CSHA_STAA8
ID CSHA_STAA8 Reviewed; 506 AA.
AC Q2FWH5;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 108.
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};
GN OrderedLocusNames=SAOUHSC_02316;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [2]
RP INTERACTION WITH ENO; PFKA; RNPA AND RNY, AND SUBUNIT.
RC STRAIN=UAMS-1;
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 [3]
RP DISRUPTION PHENOTYPE.
RC STRAIN=SA564;
RX PubMed=22447609; DOI=10.1128/aem.00202-12;
RA Redder P., Linder P.;
RT "New range of vectors with a stringent 5-fluoroorotic acid-based
RT counterselection system for generating mutants by allelic replacement in
RT Staphylococcus aureus.";
RL Appl. Environ. Microbiol. 78:3846-3854(2012).
RN [4]
RP FUNCTION AS AN ATPASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF LYS-52.
RC STRAIN=S30, and SA564;
RX PubMed=23229022; DOI=10.4161/rna.22899;
RA Oun S., Redder P., Didier J.P., Francois P., Corvaglia A.R., Buttazzoni E.,
RA Giraud C., Girard M., Schrenzel J., Linder P.;
RT "The CshA DEAD-box RNA helicase is important for quorum sensing control in
RT Staphylococcus aureus.";
RL RNA Biol. 10:157-165(2013).
CC -!- FUNCTION: A probable ATP-dependent RNA helicase with RNA-dependent
CC ATPase activity. Involved in regulation of biofilm formation and
CC hemolysis via its effects on stability of mRNA from the agrBDCA operon.
CC Also involved in response to cold stress.
CC {ECO:0000269|PubMed:23229022}.
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 ECO:0000269|PubMed:23229022};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.7 mM for ATP {ECO:0000269|PubMed:23229022};
CC Note=kcat 140 min(-1), in strain S30.;
CC -!- SUBUNIT: Homodimer (Probable). Component of a possible RNA degradosome
CC complex composed of cshA, eno, pfkA, pnp, rnjA, rnjB, rnpA and rny.
CC Interacts specifically with enolase, phosphofructokinase and RNases
CC RnpA and Y. {ECO:0000269|PubMed:21764917, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01493}.
CC -!- DISRUPTION PHENOTYPE: In strain S30, cold-sensitive; decreased growth
CC at 30 degrees Celsius, no growth at 20 degrees Celsius. Reduced biofilm
CC formation, increased hemolytic activity, increased stability of mRNAs
CC of the agrBDCA operon. A double agrA-cshA mutation has wild-type
CC biofilm and hemolytic activity (all phenotypes in strain S30).
CC {ECO:0000269|PubMed:22447609, ECO:0000269|PubMed:23229022}.
CC -!- MISCELLANEOUS: All disruption phenotypes were also seen for deletion in
CC strain SA564.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. CshA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01493}.
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DR EMBL; CP000253; ABD31350.1; -; Genomic_DNA.
DR RefSeq; WP_001178942.1; NZ_LS483365.1.
DR RefSeq; YP_500795.1; NC_007795.1.
DR AlphaFoldDB; Q2FWH5; -.
DR SMR; Q2FWH5; -.
DR STRING; 1280.SAXN108_2326; -.
DR EnsemblBacteria; ABD31350; ABD31350; SAOUHSC_02316.
DR GeneID; 3920941; -.
DR KEGG; sao:SAOUHSC_02316; -.
DR PATRIC; fig|93061.5.peg.2099; -.
DR eggNOG; COG0513; Bacteria.
DR HOGENOM; CLU_003041_21_1_9; -.
DR OMA; EHKDGQR; -.
DR BRENDA; 3.6.4.13; 3352.
DR PRO; PR:Q2FWH5; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR GO; GO:0033592; F:RNA strand annealing activity; IBA:GO_Central.
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; 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 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Helicase; Hydrolase; Nucleotide-binding;
KW Reference proteome; RNA-binding; Stress response.
FT CHAIN 1..506
FT /note="DEAD-box ATP-dependent RNA helicase CshA"
FT /id="PRO_0000284825"
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"
FT MUTAGEN 52
FT /note="K->A: Loss of RNA-dependent ATPase. Does not
FT complement disruption mutant at 20 or 30 degrees Celsius,
FT does not resotre biofilm formation."
FT /evidence="ECO:0000269|PubMed:23229022"
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
