CSHA_BACCR
ID CSHA_BACCR Reviewed; 533 AA.
AC Q81IT9;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 123.
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}; OrderedLocusNames=BC_0259;
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=20370835; DOI=10.1111/j.1574-6968.2010.01953.x;
RA Broussolle V., Pandiani F., Haddad N., Michaud C., Carlin F.,
RA Nguyen-the C., Brillard J.;
RT "Insertional mutagenesis reveals genes involved in Bacillus cereus ATCC
RT 14579 growth at low temperature.";
RL FEMS Microbiol. Lett. 306:177-183(2010).
RN [4]
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 possibly involved in RNA degradation.
CC May work in conjunction with the cold shock proteins to ensure proper
CC initiation of transcription at low and optimal temperatures. Unwinds
CC dsRNA in both 5'- and 3'-directions and shows RNA-dependent ATPase
CC activity (By similarity). Probably has a somewhat redundant function
CC with cshB, as cshA can partially complement the growth effects of a
CC cshB deletion. Plays a role in adaptation to cold, oxididant and pH
CC stress. {ECO:0000250, 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 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 -!- INDUCTION: More highly expressed in lag than stationary phase at 10, 30
CC or 37 degrees Celsius. Induced at 10 degrees Celsius. Encoded by a
CC monocistronic operon. {ECO:0000269|PubMed:20370835,
CC ECO:0000269|PubMed:20709848, ECO:0000269|PubMed:21705526}.
CC -!- DISRUPTION PHENOTYPE: Longer lag phase and slight reduction in growth
CC rate between 20 and 45 degrees Celsius, no growth at 10 degrees
CC Celsius. At 15 degrees Celsius the unusually long cells form large
CC aggregates and are curved at the pole, with incompletely divided,
CC thickened internal membranes. Decreased growth in the presence of
CC H(2)O(2), diamide and at acidic and basic pH.
CC {ECO:0000269|PubMed:20370835, ECO:0000269|PubMed:20709848,
CC ECO:0000269|PubMed:21705526}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. CshA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01493}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAP07328.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AE016877; AAP07328.1; ALT_FRAME; Genomic_DNA.
DR RefSeq; NP_830127.1; NC_004722.1.
DR RefSeq; WP_000206592.1; NZ_CP034551.1.
DR AlphaFoldDB; Q81IT9; -.
DR SMR; Q81IT9; -.
DR STRING; 226900.BC_0259; -.
DR MetOSite; Q81IT9; -.
DR DNASU; 1202612; -.
DR EnsemblBacteria; AAP07328; AAP07328; BC_0259.
DR GeneID; 67504945; -.
DR KEGG; bce:BC0259; -.
DR PATRIC; fig|226900.8.peg.259; -.
DR HOGENOM; CLU_003041_21_0_9; -.
DR OMA; EHKDGQR; -.
DR Proteomes; UP000001417; Chromosome.
DR GO; GO:0043590; C:bacterial nucleoid; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0003724; F:RNA helicase activity; ISS:UniProtKB.
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 GO; GO:0006401; P:RNA catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0010501; P:RNA secondary structure unwinding; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 2.
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 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Helicase; Hydrolase; Nucleotide-binding;
KW Reference proteome; RNA-binding; Stress response.
FT CHAIN 1..533
FT /note="DEAD-box ATP-dependent RNA helicase CshA"
FT /id="PRO_0000280051"
FT DOMAIN 33..203
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01493"
FT DOMAIN 214..374
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01493"
FT REGION 428..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 2..30
FT /note="Q motif"
FT MOTIF 151..154
FT /note="DEAD box"
FT COMPBIAS 459..509
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 46..53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01493"
SQ SEQUENCE 533 AA; 59457 MW; D7FE819EC5926643 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 SRGGGSKKRG GNGGGYRDGN RNRSRDGRGG GDGRNRDRNR
DGRNRDGNRD RNRDGNRDRN RDGGSRGRRG EGQGRPGSSN GRGERKHHSR PQA
