RHLB_SHEHH
ID RHLB_SHEHH Reviewed; 436 AA.
AC B0TJ29;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=Shal_3892;
OS Shewanella halifaxensis (strain HAW-EB4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=458817;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HAW-EB4;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Kim E., Zhao J.-S., Richardson P.;
RT "Complete sequence of Shewanella halifaxensis HAW-EB4.";
RL Submitted (JAN-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}.
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DR EMBL; CP000931; ABZ78432.1; -; Genomic_DNA.
DR RefSeq; WP_012278949.1; NC_010334.1.
DR AlphaFoldDB; B0TJ29; -.
DR SMR; B0TJ29; -.
DR STRING; 458817.Shal_3892; -.
DR EnsemblBacteria; ABZ78432; ABZ78432; Shal_3892.
DR KEGG; shl:Shal_3892; -.
DR eggNOG; COG0513; Bacteria.
DR HOGENOM; CLU_003041_28_3_6; -.
DR OMA; EYCTPIQ; -.
DR OrthoDB; 626183at2; -.
DR Proteomes; UP000001317; 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..436
FT /note="ATP-dependent RNA helicase RhlB"
FT /id="PRO_1000082862"
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 392..436
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 436 AA; 48992 MW; A15DF6571A05816C CRC64;
MSDTHLSTQK FADFPLHKEV HQALNEAGFE FCTPIQALSL PILLEKKDIA GQAQTGTGKT
LAFLVATFNH LLSTPIPAER QLNQPRAIIM APTRELAIQI AKDANLLAKH TGLKVGIVYG
GEGYEVQRKV LDKGVDILIG TTGRIIDYVR QGVINVSCIQ AVVLDEADRM FDLGFIKDIR
FLFRRMPDAK SRLNMLFSAT LSMKVQELAY DHMNEPEKVE IAPNEKTSKN IKEEIFYPSM
EEKMPLLLSL LEEDWPEKAI VFSNTKHSCE KVWSWLEGDG HRAGLLTGDV PQKKRLRILE
QFTKGEIDIL VATDVAARGL HIADVSHVYN YDLPDDCEDY VHRIGRTGRA GQKGISVSFA
CEEYALNLPA IESYIQHSIP VTSYDSDALL DDIPPPVRIH RKPSTHTRNT RDRGASRPQG
GQRSGPRRHD RTRRHS