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Database: UniProt
Entry: P96614
LinkDB: P96614
Original site: P96614 
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   16-OCT-2019, entry version 132.
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
RT   Bacillus 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.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   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.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   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
RT   Bacillus 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
RP   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,
RT   and RNA 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.,
RA   Marahiel M.A.;
RT   "Cold-induced putative DEAD box RNA helicases CshA and CshB are
RT   essential for cold adaptation and interact with cold shock protein B
RT   in Bacillus 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
RT   the 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.,
RA   Rodrigues C., Herzberg C., Commichau F.M., Lewis R.J., Stulke J.;
RT   "RNase Y in Bacillus subtilis: a natively disordered protein that is
RT   the 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
RT   and act independently from each other.";
RL   J. Bacteriol. 195:534-544(2013).
CC   -!- FUNCTION: The most abundant DEAD-box RNA helicase. An ATP-
CC       dependent RNA helicase with RNA-dependent ATPase activity. May
CC       work in conjunction with the cold shock proteins to ensure proper
CC       initiation of transcription at low and optimal temperatures. In
CC       vitro, unwinds dsRNA in both 5'- and 3'- directions. Plays a role
CC       in ribosomal 50S subunit assembly. Its deletion leads to changes
CC       in mRNA levels for over 200 transcripts.
CC       {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
CC       CshB and DbpA (DeaD). Probably a component of the RNA degradosome
CC       complex composed of rny, rnjA, rnjB, pnp, pfkA and eno, and
CC       possibly also rnpA (although rnjA and rnjB's presence is unclear).
CC       Interacts with ribosomal proteins L1 and L3 (rplA and rplC) and
CC       the protein component 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.
CC       Note=Shows transcription-dependent localization at subcellular
CC       sites surrounding the nucleoid (PubMed:16352840). Associated with
CC       free 50S ribosomal subunit, 70S ribosome and polysomes
CC       (PubMed:16861794). Cell membrane association shown in
CC       (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
CC       and in exponential, transition and stationary phase (at protein
CC       level) (PubMed:20572937, PubMed:23175651). Protein level not
CC       increased at 16 degrees Celsius (at protein level)
CC       (PubMed:20572937). {ECO:0000269|PubMed:12399512,
CC       ECO:0000269|PubMed:16352840, ECO:0000269|PubMed:20572937,
CC       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,
CC       whereas dimerization or oligomerization only requires the extreme
CC       C-terminus (residues 413-494). Addition of the latter domain to
CC       CshB confers on it the ability to interact with Rny.
CC       {ECO:0000269|PubMed:20572937}.
CC   -!- DISRUPTION PHENOTYPE: Slow vegetative growth at 37 degrees
CC       Celsius, impaired growth at 22 degrees Celsius (PubMed:16861794)
CC       and 16 degrees Celsius (PubMed:23175651). Another report shows no
CC       growth difference at 15 degrees Celsius (PubMed:16352840). The
CC       presence of CshA or CshB is essential for viability; in a cshA
CC       disruption mutant further depletion of cshB stops growth after 1
CC       cell duplication (PubMed:16352840). Others show a quadruple
CC       disruption of all RNA helicases (cshA, cshB, deaD, yfmL) was not
CC       lethal at 37 degrees Celsius, although both 50S and 70S ribosomes
CC       are decreased, growth stops at 16 degrees (PubMed:23175651). At 20
CC       degrees Celsius cells are elongated and wrinkled, with smaller
CC       cell diameter and thickened walls, and decreased amounts of 70S
CC       and 50S 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
CC       subfamily. {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;
KW   ATP-binding; Cell membrane; Complete proteome; Cytoplasm; Helicase;
KW   Hydrolase; Membrane; Nucleotide-binding; Reference proteome;
KW   Ribosome biogenesis; RNA-binding; Stress response.
FT   CHAIN         1    494       DEAD-box ATP-dependent RNA helicase CshA.
FT                                /FTId=PRO_0000280054.
FT   DOMAIN       34    204       Helicase ATP-binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01493}.
FT   DOMAIN      215    375       Helicase C-terminal. {ECO:0000255|HAMAP-
FT                                Rule:MF_01493}.
FT   NP_BIND      47     54       ATP. {ECO:0000255|HAMAP-Rule:MF_01493}.
FT   REGION      413    494       Required for dimerization or
FT                                oligomerization.
FT   MOTIF         3     31       Q motif.
FT   MOTIF       152    155       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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