RHLB_SHIDS
ID RHLB_SHIDS Reviewed; 421 AA.
AC Q329V8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=SDY_3969;
OS Shigella dysenteriae serotype 1 (strain Sd197).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300267;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sd197;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
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; CP000034; ABB63897.1; -; Genomic_DNA.
DR RefSeq; WP_000047532.1; NC_007606.1.
DR RefSeq; YP_405388.1; NC_007606.1.
DR AlphaFoldDB; Q329V8; -.
DR SMR; Q329V8; -.
DR STRING; 300267.SDY_3969; -.
DR EnsemblBacteria; ABB63897; ABB63897; SDY_3969.
DR KEGG; sdy:SDY_3969; -.
DR PATRIC; fig|300267.13.peg.4680; -.
DR HOGENOM; CLU_003041_1_3_6; -.
DR OMA; EYCTPIQ; -.
DR Proteomes; UP000002716; 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 Reference proteome; RNA-binding.
FT CHAIN 1..421
FT /note="ATP-dependent RNA helicase RhlB"
FT /id="PRO_1000082872"
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 392..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; 47172 MW; 3998FD8A4F90A863 CRC64;
MSKTHLTEQK FSDFSLHPKV VEALEKKGFH NCTPIQALAL PLTLAGRDVA GQAQTGTGKT
MAFLTSMFHY LLSHPAIADR KVNKPRALIM APTRELAVQI HADAEPLAEA TGLKLGLAYG
GDGYDKQLKV LESGVDILIG TTGRLIDYAK QNHINLGAIQ VVVLDEADRM YDLGFIKDIR
WLFRRMPPAN QRLNMLFSAT LSYRVRELAF EQMNNAEYIE VEPEQKTGHR IKEELFYPSN
EEKMRLLQTL IEEEWPDRAI IFANTKHRCE EIWGHLAADG HRVGLLTGDV AQKKRLRILD
EFTRGDLDIL VATDVAARGL HIPAVTHVFN YDLPDDCEDY VHRIGRTGRA GASGHSISLA
CEEYALNLPA IETYIGHSIP VSKYNPDALM TDLPKPLRLT RPRTGNGPRR TGAPRNRRRS
G
