CSHB_STAA8
ID CSHB_STAA8 Reviewed; 448 AA.
AC Q2FY15;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=DEAD-box ATP-dependent RNA helicase CshB {ECO:0000255|HAMAP-Rule:MF_01494};
DE EC=3.6.4.13 {ECO:0000255|HAMAP-Rule:MF_01494};
GN Name=cshB {ECO:0000255|HAMAP-Rule:MF_01494};
GN OrderedLocusNames=SAOUHSC_01659;
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 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).
CC -!- FUNCTION: Probable DEAD-box RNA helicase. May work in conjunction with
CC the cold shock proteins to ensure proper initiation of transcription at
CC low and optimal temperatures. {ECO:0000255|HAMAP-Rule:MF_01494}.
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_01494};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01494}.
CC -!- DISRUPTION PHENOTYPE: Cold sensitive. Double cshB-nfo mutants are as
CC cold-sensitive as the single cshB mutant.
CC {ECO:0000269|PubMed:22447609}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. CshB subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01494}.
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DR EMBL; CP000253; ABD30734.1; -; Genomic_DNA.
DR RefSeq; WP_001062180.1; NZ_LS483365.1.
DR RefSeq; YP_500170.1; NC_007795.1.
DR AlphaFoldDB; Q2FY15; -.
DR SMR; Q2FY15; -.
DR STRING; 1280.SAXN108_1580; -.
DR PRIDE; Q2FY15; -.
DR EnsemblBacteria; ABD30734; ABD30734; SAOUHSC_01659.
DR GeneID; 3920110; -.
DR KEGG; sao:SAOUHSC_01659; -.
DR PATRIC; fig|93061.5.peg.1509; -.
DR eggNOG; COG0513; Bacteria.
DR HOGENOM; CLU_003041_1_3_9; -.
DR OMA; IKPICRK; -.
DR PRO; PR:Q2FY15; -.
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:0009409; P:response to cold; IEA:InterPro.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IBA:GO_Central.
DR GO; GO:0006401; P:RNA catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_01494; DEAD_helicase_CshB; 1.
DR InterPro; IPR030881; CshB.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
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; 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 Reference proteome; RNA-binding; Stress response.
FT CHAIN 1..448
FT /note="DEAD-box ATP-dependent RNA helicase CshB"
FT /id="PRO_0000430111"
FT DOMAIN 35..206
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01494"
FT DOMAIN 236..386
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01494"
FT REGION 400..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 4..32
FT /note="Q motif"
FT MOTIF 154..157
FT /note="DEAD box"
FT COMPBIAS 400..414
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..435
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 48..55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01494"
SQ SEQUENCE 448 AA; 51081 MW; 3D64906033C2D138 CRC64;
MAKHPFEQFN LESSLIDAVK DLNFEKPTEI QNRIIPRILK RTNLIGQSQT GTGKSHAFLL
PLMQLIDSEI KEPQAIVVAP TRELAQQLYD AANHLSQFKA GVSVKVFIGG TDIEKDRQRC
NAQPQLIIGT PTRINDLAKT GHLHVHLASY LVIDEADLMI DLGLIEDVDY IAARLEDNAN
IAVFSATIPQ QLQPFLNKYL SHPEYVAVDS KKQNKKNIEF YLIPTKGAAK VEKTLNLIDI
LNPYLCIIFC NSRDNANDLA RSLNEAGIKV GMIHGGLTPR ERKQQMKRIR NLEFQYVIAS
DLASRGIDIE GVSHVINFDV PNDIDFFTHR VGRTGRGNYK GVAITLYSPD EEHNISLIED
RGFVFNTVDI KDGELKEVKA HNQRQARMRK DDHLTNQVKN KVRSKIKNKV KPGYKKKFKQ
EVEKMKRQER KQFSKQQNRQ KRKQNKKG
