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Database: UniProt
Entry: B4EBW3_BURCJ
LinkDB: B4EBW3_BURCJ
Original site: B4EBW3_BURCJ 
ID   B4EBW3_BURCJ            Unreviewed;       477 AA.
AC   B4EBW3;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 90.
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=rhlE1 {ECO:0000313|EMBL:CAR51239.1};
GN   Synonyms=rhlE {ECO:0000256|HAMAP-Rule:MF_00968};
GN   ORFNames=BCAL0933 {ECO:0000313|EMBL:CAR51239.1};
OS   Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 /
OS   NCTC 13227 / J2315 / CF5610) (Burkholderia cepacia (strain J2315)).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=216591 {ECO:0000313|EMBL:CAR51239.1, ECO:0000313|Proteomes:UP000001035};
RN   [1] {ECO:0000313|EMBL:CAR51239.1, ECO:0000313|Proteomes:UP000001035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 /
RC   CF5610 {ECO:0000313|Proteomes:UP000001035};
RX   PubMed=18931103; DOI=10.1128/JB.01230-08;
RA   Holden M.T., Seth-Smith H.M., Crossman L.C., Sebaihia M., Bentley S.D.,
RA   Cerdeno-Tarraga A.M., Thomson N.R., Bason N., Quail M.A., Sharp S.,
RA   Cherevach I., Churcher C., Goodhead I., Hauser H., Holroyd N., Mungall K.,
RA   Scott P., Walker D., White B., Rose H., Iversen P., Mil-Homens D.,
RA   Rocha E.P., Fialho A.M., Baldwin A., Dowson C., Barrell B.G., Govan J.R.,
RA   Vandamme P., Hart C.A., Mahenthiralingam E., Parkhill J.;
RT   "The genome of Burkholderia cenocepacia J2315, an epidemic pathogen of
RT   cystic fibrosis patients.";
RL   J. Bacteriol. 191:261-277(2009).
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; AM747720; CAR51239.1; -; Genomic_DNA.
DR   RefSeq; WP_006497357.1; NC_011000.1.
DR   AlphaFoldDB; B4EBW3; -.
DR   KEGG; bcj:BCAL0933; -.
DR   eggNOG; COG0513; Bacteria.
DR   HOGENOM; CLU_003041_28_3_4; -.
DR   BioCyc; BCEN216591:G1G1V-1030-MONOMER; -.
DR   Proteomes; UP000001035; Chromosome 1.
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; 2.
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}; 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..209
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          232..381
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          375..477
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"
SQ   SEQUENCE   477 AA;  51387 MW;  899825A780DF4300 CRC64;
     MSFESLGLAE PLVKAVNELG YTSPTPIQQQ AIPAVLGGGD LLAGAQTGTG KTAGFTLPIL
     QRLHTFYAEH RGAKRAVRAL ILTPTRELAA QVEESVRAYS KYLKLRSTVM FGGVSINPQI
     DALKRGVDIV VATPGRLLDH MQQKTIDLSD LDILVLDEAD RMLDMGFIHD IKRVLAKLPP
     QRQNLLFSAT FSDEIKALAD SLLDSPALIE VARRNTTAES VAQKIHPVDR DRKRELLTHL
     IREHNWFQVL VFTRTKHGAN RLAEQLTKDG ISAMAIHGNK SQSARTRALA EFKNSTLQVL
     VATDIAARGI DIDQLPHVVN FDLPNVPEDY VHRIGRTGRA GATGEAVSLV CVDEKQLLRD
     IERLIKREIP QEVIAGFEPD PNAKPEPIQQ RRGQQQPRGG GGGGNRQPRA GGSGQPAAKR
     DGHAQPKAAK PRTQGGAGAG GNGGGRPAGG GNGARPANGN AAHANRNRSS RSGQRGH
//
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