CSHB_BACSU
ID CSHB_BACSU Reviewed; 438 AA.
AC P54475;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=DEAD-box ATP-dependent RNA helicase CshB {ECO:0000255|HAMAP-Rule:MF_01494};
DE EC=3.6.4.13 {ECO:0000255|HAMAP-Rule:MF_01494};
GN Name=cshB {ECO:0000255|HAMAP-Rule:MF_01494}; Synonyms=yqfR;
GN OrderedLocusNames=BSU25140;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / JH642;
RX PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA Kobayashi Y.;
RT "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT Bacillus subtilis genome containing the skin element and many sporulation
RT genes.";
RL Microbiology 142:3103-3111(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP INDUCTION BY COLD SHOCK.
RC STRAIN=168 / JH642;
RX PubMed=12399512; DOI=10.1128/jb.184.22.6395-6402.2002;
RA Beckering C.L., Steil L., Weber M.H.W., Voelker U., Marahiel M.A.;
RT "Genomewide transcriptional analysis of the cold shock response in Bacillus
RT subtilis.";
RL J. Bacteriol. 184:6395-6402(2002).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CSPB, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=168 / JH642;
RX PubMed=16352840; DOI=10.1128/jb.188.1.240-248.2006;
RA Hunger K., Beckering C.L., Wiegeshoff F., Graumann P.L., Marahiel M.A.;
RT "Cold-induced putative DEAD box RNA helicases CshA and CshB are essential
RT for cold adaptation and interact with cold shock protein B in Bacillus
RT subtilis.";
RL J. Bacteriol. 188:240-248(2006).
RN [5]
RP INTERACTION WITH PNP, SUBUNIT, SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=168;
RX PubMed=20572937; DOI=10.1111/j.1365-2958.2010.07264.x;
RA Lehnik-Habrink M., Pfortner H., Rempeters L., Pietack N., Herzberg C.,
RA Stulke J.;
RT "The RNA degradosome in Bacillus subtilis: identification of CshA as the
RT major RNA helicase in the multiprotein complex.";
RL Mol. Microbiol. 77:958-971(2010).
RN [6]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=23175651; DOI=10.1128/jb.01475-12;
RA Lehnik-Habrink M., Rempeters L., Kovacs A.T., Wrede C., Baierlein C.,
RA Krebber H., Kuipers O.P., Stulke J.;
RT "DEAD-box RNA helicases in Bacillus subtilis have multiple functions and
RT act independently from each other.";
RL J. Bacteriol. 195:534-544(2013).
CC -!- FUNCTION: DEAD-box RNA helicase that plays a role in 70S ribosome
CC assembly. May work in conjunction with the cold shock proteins to
CC ensure proper initiation of transcription at low and optimal
CC temperatures. {ECO:0000269|PubMed:16352840,
CC ECO:0000269|PubMed:23175651}.
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_01494};
CC -!- SUBUNIT: Interacts with CspB when cells are transcriptionally active.
CC May interact with RNA helicases CshA and DbpA (DeaD), may be a
CC component of a possible RNA degradosome complex composed of rny, rnja,
CC rnjb, pnp, pfkA and eno (although rnjA and rnjB's presence is unclear).
CC Specifically interacts with pnp and rny (PubMed:20572937).
CC {ECO:0000269|PubMed:16352840, ECO:0000269|PubMed:20572937}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid {ECO:0000269|PubMed:16352840,
CC ECO:0000269|PubMed:20572937}. Note=Shows transcription-dependent
CC localization at subcellular sites surrounding the nucleoid.
CC -!- INDUCTION: Induced by cold shock (PubMed:12399512). In rich medium
CC highest expression in logarithmic growth, expression decreases and then
CC disappears in stationary phase (at protein level) (PubMed:20572937,
CC PubMed:23175651). Protein level not increased at 16 degrees Celsius.
CC Not detected in minimal medium (at protein level) (PubMed:20572937).
CC {ECO:0000269|PubMed:12399512, ECO:0000269|PubMed:16352840,
CC ECO:0000269|PubMed:20572937, ECO:0000269|PubMed:23175651}.
