ID   RHLB_HAEIN              Reviewed;         415 AA.
AC   P44922;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2003, sequence version 2.
DT   03-AUG-2022, entry version 139.
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=HI_0892;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
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=AAC22552.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; L42023; AAC22552.1; ALT_INIT; Genomic_DNA.
DR   PIR; E64100; E64100.
DR   RefSeq; NP_439053.1; NC_000907.1.
DR   RefSeq; WP_032828332.1; NC_000907.1.
DR   AlphaFoldDB; P44922; -.
DR   SMR; P44922; -.
DR   STRING; 71421.HI_0892; -.
DR   EnsemblBacteria; AAC22552; AAC22552; HI_0892.
DR   KEGG; hin:HI_0892; -.
DR   PATRIC; fig|71421.8.peg.934; -.
DR   eggNOG; COG0513; Bacteria.
DR   HOGENOM; CLU_003041_1_3_6; -.
DR   PhylomeDB; P44922; -.
DR   Proteomes; UP000000579; 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   CHAIN           1..415
FT                   /note="ATP-dependent RNA helicase RhlB"
FT                   /id="PRO_0000200773"
FT   DOMAIN          40..218
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00661"
FT   DOMAIN          241..389
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00661"
FT   MOTIF           9..37
FT                   /note="Q motif"
FT   MOTIF           164..167
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   415 AA;  46659 MW;  E543BF942BA6530C CRC64;
     MQQDYLSQQR FSALPLHPIV RGALAKKGFD FCTPIQALSL PISLNGRDVA GQAQTGTGKT
     MAFLTATFHH LLTHQDPNLK YPHPRALILA PTRELAVQIS NDAEFLAKAS GLKTALAYGG
     DGYDKQLQAI ERGVDILIGT TGRVIDYVKQ GVIGLDEIQV VVLDEADRMF DLGFIRDIRY
     LLRKCPAPQA RLTMLFSATL SYKVRELAFE DMNEPEYIEI EPEQKTGHRI KEELFYPSNQ
     DKMALLLTLM EDEWPERCIV FANTKHRCEE IWGYLAADGH RVGLLTGDVA QKKRLSLLKQ
     FTDGDLDILV ATDVAARGLH ISDVTHVFNY DLPDDREDYV HRIGRTGRAG ESGVSISFAC
     EEYAMNLPAI EEYIGHSIPV SQYETEALLE LPKPYRLKRA VPPQGHTRHR SYHAK