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Database: UniProt
Entry: Q81IT9
LinkDB: Q81IT9
Original site: Q81IT9 
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   16-OCT-2019, entry version 110.
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=BC_0259;
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=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
RT   ATCC 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 / 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 possibly involved in RNA
CC       degradation. May work in conjunction with the cold shock proteins
CC       to ensure proper initiation of transcription at low and optimal
CC       temperatures. Unwinds dsRNA in both 5'- and 3'-directions and
CC       shows RNA-dependent ATPase activity (By similarity). Probably has
CC       a somewhat redundant function with cshB, as cshA can partially
CC       complement the growth effects of a cshB deletion. Plays a role in
CC       adaptation to cold, oxididant and pH stress. {ECO:0000250,
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         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
CC       10, 30 or 37 degrees Celsius. Induced at 10 degrees Celsius.
CC       Encoded by a 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
CC       growth rate between 20 and 45 degrees Celsius, no growth at 10
CC       degrees Celsius. At 15 degrees Celsius the unusually long cells
CC       form large aggregates and are curved at the pole, with
CC       incompletely divided, thickened internal membranes. Decreased
CC       growth in the presence of H(2)O(2), diamide and at acidic and
CC       basic pH. {ECO:0000269|PubMed:20370835,
CC       ECO:0000269|PubMed:20709848, ECO:0000269|PubMed:21705526}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. CshA
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01493}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAP07328.1; Type=Frameshift; Evidence={ECO:0000305};
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   SMR; Q81IT9; -.
DR   PRIDE; Q81IT9; -.
DR   DNASU; 1202612; -.
DR   EnsemblBacteria; AAP07328; AAP07328; BC_0259.
DR   GeneID; 1202612; -.
DR   KEGG; bce:BC0259; -.
DR   PATRIC; fig|226900.8.peg.259; -.
DR   eggNOG; COG0513; LUCA.
DR   KO; K05592; -.
DR   OMA; RNPIRIL; -.
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: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   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; Complete proteome; Cytoplasm; Helicase; Hydrolase;
KW   Nucleotide-binding; Reference proteome; RNA-binding; Stress response.
FT   CHAIN         1    533       DEAD-box ATP-dependent RNA helicase CshA.
FT                                /FTId=PRO_0000280051.
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    530       Arg/Gly-rich.
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
//
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