(data stored in ACNUC7421 zone)

SWISSPROT: CSHA_BACSU

ID   CSHA_BACSU              Reviewed;         494 AA.
AC   P96614; Q797L0;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 2.
DT   11-DEC-2019, entry version 133.
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}; Synonyms=ydbR;
GN   OrderedLocusNames=BSU04580;
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;
RA   Kasahara Y., Nakai S., Lee S., Sadaie Y., Ogasawara N.;
RT   "A 148 kbp sequence of the region between 35 and 47 degree of the Bacillus
RT   subtilis genome.";
RL   Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
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 AS AN ATPASE, FUNCTION AS AN RNA HELICASE, COFACTOR, ACTIVITY
RP   REGULATION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND RNA-BINDING.
RC   STRAIN=168;
RX   PubMed=16861794; DOI=10.1271/bbb.50678;
RA   Ando Y., Nakamura K.;
RT   "Bacillus subtilis DEAD protein YdbR possesses ATPase, RNA binding, and RNA
RT   unwinding activities.";
RL   Biosci. Biotechnol. Biochem. 70:1606-1615(2006).
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND 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   [6]
RP   SUBUNIT, SUBCELLULAR LOCATION, INDUCTION, AND DOMAIN.
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   [7]
RP   INTERACTION WITH RNY, AND SUBUNIT.
RC   STRAIN=168;
RX   PubMed=21803996; DOI=10.1128/jb.05500-11;
RA   Lehnik-Habrink M., Newman J., Rothe F.M., Solovyova A.S., Rodrigues C.,
RA   Herzberg C., Commichau F.M., Lewis R.J., Stulke J.;
RT   "RNase Y in Bacillus subtilis: a natively disordered protein that is the
RT   functional equivalent of RNase E from Escherichia coli.";
RL   J. Bacteriol. 193:5431-5441(2011).
RN   [8]
RP   INTERACTION WITH RNPA, AND SUBUNIT.
RX   PubMed=21764917; DOI=10.1128/jb.05485-11;
RA   Roux C.M., DeMuth J.P., Dunman P.M.;
RT   "Characterization of components of the Staphylococcus aureus mRNA
RT   degradosome holoenzyme-like complex.";
RL   J. Bacteriol. 193:5520-5526(2011).
RN   [9]
RP   FUNCTION, INTERACTION WITH RPLA AND RPLC, SUBUNIT, INDUCTION, AND
RP   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: The most abundant DEAD-box RNA helicase. An ATP-dependent RNA
CC       helicase with RNA-dependent ATPase activity. May work in conjunction
CC       with the cold shock proteins to ensure proper initiation of
CC       transcription at low and optimal temperatures. In vitro, unwinds dsRNA
CC       in both 5'- and 3'- directions. Plays a role in ribosomal 50S subunit
CC       assembly. Its deletion leads to changes in mRNA levels for over 200
CC       transcripts. {ECO:0000269|PubMed:16352840, ECO:0000269|PubMed:16861794,
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_01493};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000305|PubMed:16861794};
CC   -!- ACTIVITY REGULATION: RNA helicase activity is inhibited by EDTA.
CC       {ECO:0000269|PubMed:16861794}.
CC   -!- SUBUNIT: Homodimer or oligomer. May interact with RNA helicases CshB
CC       and DbpA (DeaD). Probably a component of the RNA degradosome complex
CC       composed of rny, rnjA, rnjB, pnp, pfkA and eno, and possibly also rnpA
CC       (although rnjA and rnjB's presence is unclear). Interacts with
CC       ribosomal proteins L1 and L3 (rplA and rplC) and the protein component
CC       of RNase RnpA. {ECO:0000269|PubMed:20572937,
CC       ECO:0000269|PubMed:21764917, ECO:0000269|PubMed:21803996,
CC       ECO:0000269|PubMed:23175651}.
CC   -!- INTERACTION:
CC       O31774:rny; NbExp=2; IntAct=EBI-6415210, EBI-6415578;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid. Cell membrane. Note=Shows
CC       transcription-dependent localization at subcellular sites surrounding
CC       the nucleoid (PubMed:16352840). Associated with free 50S ribosomal
CC       subunit, 70S ribosome and polysomes (PubMed:16861794). Cell membrane
CC       association shown in (PubMed:20572937). {ECO:0000269|PubMed:16352840,
CC       ECO:0000269|PubMed:16861794, ECO:0000269|PubMed:20572937}.
CC   -!- INDUCTION: Induced by cold shock (PubMed:12399512). Constitutively
CC       expressed at 37 and 16 degrees Celsius in rich and minimal medium and
CC       in exponential, transition and stationary phase (at protein level)
CC       (PubMed:20572937, PubMed:23175651). Protein level not increased at 16
CC       degrees Celsius (at protein level) (PubMed:20572937).
CC       {ECO:0000269|PubMed:12399512, ECO:0000269|PubMed:16352840,
