CSHA_STRPN
ID CSHA_STRPN Reviewed; 524 AA.
AC P0A4D7; P35599;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=SP_1586;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
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; AE005672; AAK75672.1; -; Genomic_DNA.
DR PIR; G95184; G95184.
DR RefSeq; WP_000671113.1; NZ_AKVY01000001.1.
DR AlphaFoldDB; P0A4D7; -.
DR SMR; P0A4D7; -.
DR STRING; 170187.SP_1586; -.
DR EnsemblBacteria; AAK75672; AAK75672; SP_1586.
DR GeneID; 60234437; -.
DR KEGG; spn:SP_1586; -.
DR eggNOG; COG0513; Bacteria.
DR OMA; EHKDGQR; -.
DR PhylomeDB; P0A4D7; -.
DR BioCyc; SPNE170187:G1FZB-1605-MON; -.
DR Proteomes; UP000000585; Chromosome.
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..524
FT /note="DEAD-box ATP-dependent RNA helicase CshA"
FT /id="PRO_0000055119"
FT DOMAIN 32..202
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01493"
FT DOMAIN 213..373
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01493"
FT REGION 440..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1..29
FT /note="Q motif"
FT MOTIF 150..153
FT /note="DEAD box"
FT COMPBIAS 459..508
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 45..52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01493"
SQ SEQUENCE 524 AA; 58827 MW; B6523D038C2F1EF4 CRC64;
MKFNELNLSA DLLAEIEKAG FVEASPIQEQ TIPLALEGKD VIGQAQTGTG KTAAFGLPTL
EKIRTEEATI QALVIAPTRE LAVQSQEELF RFGRSKGVKV RSVYGGSSIE KQIKALKSGA
HIVVGTPGRL LDLIKRKALK LQDIETLILD EADEMLNMGF LEDIEAIISR VPENRQTLLF
SATMPDAIKR IGVQFMKAPE HVKIAAKELT TELVDQYYIR VKEQEKFDTM TRLMDVAQPE
LAIVFGRTKR RVDELTRGLK IRGFRAEGIH GDLDQNKRLR VLRDFKNGNL DVLVATDVAA
RGLDISGVTH VYNYDIPQDP ESYVHRIGRT GRAGKSGQSI TFVAPNEMGY LQIIENLTKK
RMKGLKPASV EESFQSKKQV ALKKIERDFA DETIRANFEK FGKDARKLAA EFTPEELAMY
ILSLTVQDPD SLPEVEIARE KPLPFKPSGN GFGGKAKGGR GGRRGDDRRE RDRRGNGRRD
EFKKGSRGND RFDKEKRYRK DNKKPRNTLS EKQTGFVIRN KGDK