ID F5VZA0_9STRE Unreviewed; 524 AA.
AC F5VZA0;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-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:EGL87078.1};
GN ORFNames=HMPREF9967_1448 {ECO:0000313|EMBL:EGL87078.1};
OS Streptococcus infantis SK1076.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1005705 {ECO:0000313|EMBL:EGL87078.1, ECO:0000313|Proteomes:UP000010138};
RN [1] {ECO:0000313|EMBL:EGL87078.1, ECO:0000313|Proteomes:UP000010138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK1076 {ECO:0000313|EMBL:EGL87078.1,
RC ECO:0000313|Proteomes:UP000010138};
RA Durkin A.S., Radune D., Hostetler J., Torralba M., Gillis M., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (APR-2011) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGL87078.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AFNN01000010; EGL87078.1; -; Genomic_DNA.
DR RefSeq; WP_006150107.1; NZ_AFNN01000010.1.
DR AlphaFoldDB; F5VZA0; -.
DR eggNOG; COG0513; Bacteria.
DR OrthoDB; 9805696at2; -.
DR Proteomes; UP000010138; 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 440..524
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 459..524
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 524 AA; 58926 MW; 4BCE75AB73094166 CRC64;
MKFNEFNLSA DLLAEIEKAG FVEASPIQEQ TIPLALEGKD VIGQAQTGTG KTAAFGLPTL
EKIHTEDQTI QALVIAPTRE LAVQSQEELF RFGRSKGVKV RSVYGGSSIE KQIKALKSGA
HIVVGTPGRL LDLIKRKALK LQDIETLILD EADEMLNMGF LEDIEAIISR VPENRQTLLF
SATMPEAIKR IGVQFMKDPE HVKIAAKELT TELVDQYYIR VKEQEKFDTM TRLMDVEQPE
LAIVFGRTKR RVDELTRGLK IRGFRAEGIH GDLDQNKRLR VLRDFKNGNL DVLVATDVAA
RGLDISGVTH VYNYDIPQDP ESYVHRIGRT GRAGKSGQSI TFVAPNEMGY LQIIENLTKK
RMKGLKPATA EEAFQAKKHV ALKKIERDFA DESIRGNFDK FAKDARKLAA EFSPEELAMY
ILSLTVQDPD SLPEVEIARE KPLPFKPSGG GFGAKGKSGR GGRRGDDRRD RDRRGNGRRD
DFKKGSRKND RFEKEKRYRK DNKKPRNTSS EKKTGFVIRN KGDK
//
