ID E9DKN0_9STRE Unreviewed; 528 AA.
AC E9DKN0;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=DEAD-box ATP-dependent RNA helicase CshA {ECO:0000256|HAMAP-Rule:MF_01493};
DE EC=3.6.4.13 {ECO:0000256|HAMAP-Rule:MF_01493};
GN Name=cshA {ECO:0000256|HAMAP-Rule:MF_01493,
GN ECO:0000313|EMBL:EFX55589.1};
GN ORFNames=HMPREF0848_01186 {ECO:0000313|EMBL:EFX55589.1};
OS Streptococcus sp. C150.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=435842 {ECO:0000313|EMBL:EFX55589.1, ECO:0000313|Proteomes:UP000005993};
RN [1] {ECO:0000313|EMBL:EFX55589.1, ECO:0000313|Proteomes:UP000005993}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C150 {ECO:0000313|EMBL:EFX55589.1,
RC ECO:0000313|Proteomes:UP000005993};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Earl A., Feldgarden M., Gevers D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Borenstein D., Chapman S.B., Chen Z., Engels R.,
RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E.R.,
RA Heiman D.I., Hepburn T.A., Howarth C., Jen D., Larson L., Mehta T.,
RA Park D., Pearson M., Richards J., Roberts A., Saif S., Shea T.D.,
RA Shenoy N., Sisk P., Stolte C., Sykes S.N., Walk T., White J., Yandava C.,
RA Sibley C.D., Field T.R., Grinwis M., Eshaghurshan C.S., Surette M.G.,
RA Haas B., Nusbaum C., Birren B.;
RT "The Genome Sequence of Streptococcus sp. C150.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-Rule:MF_01493};
CC -!- SUBUNIT: Oligomerizes, may be a member of the RNA degradosome.
CC {ECO:0000256|HAMAP-Rule:MF_01493}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01493}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. CshA subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01493}.
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DR EMBL; GL698449; EFX55589.1; -; Genomic_DNA.
DR RefSeq; WP_008535313.1; NZ_GL698449.1.
DR AlphaFoldDB; E9DKN0; -.
DR eggNOG; COG0513; Bacteria.
DR HOGENOM; CLU_003041_21_0_9; -.
DR Proteomes; UP000005993; Unassembled WGS sequence.
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 CDD; cd00268; DEADc; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 PANTHER; PTHR47963; DEAD-BOX ATP-DEPENDENT RNA HELICASE 47, MITOCHONDRIAL; 1.
DR PANTHER; PTHR47963:SF5; DEAD-BOX ATP-DEPENDENT RNA HELICASE CSHA; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01493}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01493};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_01493};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01493};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01493}; RNA-binding {ECO:0000256|HAMAP-Rule:MF_01493};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_01493}.
FT DOMAIN 1..29
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 32..202
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 213..373
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 439..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1..29
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 460..528
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 528 AA; 59198 MW; AC94FF88A98F2458 CRC64;
MKFTDLNLSE DIQSAVVAAG FEKPSPIQEL TIPLALEGKD VIGQAQTGTG KTAAFGLPTL
DKIRTEENTI QALVIAPTRE LAVQSQEELF RFGRDKGVKV RSVYGGSSIE KQIKALRSGA
HIVVGTPGRL LDLIKRKALK LNNIETLILD EADEMLNMGF LEDIEAIISR VPEERQTLLF
SATMPDAIKR IGVQFMKDPE HVKIKAKELT NVNVDQYFIR VKEQEKFDTM TRLMDVDQPE
LSIVFGRTKR RVDELTRGLK LRGFRAEGIH GDLDQNKRLR VIRDFKNDQI DILVATDVAA
RGLDISGVTH VYNYDIPQDP ESYVHRIGRT GRAGQSGQSI TFVAPNEMGY LGIIENLTKK
RMKGLKPPTA QEAFQAKKKV ALKKIERDFA DEAIRSNFDK FKGDAVKLAQ EFTPEELALY
ILSLTVQDPE TMPEVEIARE KPLPFKPSGG GFGGKGGKGG RGNRGRDNNR RGGYRGDRNR
DDRDGGRRDF KRKSKKNSRD FENHGNKRPH RTSSEKKNGF VIRNKGDK
//
