(data stored in SCRATCH zone)

SWISSPROT: 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   11-DEC-2019, entry version 133.
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}.
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   SMR; P54475; -.
DR   IntAct; P54475; 1.
DR   STRING; 224308.BSU25140; -.
DR   PaxDb; P54475; -.
DR   PRIDE; P54475; -.
DR   EnsemblBacteria; CAB14444; CAB14444; BSU25140.
DR   GeneID; 937908; -.
DR   KEGG; bsu:BSU25140; -.
DR   PATRIC; fig|224308.179.peg.2733; -.
DR   eggNOG; COG0513; LUCA.
DR   HOGENOM; HOG000268806; -.
DR   InParanoid; P54475; -.
DR   KO; K18692; -.
DR   OMA; DWNLMSS; -.
DR   PhylomeDB; P54475; -.
DR   BioCyc; BSUB:BSU25140-MONOMER; -.
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: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   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;
DR   PRODOM; P54475.
DR   SWISS-2DPAGE; P54475.
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   NP_BIND         48..55
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01494"
FT   MOTIF           4..32
FT                   /note="Q motif"
FT   MOTIF           156..159
FT                   /note="DEAD box"
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
//

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