFoldDB; Q81E85; -.
DR SMR; Q81E85; -.
DR STRING; 226900.BC_2103; -.
DR EnsemblBacteria; AAP09072; AAP09072; BC_2103.
DR GeneID; 59157689; -.
DR GeneID; 64203913; -.
DR GeneID; 67506748; -.
DR KEGG; bce:BC2103; -.
DR PATRIC; fig|226900.8.peg.2118; -.
DR HOGENOM; CLU_003041_1_3_9; -.
DR OMA; TYEDRHT; -.
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 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;
KW Stress response.
FT CHAIN 1..389
FT /note="DEAD-box ATP-dependent RNA helicase CshC"
FT /id="PRO_0000430103"
FT DOMAIN 29..199
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 209..379
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 368..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1..26
FT /note="Q motif"
FT MOTIF 147..150
FT /note="DEAD box"
FT BINDING 42..49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 389 AA; 44067 MW; 91ACD38C5FAC6AB6 CRC64;
MIKDMQPFLQ QAWEKAGFKE LTEIQKQAIP TILEGQDVIA ESPTGTGKTL AYLLPLLHKI
NPEVKQPQVV VLAPTRELVM QIHEEVQKFT AGTEISGASL IGGADIKRQV EKLKKHPRVI
VGSPGRILEL IRMKKLKMHE VKTIVFDEFD QIVKQKMMGA VQDVIKSTMR DRQLVFFSAT
MTKAAEDAAR DLAVEPQLVR VTRAESKSLV EHTYIICERR EKNDYVRRIM HMGDVKAVAF
LNDPFRLDEI TEKLKFRKMK AAALHAEASK QEREATMRAF RGGKLEILLA TDIAARGIDI
DDLTHVIHLE LPDTVDQYIH RSGRTGRMGK EGTVVSLVTP QEERKLLQFA KKLGIVFTKQ
EMFKGSFVET KPKAPKKKKP AFTGKKKPR
