ID   CSHA_STAAS              Reviewed;         506 AA.
AC   Q6G7M9;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 120.
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}; OrderedLocusNames=SAS1985;
OS   Staphylococcus aureus (strain MSSA476).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSSA476;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC   -!- FUNCTION: DEAD-box RNA helicase possibly involved in RNA degradation.
CC       Unwinds dsRNA in both 5'- and 3'-directions, has RNA-dependent ATPase
CC       activity. {ECO:0000255|HAMAP-Rule:MF_01493}.
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   -!- SUBUNIT: Oligomerizes, may be a member of the RNA degradosome.
CC       {ECO:0000255|HAMAP-Rule:MF_01493}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01493}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. CshA subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01493}.
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DR   EMBL; BX571857; CAG43792.1; -; Genomic_DNA.
DR   RefSeq; WP_001178942.1; NC_002953.3.
DR   AlphaFoldDB; Q6G7M9; -.
DR   SMR; Q6G7M9; -.
DR   PRIDE; Q6G7M9; -.
DR   KEGG; sas:SAS1985; -.
DR   HOGENOM; CLU_003041_21_1_9; -.
DR   OMA; EHKDGQR; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006401; P:RNA catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0010501; P:RNA secondary structure unwinding; IEA:InterPro.
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   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Helicase; Hydrolase; Nucleotide-binding;
KW   RNA-binding; Stress response.
FT   CHAIN           1..506
FT                   /note="DEAD-box ATP-dependent RNA helicase CshA"
FT                   /id="PRO_0000284821"
FT   DOMAIN          33..203
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01493"
FT   DOMAIN          214..375
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01493"
FT   REGION          436..506
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           2..30
FT                   /note="Q motif"
FT   MOTIF           150..153
FT                   /note="DEAD box"
FT   COMPBIAS        484..506
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         46..53
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01493"
SQ   SEQUENCE   506 AA;  56942 MW;  715B524C11F4D2D4 CRC64;
     MQNFKELGIS DNTVQSLESM GFKEPTPIQK DSIPYALQGI DILGQAQTGT GKTGAFGIPL
     IEKVVGKQGV QSLILAPTRE LAMQVAEQLR EFSRGQGVQV VTVFGGMPIE RQIKALKKGP
     QIVVGTPGRV IDHLNRRTLK TDGIHTLILD EADEMMNMGF IDDMRFIMDK IPAVQRQTML
     FSATMPKAIQ ALVQQFMKSP KIIKTMNNEM SDPQIEEFYT IVKELEKFDT FTNFLDVHQP
     ELAIVFGRTK RRVDELTSAL ISKGYKAEGL HGDITQAKRL EVLKKFKNDQ INILVATDVA
     ARGLDISGVS HVYNFDIPQD TESYTHRIGR TGRAGKEGIA VTFVNPIEMD YIRQIEDANG
     RKMSALRPPH RKEVLQARED DIKEKVENWM SKESESRLKR ISTELLNEYN DVDLVAALLQ
     ELVEANDEVE VQLTFEKPLS RKGRNGKPSG SRNRNSKRGN PKFDSKSKRS KGYSSKKKST
     KKFDRKEKSS GGSRPMKGRT FADHQK