ID RHLB_ALIF1 Reviewed; 432 AA.
AC Q5E8U5;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 27-MAR-2024, entry version 105.
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=VF_0056;
GN ORFNames=VF0055;
OS Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=312309;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700601 / ES114;
RX PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT pathogenic congeners.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=18366731; DOI=10.1186/1471-2164-9-138;
RA Mandel M.J., Stabb E.V., Ruby E.G.;
RT "Comparative genomics-based investigation of resequencing targets in Vibrio
RT fischeri: focus on point miscalls and artefactual expansions.";
RL BMC Genomics 9:138-138(2008).
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; CP000020; AAW84551.2; -; Genomic_DNA.
DR RefSeq; WP_005416870.1; NC_006840.2.
DR RefSeq; YP_203439.2; NC_006840.2.
DR AlphaFoldDB; Q5E8U5; -.
DR SMR; Q5E8U5; -.
DR STRING; 312309.VF_0056; -.
DR EnsemblBacteria; AAW84551; AAW84551; VF_0056.
DR KEGG; vfi:VF_0056; -.
DR PATRIC; fig|312309.11.peg.56; -.
DR eggNOG; COG0513; Bacteria.
DR HOGENOM; CLU_003041_28_3_6; -.
DR OrthoDB; 9805696at2; -.
DR Proteomes; UP000000537; Chromosome I.
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 CDD; cd00268; DEADc; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 PANTHER; PTHR47959:SF10; ATP-DEPENDENT RNA HELICASE RHLB; 1.
DR PANTHER; PTHR47959; ATP-DEPENDENT RNA HELICASE RHLE-RELATED; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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..432
FT /note="ATP-dependent RNA helicase RhlB"
FT /id="PRO_1000131311"
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..432
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 402..417
FT /note="Polar 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 432 AA; 48634 MW; A75FB0178D8FD752 CRC64;
MKKTHITEQN FADLGLQPQV IDGLNAKGFI KCTPIQAKAL PVLLAGQDIA GQAQTGTGKT
LAFLTATFNH LLTTPAPEGR KITQPRAIIM APTRELAIQI FNDAESLIAS TGLKAALAYG
GERYEKQQQV IEQGVDILIG TTGRIIDFYK QGHIDFKMIQ AVVLDEADRM FDLGFIKDIR
FIFRRMPAPT ERLNMLFSAT LSYRVQELAF EHMQEPEHVV VEPEQKTGHR IKEELFYPSN
DHKMALLQTL IEEEWPDRAI IFANTKHKCE SVWGHLAADK HRVGLLTGDV PQKKRERILE
EFTQGNVDIL VATDVAARGL HIPQVTHVFN FDLPNEAEDY VHRIGRTGRA GASGNSISFA
CEEYAINLPA IEEYIEHSIP QSDYDASALL EDLPAPLRLQ RRPQQNRRNN NGQRQGGNRK
HTRPRQPRNT QS
//