CC       ECO:0000269|PubMed:20572937, ECO:0000269|PubMed:23175651}.
CC   -!- DOMAIN: The C-terminal half of the protein (residues 225-494) is
CC       required for interaction with most RNA degradosome partners, whereas
CC       dimerization or oligomerization only requires the extreme C-terminus
CC       (residues 413-494). Addition of the latter domain to CshB confers on it
CC       the ability to interact with Rny. {ECO:0000269|PubMed:20572937}.
CC   -!- DISRUPTION PHENOTYPE: Slow vegetative growth at 37 degrees Celsius,
CC       impaired growth at 22 degrees Celsius (PubMed:16861794) and 16 degrees
CC       Celsius (PubMed:23175651). Another report shows no growth difference at
CC       15 degrees Celsius (PubMed:16352840). The presence of CshA or CshB is
CC       essential for viability; in a cshA disruption mutant further depletion
CC       of cshB stops growth after 1 cell duplication (PubMed:16352840). Others
CC       show a quadruple disruption of all RNA helicases (cshA, cshB, deaD,
CC       yfmL) was not lethal at 37 degrees Celsius, although both 50S and 70S
CC       ribosomes are decreased, growth stops at 16 degrees (PubMed:23175651).
CC       At 20 degrees Celsius cells are elongated and wrinkled, with smaller
CC       cell diameter and thickened walls, and decreased amounts of 70S and 50S
CC       ribosomes; levels of over 200 transcripts are altered
CC       (PubMed:23175651). {ECO:0000269|PubMed:16352840,
CC       ECO:0000269|PubMed:16861794, ECO:0000269|PubMed:23175651}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. CshA subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01493}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA19295.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
DR   EMBL; AB001488; BAA19295.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AL009126; CAB12265.2; -; Genomic_DNA.
DR   PIR; D69772; D69772.
DR   RefSeq; NP_388339.1; NC_000964.3.
DR   RefSeq; WP_003246685.1; NC_000964.3.
DR   SMR; P96614; -.
DR   IntAct; P96614; 3.
DR   MINT; P96614; -.
DR   STRING; 224308.BSU04580; -.
DR   jPOST; P96614; -.
DR   PaxDb; P96614; -.
DR   PRIDE; P96614; -.
DR   DNASU; 938170; -.
DR   EnsemblBacteria; CAB12265; CAB12265; BSU04580.
DR   GeneID; 938170; -.
DR   KEGG; bsu:BSU04580; -.
DR   PATRIC; fig|224308.179.peg.486; -.
DR   eggNOG; ENOG4105C1J; Bacteria.
DR   eggNOG; COG0513; LUCA.
DR   HOGENOM; HOG000268810; -.
DR   InParanoid; P96614; -.
DR   KO; K05592; -.
DR   OMA; RNPIRIL; -.
DR   BioCyc; BSUB:BSU04580-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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR   GO; GO:0003724; F:RNA helicase activity; IDA: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   GO; GO:0010501; P:RNA secondary structure unwinding; IDA:UniProtKB.
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   1: Evidence at protein level;
DR   PRODOM; P96614.
DR   SWISS-2DPAGE; P96614.
KW   ATP-binding; Cell membrane; Cytoplasm; Helicase; Hydrolase; Membrane;
KW   Nucleotide-binding; Reference proteome; Ribosome biogenesis; RNA-binding;
KW   Stress response.
FT   CHAIN           1..494
FT                   /note="DEAD-box ATP-dependent RNA helicase CshA"
FT                   /id="PRO_0000280054"
FT   DOMAIN          34..204
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01493"
FT   DOMAIN          215..375
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01493"
FT   NP_BIND         47..54
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01493"
FT   REGION          413..494
FT                   /note="Required for dimerization or oligomerization"
FT   MOTIF           3..31
FT                   /note="Q motif"
FT   MOTIF           152..155
FT                   /note="DEAD box"
SQ   SEQUENCE   494 AA;  55330 MW;  A44C5EAE314E46ED CRC64;
     MTITFQDFNL SSDLMKAINR MGFEEATPIQ AQTIPLGLSN KDVIGQAQTG TGKTAAFGIP
     LVEKINPESP NIQAIVIAPT RELAIQVSEE LYKIGQDKRA KVLPIYGGQD IGRQIRALKK
     NPNIIVGTPG RLLDHINRRT IRLNNVNTVV MDEADEMLNM GFIDDIESIL SNVPSEHQTL
     LFSATMPAPI KRIAERFMTE PEHVKVKAKE MTVSNIQQFY LEVQERKKFD TLTRLLDIQS
     PELAIVFGRT KRRVDELAEA LNLRGYAAEG IHGDLTQAKR MVALRKFKEG AIEVLVATDV
     AARGLDISGV THVYNFDVPQ DPESYVHRIG RTGRAGKTGM AMTFITPREK SMLRAIEQTT
     KRKMDRMKEP TLDEALEGQQ QVTVERLRTT ISENNLNFYM TAAAELLEDH DAVTVVAAAI
     KMATKEPDDT PVRLTDEAPM VSKRYKNQRS SKRRDGQGGG YRGGKGKSNN RSSYDKKRSN
     DRRSSGDRRQ KKSY
//

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