ID J7SKX6_MORMO Unreviewed; 448 AA.
AC J7SKX6;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=ATP-dependent RNA helicase RhlE {ECO:0000256|HAMAP-Rule:MF_00968};
DE EC=3.6.4.13 {ECO:0000256|HAMAP-Rule:MF_00968};
GN Name=rhlE {ECO:0000256|HAMAP-Rule:MF_00968};
GN ORFNames=MU9_1441 {ECO:0000313|EMBL:AGG30487.1};
OS Morganella morganii subsp. morganii KT.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Morganella.
OX NCBI_TaxID=1124991 {ECO:0000313|EMBL:AGG30487.1, ECO:0000313|Proteomes:UP000011834};
RN [1] {ECO:0000313|EMBL:AGG30487.1, ECO:0000313|Proteomes:UP000011834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KT {ECO:0000313|EMBL:AGG30487.1,
RC ECO:0000313|Proteomes:UP000011834};
RX PubMed=23282187;
RA Chen Y.T., Peng H.L., Shia W.C., Hsu F.R., Ken C.F., Tsao Y.M., Chen C.H.,
RA Liu C.E., Hsieh M.F., Chen H.C., Tang C.Y., Ku T.H.;
RT "Whole-genome sequencing and identification of Morganella morganii KT
RT pathogenicity-related genes.";
RL BMC Genomics 13:S4-S4(2012).
CC -!- FUNCTION: DEAD-box RNA helicase involved in ribosome assembly. Has RNA-
CC dependent ATPase activity and unwinds double-stranded RNA.
CC {ECO:0000256|HAMAP-Rule:MF_00968}.
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_00968};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00968}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. RhlE subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00968}.
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DR EMBL; CP004345; AGG30487.1; -; Genomic_DNA.
DR RefSeq; WP_004235705.1; NC_020418.1.
DR AlphaFoldDB; J7SKX6; -.
DR GeneID; 69679599; -.
DR KEGG; mmk:MU9_1441; -.
DR eggNOG; COG0513; Bacteria.
DR HOGENOM; CLU_003041_28_3_6; -.
DR Proteomes; UP000011834; 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:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042255; P:ribosome assembly; IEA:InterPro.
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_00968; DEAD_helicase_RhlE; 1.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR028622; DEAD_helicase_RhlE.
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; IPR014014; RNA_helicase_DEAD_Q_motif.
DR PANTHER; PTHR47959:SF13; ATP-DEPENDENT RNA HELICASE RHLE; 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_00968}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00968};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_00968};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00968};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00968}; Reference proteome {ECO:0000313|Proteomes:UP000011834};
KW Ribosome biogenesis {ECO:0000256|HAMAP-Rule:MF_00968}.
FT DOMAIN 1..29
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 32..207
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 218..378
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 371..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1..29
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 434..448
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 448 AA; 48815 MW; 38D250919E8AF023 CRC64;
MSFSSLPLCP EIQKAVAEMG YEQPTPIQMQ AIPQVLAGHD LLASAQTGTG KTAGFTLPIL
QYLQDNPRKG GGRPVRALIL SPTRELAAQI GENVREYSRH LRTRSLVVFG GVSINPQMMK
LRGGVDILIA TPGRLLDLEH QNAVDLSKVE ILVLDEADRM LDMGFIHDIR RVIKKLPVKR
QNLLFSATFS NGIKSLANTI LNNPVTVEVS PRNSASQQVT QFVHLVDKKR KAELLAHLIG
RDNWEQVLIF TRTKHGANRL AEFLNDSGIK AAAIHGNKSQ GARTRALADF KSGAIRALVA
TDIAARGLDI EQLPYVVNYE LPNVAEDYVH RIGRTGRAEA TGLALSLVCV DEHDLLRDIE
KLLKKQIERM AEPGYDPDPS IKAEPIQKAK QGRGGNGRSG GGRQGGQGRS AEGRGNSGGG
DKRPPRPRQH KPRSGNSDSG SPWGNRGK
//
