RHLE_ECOLI
ID RHLE_ECOLI Reviewed; 454 AA.
AC P25888;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 3.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=ATP-dependent RNA helicase RhlE {ECO:0000255|HAMAP-Rule:MF_00968};
DE EC=3.6.4.13 {ECO:0000255|HAMAP-Rule:MF_00968};
GN Name=rhlE {ECO:0000255|HAMAP-Rule:MF_00968};
GN OrderedLocusNames=b0797, JW0781;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8037924; DOI=10.1266/jjg.69.1;
RA Ohmori H.;
RT "Structural analysis of the rhlE gene of Escherichia coli.";
RL Jpn. J. Genet. 69:1-12(1994).
RN [2]
RP ERRATUM OF PUBMED:8037924, AND SEQUENCE REVISION TO C-TERMINUS.
RA Ohmori H.;
RL Jpn. J. Genet. 69:425-425(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 50-335.
RC STRAIN=K12;
RX PubMed=1931833;
RA Kalman M., Murphy H., Cashel M.;
RT "rhlB, a new Escherichia coli K-12 gene with an RNA helicase-like protein
RT sequence motif, one of at least five such possible genes in a prokaryote.";
RL New Biol. 3:886-895(1991).
RN [7]
RP INTERACTION WITH PCNB.
RX PubMed=10361280; DOI=10.1046/j.1365-2958.1999.01394.x;
RA Raynal L.C., Carpousis A.J.;
RT "Poly(A) polymerase I of Escherichia coli: characterization of the
RT catalytic domain, an RNA binding site and regions for the interaction with
RT proteins involved in mRNA degradation.";
RL Mol. Microbiol. 32:765-775(1999).
RN [8]
RP INDUCTION BY COLD SHOCK.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=14527658; DOI=10.1016/s0923-2508(03)00167-0;
RA Polissi A., De Laurentis W., Zangrossi S., Briani F., Longhi V., Pesole G.,
RA Deho G.;
RT "Changes in Escherichia coli transcriptome during acclimatization at low
RT temperature.";
RL Res. Microbiol. 154:573-580(2003).
RN [9]
RP FUNCTION AS RNA-HELICASE, FUNCTION AS ATPASE, CATALYTIC ACTIVITY, AND
RP ACTIVITY REGULATION.
RX PubMed=15196029; DOI=10.1021/bi049852s;
RA Bizebard T., Ferlenghi I., Iost I., Dreyfus M.;
RT "Studies on three E. coli DEAD-box helicases point to an unwinding
RT mechanism different from that of model DNA helicases.";
RL Biochemistry 43:7857-7866(2004).
RN [10]
RP INTERACTION WITH RNASE E.
RX PubMed=15554979; DOI=10.1111/j.1365-2958.2004.04361.x;
RA Khemici V., Toesca I., Poljak L., Vanzo N.F., Carpousis A.J.;
RT "The RNase E of Escherichia coli has at least two binding sites for DEAD-
RT box RNA helicases: functional replacement of RhlB by RhlE.";
RL Mol. Microbiol. 54:1422-1430(2004).
RN [11]
RP FUNCTION IN RIBOSOME ASSEMBLY, AND SUBCELLULAR LOCATION.
RX PubMed=18083833; DOI=10.1261/rna.800308;
RA Jain C.;
RT "The E. coli RhlE RNA helicase regulates the function of related RNA
RT helicases during ribosome assembly.";
RL RNA 14:381-389(2008).
RN [12]
RP INDUCTION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=27112147; DOI=10.1099/mic.0.000292;
RA Yamanaka Y., Shimada T., Yamamoto K., Ishihama A.;
RT "Transcription factor CecR (YbiH) regulates a set of genes affecting the
RT sensitivity of Escherichia coli against cefoperazone and chloramphenicol.";
RL Microbiology 162:1253-1264(2016).
CC -!- FUNCTION: DEAD-box RNA helicase involved in ribosome assembly. Has RNA-
CC dependent ATPase activity and unwinds double-stranded RNA. May play a
CC role in the interconversion of ribosomal RNA-folding intermediates that
CC are further processed by DeaD or SrmB during ribosome maturation.
CC {ECO:0000255|HAMAP-Rule:MF_00968, ECO:0000269|PubMed:15196029,
CC ECO:0000269|PubMed:18083833}.
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_00968,
CC ECO:0000269|PubMed:15196029};
CC -!- ACTIVITY REGULATION: ATPase activity is stimulated by both long RNAs
CC and short oligoribonucleotides. {ECO:0000269|PubMed:15196029}.
CC -!- SUBUNIT: Interacts with PcnB. Interacts in vitro with RNase E.
