RHLB_ACTSZ
ID RHLB_ACTSZ Reviewed; 413 AA.
AC A6VKC3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=ATP-dependent RNA helicase RhlB {ECO:0000255|HAMAP-Rule:MF_00661};
DE EC=3.6.4.13 {ECO:0000255|HAMAP-Rule:MF_00661};
GN Name=rhlB {ECO:0000255|HAMAP-Rule:MF_00661}; OrderedLocusNames=Asuc_0039;
OS Actinobacillus succinogenes (strain ATCC 55618 / DSM 22257 / CCUG 43843 /
OS 130Z).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=339671;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55618 / DSM 22257 / CCUG 43843 / 130Z;
RX PubMed=21118570; DOI=10.1186/1471-2164-11-680;
RA McKinlay J.B., Laivenieks M., Schindler B.D., McKinlay A.A.,
RA Siddaramappa S., Challacombe J.F., Lowry S.R., Clum A., Lapidus A.L.,
RA Burkhart K.B., Harkins V., Vieille C.;
RT "A genomic perspective on the potential of Actinobacillus succinogenes for
RT industrial succinate production.";
RL BMC Genomics 11:680-680(2010).
CC -!- FUNCTION: DEAD-box RNA helicase involved in RNA degradation. Has RNA-
CC dependent ATPase activity and unwinds double-stranded RNA.
CC {ECO:0000255|HAMAP-Rule:MF_00661}.
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_00661};
CC -!- SUBUNIT: Component of the RNA degradosome, which is a multiprotein
CC complex involved in RNA processing and mRNA degradation.
CC {ECO:0000255|HAMAP-Rule:MF_00661}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00661}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. RhlB subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00661}.
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DR EMBL; CP000746; ABR73420.1; -; Genomic_DNA.
DR RefSeq; WP_011978696.1; NC_009655.1.
DR AlphaFoldDB; A6VKC3; -.
DR SMR; A6VKC3; -.
DR STRING; 339671.Asuc_0039; -.
DR EnsemblBacteria; ABR73420; ABR73420; Asuc_0039.
DR KEGG; asu:Asuc_0039; -.
DR eggNOG; COG0513; Bacteria.
DR HOGENOM; CLU_003041_1_3_6; -.
DR OMA; EYCTPIQ; -.
DR OrthoDB; 626183at2; -.
DR Proteomes; UP000001114; 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 Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_00661; DEAD_helicase_RhlB; 1.
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; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR023554; RNA_helicase_ATP-dep_RhlB.
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 Reference proteome; RNA-binding.
FT CHAIN 1..413
FT /note="ATP-dependent RNA helicase RhlB"
FT /id="PRO_1000082833"
FT DOMAIN 40..217
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00661"
FT DOMAIN 241..388
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00661"
FT MOTIF 9..37
FT /note="Q motif"
FT MOTIF 163..166
FT /note="DEAD box"
FT BINDING 53..60
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00661"
SQ SEQUENCE 413 AA; 46887 MW; 2C027D44C4F336B6 CRC64;
MTTEHLSQQR FADLPLHPQI LAALNDQNFE YCTPIQALSL PLTLQGKDVA GQAQTGTGKT
MAFLTATFHH LLTHQPDFIT NQPRALILAP TRELAVQIAH DAESLAQTTK LRIALAYGGD
GYDKQLKTIE NGVDILIGTT GRVIDYVKQG IIRFNDIQVV VLDEADRMFD LGFIKDIRYL
LRKCPAPKSR LTMLFSATLS YKVRELAFED MNDPEYIEIE PLQKTGHRIK EELFYPSNRD
KMALLMTLLE EEWPERCIIF ANTKHRCEEI WGYLAADGQR VGLLTGDVAQ KKRLALLKQF
TDGELDILVA TDVAARGLHI PDVTHVFNYD LPDDREDYVH RIGRTGRAGE SGMSISFACE
QYAMNLPAIE EYIGHHIPVS QYDPDSLIND LPKPYRIKRN HTIPHSSRDY KKR