RHLB_SALTY
ID RHLB_SALTY Reviewed; 421 AA.
AC P0A2P0; P40863; Q9L6R8;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 108.
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=STM3914;
GN ORFNames=STMD1.76;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-57.
RC STRAIN=LT2;
RX PubMed=1561103; DOI=10.1093/nar/20.6.1424;
RA Kotani H., Nakajima K.;
RT "Cloning and sequence of thioredoxin gene of Salmonella typhimurium LT2.";
RL Nucleic Acids Res. 20:1424-1424(1992).
RN [3]
RP IDENTIFICATION.
RX PubMed=7920643; DOI=10.1038/ng0694-205;
RA Robison K., Gilbert W., Church G.M.;
RT "Large scale bacterial gene discovery by similarity search.";
RL Nat. Genet. 7:205-214(1994).
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 -!- SEQUENCE CAUTION:
CC Sequence=AAF33472.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=D10015; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF233324; AAF33472.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AE006468; AAL22764.1; -; Genomic_DNA.
DR EMBL; D10015; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_462805.1; NC_003197.2.
DR RefSeq; WP_000047525.1; NC_003197.2.
DR AlphaFoldDB; P0A2P0; -.
DR SMR; P0A2P0; -.
DR STRING; 99287.STM3914; -.
DR PaxDb; P0A2P0; -.
DR EnsemblBacteria; AAL22764; AAL22764; STM3914.
DR GeneID; 1255440; -.
DR KEGG; stm:STM3914; -.
DR PATRIC; fig|99287.12.peg.4136; -.
DR HOGENOM; CLU_003041_1_3_6; -.
DR OMA; EYCTPIQ; -.
DR PhylomeDB; P0A2P0; -.
DR BioCyc; SENT99287:STM3914-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..421
FT /note="ATP-dependent RNA helicase RhlB"
FT /id="PRO_0000200783"
FT DOMAIN 40..219
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00661"
FT DOMAIN 245..390
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00661"
FT REGION 396..421
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 421 AA; 47093 MW; 8A48375C667EBD67 CRC64;
MSKTHLTEQK FSDFALHPQV VEALEKKGFY NCTPIQALAL PLTLAGRDVA GQAQTGTGKT
MAFLTSTFHY LLSHPAIDDR KVNQPRALIM APTRELAVQI HADAEPLAQA TGLKLGLAYG
GDGYDKQLKV LESGVDILIG TTGRLIDYAK QNHINLGAIQ VVVLDEADRM YDLGFIKDIR
WLFRRMPPAA QRLNMLFSAT LSYRVRELAF EQMNNAEYVE VEPEQKTGHR IKEELFYPSN
EEKMRLLQTL IEEEWPDRAI IFANTKHRCE DIWGHLAADG HRVGLLTGDV AQKKRLRILD
EFTRGDLDIL VATDVAARGL HIPAVTHVFN YDLPDDCEDY VHRIGRTGRA GASGHSISLA
CEEYALNLPA IESYIGHSIP VSKYNPEALM NDLPKPLRLT RSRPGNGPRR AGAPRNRRRS
G