CC {ECO:0000269|PubMed:10361280, ECO:0000269|PubMed:15554979}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00968,
CC ECO:0000269|PubMed:18083833}. Note=Ribosome-associated. Can either bind
CC to the intact 70S ribosome or to individual ribosomal subunits.
CC -!- INDUCTION: Transiently induced by cold shock in a PNPase-dependent
CC fashion (PubMed:14527658). Induced by the transcriptional regulator
CC CecR (PubMed:27112147). {ECO:0000269|PubMed:14527658,
CC ECO:0000269|PubMed:27112147}.
CC -!- MISCELLANEOUS: In vitro, can replace RhlB in degradosome and facilitate
CC the degradation of RNA by PNPase. {ECO:0000305|PubMed:15554979}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. RhlE subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00968}.
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DR EMBL; L02123; AAA53653.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73884.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35457.1; -; Genomic_DNA.
DR EMBL; X56307; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; E64816; E64816.
DR RefSeq; NP_415318.1; NC_000913.3.
DR RefSeq; WP_000007101.1; NZ_SSZK01000002.1.
DR AlphaFoldDB; P25888; -.
DR SMR; P25888; -.
DR BioGRID; 4259962; 113.
DR BioGRID; 849799; 1.
DR DIP; DIP-10697N; -.
DR IntAct; P25888; 35.
DR STRING; 511145.b0797; -.
DR jPOST; P25888; -.
DR PaxDb; P25888; -.
DR PRIDE; P25888; -.
DR EnsemblBacteria; AAC73884; AAC73884; b0797.
DR EnsemblBacteria; BAA35457; BAA35457; BAA35457.
DR GeneID; 58463304; -.
DR GeneID; 945425; -.
DR KEGG; ecj:JW0781; -.
DR KEGG; eco:b0797; -.
DR PATRIC; fig|1411691.4.peg.1481; -.
DR EchoBASE; EB1217; -.
DR eggNOG; COG0513; Bacteria.
DR HOGENOM; CLU_003041_28_3_6; -.
DR InParanoid; P25888; -.
DR OMA; EHKDGQR; -.
DR PhylomeDB; P25888; -.
DR BioCyc; EcoCyc:EG11235-MON; -.
DR BioCyc; MetaCyc:EG11235-MON; -.
DR PRO; PR:P25888; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
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-KW.
DR GO; GO:0003724; F:RNA helicase activity; IDA:EcoCyc.
DR GO; GO:0009408; P:response to heat; IMP:EcoCyc.
DR GO; GO:0042255; P:ribosome assembly; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 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 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 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Helicase; Hydrolase; Nucleotide-binding;
KW Reference proteome; Ribosome biogenesis; RNA-binding.
FT CHAIN 1..454
FT /note="ATP-dependent RNA helicase RhlE"
FT /id="PRO_0000055108"
FT DOMAIN 32..208
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00968"
FT DOMAIN 219..381
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00968"
FT REGION 373..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1..29
FT /note="Q motif"
FT MOTIF 156..159
FT /note="DEAD box"
FT COMPBIAS 424..447
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 45..52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00968"
FT CONFLICT 55
FT /note="F -> G (in Ref. 6; X56307)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="L -> R (in Ref. 6; X56307)"
FT /evidence="ECO:0000305"
FT CONFLICT 210
FT /note="V -> A (in Ref. 6; X56307)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="K -> E (in Ref. 6; X56307)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="M -> L (in Ref. 6; X56307)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="A -> G (in Ref. 6; X56307)"
FT /evidence="ECO:0000305"
FT CONFLICT 286..287
FT /note="RA -> LS (in Ref. 6; X56307)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 454 AA; 49989 MW; 7576B35B7901671F CRC64;
MSFDSLGLSP DILRAVAEQG YREPTPIQQQ AIPAVLEGRD LMASAQTGTG KTAGFTLPLL
QHLITRQPHA KGRRPVRALI LTPTRELAAQ IGENVRDYSK YLNIRSLVVF GGVSINPQMM
KLRGGVDVLV ATPGRLLDLE HQNAVKLDQV EILVLDEADR MLDMGFIHDI RRVLTKLPAK
RQNLLFSATF SDDIKALAEK LLHNPLEIEV ARRNTASDQV TQHVHFVDKK RKRELLSHMI
GKGNWQQVLV FTRTKHGANH LAEQLNKDGI RSAAIHGNKS QGARTRALAD FKSGDIRVLV
ATDIAARGLD IEELPHVVNY ELPNVPEDYV HRIGRTGRAA ATGEALSLVC VDEHKLLRDI
EKLLKKEIPR IAIPGYEPDP SIKAEPIQNG RQQRGGGGRG QGGGRGQQQP RRGEGGAKSA
SAKPAEKPSR RLGDAKPAGE QQRRRRPRKP AAAQ