CC -!- DISRUPTION PHENOTYPE: No difference in growth at 37 or 15 degrees
CC Celsius (PubMed:16352840), decreased growth at 16 degrees Celsius
CC (PubMed:23175651). The presence of CshA or CshB is essential for
CC viability; in a cshA disruption mutant further depletion of cshB stops
CC growth after 1 cell duplication (PubMed:16352840). Others show a
CC quadruple disruption of all RNA helicases (cshA, cshB, deaD, yfmL) was
CC not lethal at 37 degrees Celsius, although both 50S and 70S ribosomes
CC are decreased, but growth stops at 16 degrees (PubMed:23175651). A
CC double cshB-cspB disruption mutant cannot be made. A double cshB-cspD
CC mutant grows slowly at 15 degrees Celsius (PubMed:16352840). Decreased
CC amounts of 70S ribosomes (PubMed:23175651).
CC {ECO:0000269|PubMed:16352840, ECO:0000269|PubMed:23175651}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. {ECO:0000305}.
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DR EMBL; D84432; BAA12495.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14444.1; -; Genomic_DNA.
DR PIR; D69954; D69954.
DR RefSeq; NP_390393.1; NC_000964.3.
DR RefSeq; WP_004399101.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P54475; -.
DR SMR; P54475; -.
DR IntAct; P54475; 1.
DR STRING; 224308.BSU25140; -.
DR PaxDb; P54475; -.
DR PRIDE; P54475; -.
DR EnsemblBacteria; CAB14444; CAB14444; BSU_25140.
DR GeneID; 937908; -.
DR KEGG; bsu:BSU25140; -.
DR PATRIC; fig|224308.179.peg.2733; -.
DR eggNOG; COG0513; Bacteria.
DR InParanoid; P54475; -.
DR OMA; IKPICRK; -.
DR PhylomeDB; P54475; -.
DR BioCyc; BSUB:BSU25140-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0043590; C:bacterial nucleoid; IDA: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:0009409; P:response to cold; IGI:UniProtKB.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IBA:GO_Central.
DR GO; GO:0006401; P:RNA catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_01494; DEAD_helicase_CshB; 1.
DR InterPro; IPR030881; CshB.
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 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Helicase; Hydrolase; Nucleotide-binding;
KW Reference proteome; Ribosome biogenesis; RNA-binding; Stress response.
FT CHAIN 1..438
FT /note="DEAD-box ATP-dependent RNA helicase CshB"
FT /id="PRO_0000055111"
FT DOMAIN 35..208
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01494"
FT DOMAIN 235..385
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01494"
FT REGION 380..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 4..32
FT /note="Q motif"
FT MOTIF 156..159
FT /note="DEAD box"
FT COMPBIAS 414..428
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 48..55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01494"
SQ SEQUENCE 438 AA; 50027 MW; B6D425EF6D433789 CRC64;
MKETKFELYE LKPFIIDAVH RLGFYEPTDI QKRLIPAVLK KESVIGQSQT GTGKTHAYLL
PLLNKIDPAK DVVQVVITAP TRELANQIYQ EALKITQGEE GSQIRSKCFI GGTDKQKSID
KLKIQPHLVV GTPGRIADLI KEQALSVHKA ESLVIDEADL MLDMGFLADV DYIGSRMPED
LQMLVFSATI PEKLKPFLKK YMENPKYAHV EPKQVTAAKI EHILIPSKHR DKDKLLFDIM
SHLNPYLGIV FANTKNTADH IAQYLTGKGM KIGLLHGGLT PRERKKVMKQ INDLEFTYII
ATDLAARGID IKGVSHVINY ELPDDLDFYV HRVGRTARAG SSGQAMTIYE LTDEDALVRL
EKMGIEFEYL ELEKGEWKKG DDRQRRKKRK KTPNEADEIA HRLVKKPKKV KPGYKKKMSY
EMEKIKKKQR RNQSKKRK
