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RHLB_PSEAE
ID   RHLB_PSEAE              Reviewed;         397 AA.
AC   Q9HXE5;
DT   27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 118.
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}; Synonyms=rhl;
GN   OrderedLocusNames=PA3861;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
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; AE004091; AAG07248.1; -; Genomic_DNA.
DR   PIR; C83163; C83163.
DR   RefSeq; NP_252550.3; NC_002516.2.
DR   RefSeq; WP_003119269.1; NC_002516.2.
DR   AlphaFoldDB; Q9HXE5; -.
DR   SMR; Q9HXE5; -.
DR   STRING; 287.DR97_4005; -.
DR   PaxDb; Q9HXE5; -.
DR   PRIDE; Q9HXE5; -.
DR   EnsemblBacteria; AAG07248; AAG07248; PA3861.
DR   GeneID; 879804; -.
DR   KEGG; pae:PA3861; -.
DR   PATRIC; fig|208964.12.peg.4043; -.
DR   PseudoCAP; PA3861; -.
DR   HOGENOM; CLU_003041_1_3_6; -.
DR   InParanoid; Q9HXE5; -.
DR   OMA; EYCTPIQ; -.
DR   PhylomeDB; Q9HXE5; -.
DR   BioCyc; PAER208964:G1FZ6-3932-MON; -.
DR   Proteomes; UP000002438; 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..397
FT                   /note="ATP-dependent RNA helicase RhlB"
FT                   /id="PRO_0000200779"
FT   DOMAIN          40..220
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00661"
FT   DOMAIN          243..393
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00661"
FT   MOTIF           9..37
FT                   /note="Q motif"
FT   MOTIF           166..169
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   397 AA;  44288 MW;  BDA5CB91D709B6AD CRC64;
     MVEPQEGKTR FHDFNLAPSL MHAIHDLGFP YCTPIQAQVL GFTLRGQDAI GRAQTGTGKT
     AAFLISIITQ LLQTPPPKER YMGEPRALII APTRELVVQI AKDAAALTKY TGLNVMTFVG
     GMDFDKQLKQ LEARFCDILV ATPGRLLDFN QRGEVHLDMV EVMVLDEADR MLDMGFIPQV
     RQIIRQTPHK GERQTLLFSA TFTDDVMNLA KQWTVDPAIV EIEPENVASD TVEQHVYAVA
     GSDKYKLLYN LVAQNNWERV MVFANRKDEV RRIEERLTKD GISAAQMSGD VPQHKRIRTL
     EGFREGKIRV LVATDVAGRG IHIDGISHVI NFTLPEDPDD YVHRIGRTGR AGASGTSISF
     AGEDDAFALP PIEELLGRKI TCEMPPAELL KPVPRKH
 
 
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