ID B1J179_PSEPW Unreviewed; 483 AA.
AC B1J179;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE RecName: Full=ATP-dependent RNA helicase RhlB {ECO:0000256|HAMAP-Rule:MF_00661};
DE EC=3.6.4.13 {ECO:0000256|HAMAP-Rule:MF_00661};
DE Flags: Precursor;
GN Name=rhlB {ECO:0000256|HAMAP-Rule:MF_00661};
GN OrderedLocusNames=PputW619_0902 {ECO:0000313|EMBL:ACA71407.1};
OS Pseudomonas putida (strain W619).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=390235 {ECO:0000313|EMBL:ACA71407.1};
RN [1] {ECO:0000313|EMBL:ACA71407.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=W619 {ECO:0000313|EMBL:ACA71407.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S.,
RA Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Taghavi S., Vangronsveld D., van der Lelie D.,
RA Richardson P.;
RT "Complete sequence of Psuedomonas putida W619.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: DEAD-box RNA helicase involved in RNA degradation. Has RNA-
CC dependent ATPase activity and unwinds double-stranded RNA.
CC {ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00661}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00661}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. RhlB subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00661}.
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DR EMBL; CP000949; ACA71407.1; -; Genomic_DNA.
DR AlphaFoldDB; B1J179; -.
DR STRING; 390235.PputW619_0902; -.
DR KEGG; ppw:PputW619_0902; -.
DR eggNOG; COG0513; Bacteria.
DR HOGENOM; CLU_003041_1_3_6; -.
DR OrthoDB; 9805696at2; -.
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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00661}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00661};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_00661};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00661};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00661}; RNA-binding {ECO:0000256|HAMAP-Rule:MF_00661}.
FT DOMAIN 94..122
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 125..305
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 328..478
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 94..122
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 32..46
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 483 AA; 53508 MW; A8EAE27B1423C7B0 CRC64;
MLKALKKIFG KGDAAPQAAA PAASITPAAA PVAQPEPQPS TPRTKPAAKA PMPGAVPVAE
QPAKDKPRRE RKPKPQASLW KPEDFVVEPQ EGKTRFHDFK LSNELMHAIH DLGFPYCTPI
QAQVLGYTLR GKDAIGRAQT GTGKTAAFLI SIISQLQQTP PPKERYMGEP RALIIAPTRE
LVVQIAKDAA ALTKYTGLNV MTFVGGMDFD KQLKTLEARH CDILVATPGR LLDFNQRGDV
HLDMVEVMVL DEADRMLDMG FIPQVRQIIR QTPPKSERQT LLFSATFTDD VMNLAKQWTT
DPAIVEIEPE NVASETVEQH VFAVAGSDKY KLLYNLVTQN KWERVMVFAN RKDEVRRIEE
KLVRDGINAA QLSGDVPQHK RIRTLESFRE GRITVLVATD VAGRGIHIDG ISHVINFTLP
EDPDDYVHRI GRTGRAGTSG VSISFAGEDD SYQLPAIEEL LGRKIKCEMP PDELLTPVPR
KHH
//
