ID I6CXT2_SHIFL Unreviewed; 432 AA.
AC I6CXT2;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=ATP-dependent RNA helicase DbpA {ECO:0000256|HAMAP-Rule:MF_00965};
DE EC=3.6.4.13 {ECO:0000256|HAMAP-Rule:MF_00965};
GN Name=dbpA {ECO:0000256|HAMAP-Rule:MF_00965,
GN ECO:0000313|EMBL:EIQ24324.1};
GN ORFNames=SFK315_1475 {ECO:0000313|EMBL:EIQ24324.1};
OS Shigella flexneri K-315.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=766150 {ECO:0000313|EMBL:EIQ24324.1, ECO:0000313|Proteomes:UP000005407};
RN [1] {ECO:0000313|EMBL:EIQ24324.1, ECO:0000313|Proteomes:UP000005407}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K-315 {ECO:0000313|EMBL:EIQ24324.1,
RC ECO:0000313|Proteomes:UP000005407};
RA Rasko D., Redman J., Daugherty S.C., Tallon L., Sadzewicz L., Jones K.,
RA Santana-Cruz I., Liu X.;
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: DEAD-box RNA helicase involved in the assembly of the 50S
CC ribosomal subunit. Has an RNA-dependent ATPase activity, which is
CC specific for 23S rRNA, and a 3' to 5' RNA helicase activity that uses
CC the energy of ATP hydrolysis to destabilize and unwind short rRNA
CC duplexes. {ECO:0000256|HAMAP-Rule:MF_00965}.
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_00965};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00965}.
CC -!- DOMAIN: Contains an N-terminal domain that binds non-specifically to
CC RNA and a C-terminal domain that binds specifically and tightly to
CC hairpin 92 of 23S rRNA. {ECO:0000256|HAMAP-Rule:MF_00965}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DbpA subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00965}.
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:EIQ24324.1}.
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DR EMBL; AKMY01000018; EIQ24324.1; -; Genomic_DNA.
DR AlphaFoldDB; I6CXT2; -.
DR PATRIC; fig|766150.3.peg.1437; -.
DR Proteomes; UP000005407; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0034458; F:3'-5' RNA helicase activity; IEA:UniProtKB-UniRule.
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:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR CDD; cd00268; DEADc; 1.
DR CDD; cd12501; RRM_EcDbpA_like; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR HAMAP; MF_00965; DEAD_helicase_DbpA; 1.
DR InterPro; IPR005580; DbpA/CsdA_RNA-bd_dom.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR028619; DEAD_helicase_DbpA.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR PANTHER; PTHR47959:SF19; ATP-DEPENDENT RNA HELICASE DBPA; 1.
DR PANTHER; PTHR47959; ATP-DEPENDENT RNA HELICASE RHLE-RELATED; 1.
DR Pfam; PF03880; DbpA; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00965}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00965};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_00965};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00965};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00965}; Ribosome biogenesis {ECO:0000256|HAMAP-Rule:MF_00965};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_00965}.
FT DOMAIN 9..180
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 205..351
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 358..432
FT /note="Involved in 23S rRNA binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00965"
SQ SEQUENCE 432 AA; 46522 MW; 145356FDF8F99553 CRC64;
MTPVQAAALP AILAGKDVRV QAKTGSGKTA AFGLGLLQQI DASLFQTQAL VLCPTRELAD
QVAGELRRLA RFLPNTKILT LCGGQPFGMQ RDSLQHAPHI IVATPGRLLD HLQKGTVSLD
ALNTLVMDEA DRMLDMGFSD AIDDVIRFAP ASRQTLLFSA SWPEAIAVIS GRVQRDPLAI
EIDSTDALPP IEQQFYETSS KGKIPLLQRL LSLHQPSSCV VFCNTKKDCQ AVCDALNEVG
QSALSLHGDL EQRDRDQTLV RFANGSARVL VATDVAARGL DIKSLELVVN FELAWDPEVH
VHRIGRTARA GNSGLAISFC APEEAQRANI ISDMLQIKLN WQTPPANSSI VPLEAEMATL
CIDGGKKAKM RPGDVLGALT GDIGLDGADI GKIAVHPAHV YVAVRQAVAH KAWKQLQGGK
IKGKTCRVRL LK
//
