ID   RHLB_SHEB2              Reviewed;         438 AA.
AC   B8E670;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=Sbal223_3876;
OS   Shewanella baltica (strain OS223).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=407976;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS223;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Meincke L., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Ovchinnikova G., Brettar I., Rodrigues J., Konstantinidis K.,
RA   Tiedje J.;
RT   "Complete sequence of chromosome of Shewanella baltica OS223.";
RL   Submitted (DEC-2008) 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}.
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; CP001252; ACK48351.1; -; Genomic_DNA.
DR   RefSeq; WP_006083359.1; NC_011663.1.
DR   AlphaFoldDB; B8E670; -.
DR   SMR; B8E670; -.
DR   EnsemblBacteria; ACK48351; ACK48351; Sbal223_3876.
DR   KEGG; sbp:Sbal223_3876; -.
DR   HOGENOM; CLU_003041_28_3_6; -.
DR   OMA; EYCTPIQ; -.
DR   Proteomes; UP000002507; 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..438
FT                   /note="ATP-dependent RNA helicase RhlB"
FT                   /id="PRO_1000147584"
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..438
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   438 AA;  49115 MW;  B65877A12555C4D0 CRC64;
     MSETHLSTQR FADLPLHPEV KQALAENGFE FCTPIQALSL PVLLQSKDIA GQAQTGTGKT
     MAFLVATFNH LLSTPVPEGR LINQPRAIIM APTRELAIQI AKDAILLAKH THLKVGIVYG
     GESYDVQRKV LDQGVDILIG TTGRIIDYVR QGIIGLNSIQ AVVLDEADRM FDLGFIKDIR
     FLFRRMPEAN QRLNMLFSAT LSMKVQELAY DHMNEPVKVE IAPEEKTSKN IKEEIFYPSQ
     EEKMRLLLTL IEEDWPEKAI VFSNTKHSCE TLWSWLEGDG HRVGLLTGDV PQKKRIRILE
     QFTSGQLDIL VATDVAARGL HISDVSHVYN YDLPDDCEDY VHRIGRTGRA GNKGMSISFA
     CEEYALNLPA IESYINHSIP VSNYDSEALL ADIPTPAKIH RKHPSGTRNL RDRSGTSRPG
     AQRSGARPPR HDRTRRHS