RHLB_SHESR
ID RHLB_SHESR Reviewed; 439 AA.
AC Q0HQL1;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
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};
GN OrderedLocusNames=Shewmr7_3614;
OS Shewanella sp. (strain MR-7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=60481;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-7;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Nealson K.,
RA Konstantinidis K., Klappenbach J., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Shewanella sp. MR-7.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000444; ABI44594.1; -; Genomic_DNA.
DR RefSeq; WP_011621214.1; NC_008322.1.
DR AlphaFoldDB; Q0HQL1; -.
DR SMR; Q0HQL1; -.
DR EnsemblBacteria; ABI44594; ABI44594; Shewmr7_3614.
DR KEGG; shm:Shewmr7_3614; -.
DR HOGENOM; CLU_003041_1_3_6; -.
DR OMA; EYCTPIQ; -.
DR OrthoDB; 626183at2; -.
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 RNA-binding.
FT CHAIN 1..439
FT /note="ATP-dependent RNA helicase RhlB"
FT /id="PRO_1000082869"
FT DOMAIN 40..219
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00661"
FT DOMAIN 243..390
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00661"
FT REGION 395..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 9..37
FT /note="Q motif"
FT MOTIF 165..168
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 439 AA; 49302 MW; FC0B5A9AB55A1D8B CRC64;
MSQTHLSNQK FADLPLHPEV KQALAENGFE FCTPIQALSL PVLLQSKDIA GQAQTGTGKT
MAFLVATFNH LLSTPIPENR QLNQPRAIIM APTRELAIQI AKDAILLAKH THLKVGIVYG
GESYDVQRKV LDQGVDILIG TTGRIIDYVR QGIISLNAIQ AVVLDEADRM FDLGFIKDIR
FLFRRMPNAD QRLNMLFSAT LSMKVQELAY DHMNDPVKVE IAPEEKTSKN IKEEIFYPSQ
EDKIRLLLTL IEEDWPEKAI VFSNTKHSCE NLWSWLEGDG HRVGLLTGDV PQKKRIRILE
QFTQGQLDIL VATDVAARGL HISDVSHVYN YDLPDDCEDY VHRIGRTGRA GNKGVSVSFA
CEEYALNLPA IESYINHSIP VSNYDRDALL DDIPPPVKIH RKHPAGARNL RERSGAGRPQ
GAHRSGGRPP RHDRTRRQP