ID   RHLB_SHESH              Reviewed;         435 AA.
AC   A8G0U0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 92.
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=Ssed_4109;
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) 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; CP000821; ABV38713.1; -; Genomic_DNA.
DR   RefSeq; WP_012144443.1; NC_009831.1.
DR   AlphaFoldDB; A8G0U0; -.
DR   SMR; A8G0U0; -.
DR   STRING; 425104.Ssed_4109; -.
DR   EnsemblBacteria; ABV38713; ABV38713; Ssed_4109.
DR   KEGG; sse:Ssed_4109; -.
DR   eggNOG; COG0513; Bacteria.
DR   HOGENOM; CLU_003041_1_3_6; -.
DR   OMA; EYCTPIQ; -.
DR   OrthoDB; 626183at2; -.
DR   Proteomes; UP000002015; 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   RNA-binding.
FT   CHAIN           1..435
FT                   /note="ATP-dependent RNA helicase RhlB"
FT                   /id="PRO_1000082867"
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..435
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   COMPBIAS        421..435
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         53..60
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00661"
SQ   SEQUENCE   435 AA;  48868 MW;  B26C623E81FCE6BE CRC64;
     MSETHLSNQK FADFSLQTEI KTALNESGFE YCTPIQALSL PILLQKKDIA GQAQTGTGKT
     LAFLVATFNH LLTTPIPEGR QLNQPRAIIM APTRELAIQI AKDADLLAKH TGLKVGIVYG
     GESYEVQRKV LDKGVDILIG TTGRIIDYVR QGIINVSAIQ AVVLDEADRM FDLGFIKDIR
     FLFRRMPDAK SRLNMLFSAT LSMKVQELAY DHMNEPEKVE IAPNEKTSKN IKEEIFYPSM
     DEKMRLLLTL LEEDWPDKAI VFSNTKHSCE KLWSWLEGDG HRVGLLTGDV PQKKRIRILE
     LFTEGKLDVL VATDVAARGL HISDVSHVYN YDLPDDCEDY VHRIGRTGRA GKKGVSVSFA
     CEEYALNLPA IEEYINHTIP VTNYDSEALL DDIPAPVRVH RKHNSRPQGR SGSGGKPRSG
     NRNAPRRHDK TRRHS