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 03-AUG-2022, entry version 145.
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 SUBUNIT.
RC STRAIN=168;
RX PubMed=21710567; DOI=10.1002/pmic.201000790;
RA Delumeau O., Lecointe F., Muntel J., Guillot A., Guedon E., Monnet V.,
RA Hecker M., Becher D., Polard P., Noirot P.;
RT "The dynamic protein partnership of RNA polymerase in Bacillus subtilis.";
RL Proteomics 11:2992-3001(2011).
RN [10]
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. Interacts with the RNA polymerase core
CC (PubMed:21710567). {ECO:0000269|PubMed:20572937,
CC ECO:0000269|PubMed:21710567, ECO:0000269|PubMed:21764917,
CC ECO:0000269|PubMed:21803996, ECO:0000269|PubMed:23175651}.
CC -!- INTERACTION:
CC P96614; 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};
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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; NZ_JNCM01000031.1.
DR AlphaFoldDB; P96614; -.
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; BSU_04580.
DR GeneID; 938170; -.
DR KEGG; bsu:BSU04580; -.
DR PATRIC; fig|224308.179.peg.486; -.
DR eggNOG; COG0513; Bacteria.
DR InParanoid; P96614; -.
DR OMA; EHKDGQR; -.
DR BioCyc; BSUB:BSU04580-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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
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 Gene3D; 3.40.50.300; -; 2.
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; 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 REGION 413..494
FT /note="Required for dimerization or oligomerization"
FT REGION 429..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 3..31
FT /note="Q motif"
FT MOTIF 152..155
FT /note="DEAD box"
FT COMPBIAS 429..443
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..488
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 47..54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01493"
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
