RHLB_ECOLI
ID RHLB_ECOLI Reviewed; 421 AA.
AC P0A8J8; P24229; Q2M888;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 137.
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=mmrA;
GN OrderedLocusNames=b3780, JW3753;
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;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=1379743; DOI=10.1126/science.1379743;
RA Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.;
RT "Analysis of the Escherichia coli genome: DNA sequence of the region from
RT 84.5 to 86.5 minutes.";
RL Science 257:771-778(1992).
RN [3]
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 [4]
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 [5]
RP PROTEIN SEQUENCE OF 2-16, FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=8610017; DOI=10.1038/381169a0;
RA Py B., Higgins C.F., Krisch H.M., Carpousis A.J.;
RT "A DEAD-box RNA helicase in the Escherichia coli RNA degradosome.";
RL Nature 381:169-172(1996).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, INTERACTION WITH RNASE
RP E, AND SUBUNIT.
RX PubMed=9732274; DOI=10.1101/gad.12.17.2770;
RA Vanzo N.F., Li Y.S., Py B., Blum E., Higgins C.F., Raynal L.C.,
RA Krisch H.M., Carpousis A.J.;
RT "Ribonuclease E organizes the protein interactions in the Escherichia coli
RT RNA degradosome.";
RL Genes Dev. 12:2770-2781(1998).
RN [7]
RP INTERACTION WITH RNASE E, AND SUBUNIT.
RX PubMed=10521403; DOI=10.1101/gad.13.19.2594;
RA Coburn G.A., Miao X., Briant D.J., Mackie G.A.;
RT "Reconstitution of a minimal RNA degradosome demonstrates functional
RT coordination between a 3' exonuclease and a DEAD-box RNA helicase.";
RL Genes Dev. 13:2594-2603(1999).
RN [8]
RP FUNCTION, AND INTERACTION WITH PNPASE AND RNASE E.
RX PubMed=12181321; DOI=10.1074/jbc.m206618200;
RA Liou G.-G., Chang H.-Y., Lin C.-S., Lin-Chao S.;
RT "DEAD box RhlB RNA helicase physically associates with exoribonuclease
RT PNPase to degrade double-stranded RNA independent of the degradosome-
RT assembling region of RNase E.";
RL J. Biol. Chem. 277:41157-41162(2002).
RN [9]
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=18337249; DOI=10.1074/jbc.m709118200;
RA Taghbalout A., Rothfield L.;
RT "RNaseE and RNA helicase B play central roles in the cytoskeletal
RT organization of the RNA degradosome.";
RL J. Biol. Chem. 283:13850-13855(2008).
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, ECO:0000269|PubMed:12181321,
CC ECO:0000269|PubMed:8610017, ECO:0000269|PubMed:9732274}.
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 ECO:0000269|PubMed:8610017, ECO:0000269|PubMed:9732274};
CC -!- ACTIVITY REGULATION: ATPase activity is stimulated by interaction with
CC RNase E. {ECO:0000269|PubMed:9732274}.
CC -!- SUBUNIT: Component of the RNA degradosome, which is a multiprotein
CC complex involved in RNA processing and mRNA degradation. Binds to RNase
CC E (rne) and PNPase (pnp). Forms multimers. {ECO:0000255|HAMAP-
CC Rule:MF_00661, ECO:0000269|PubMed:10521403,
CC ECO:0000269|PubMed:18337249, ECO:0000269|PubMed:8610017,
CC ECO:0000269|PubMed:9732274}.
CC -!- INTERACTION:
CC P0A8J8; P05055: pnp; NbExp=8; IntAct=EBI-555806, EBI-548080;
CC P0A8J8; P21513: rne; NbExp=18; IntAct=EBI-555806, EBI-549958;
CC P0A8J8; Q1ZS71: rne; Xeno; NbExp=4; IntAct=EBI-555806, EBI-8525650;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00661,
CC ECO:0000269|PubMed:18337249}. Note=Forms a cytoskeletal-like coiled
CC structure that extends along the length of the cell. Formation of this
CC structure does not require the presence of RNase E, MinD and/or MreB.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. RhlB subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00661}.
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DR EMBL; X56310; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M87049; AAA67581.1; -; Genomic_DNA.
DR EMBL; M83316; AAB59048.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76785.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77518.1; -; Genomic_DNA.
DR PIR; G65181; G65181.
DR RefSeq; NP_418227.1; NC_000913.3.
DR RefSeq; WP_000047499.1; NZ_SSZK01000025.1.
DR AlphaFoldDB; P0A8J8; -.
DR SMR; P0A8J8; -.
DR BioGRID; 4263320; 99.
DR BioGRID; 852589; 1.
DR ComplexPortal; CPX-403; RNA degradosome.
DR DIP; DIP-35644N; -.
DR IntAct; P0A8J8; 33.
DR MINT; P0A8J8; -.
DR STRING; 511145.b3780; -.
DR jPOST; P0A8J8; -.
DR PaxDb; P0A8J8; -.
DR PRIDE; P0A8J8; -.
DR EnsemblBacteria; AAC76785; AAC76785; b3780.
DR EnsemblBacteria; BAE77518; BAE77518; BAE77518.
DR GeneID; 66672317; -.
DR GeneID; 948290; -.
DR KEGG; ecj:JW3753; -.
DR KEGG; eco:b3780; -.
DR PATRIC; fig|511145.12.peg.3895; -.
DR EchoBASE; EB0837; -.
DR eggNOG; COG0513; Bacteria.
DR HOGENOM; CLU_003041_1_3_6; -.
DR InParanoid; P0A8J8; -.
DR OMA; EYCTPIQ; -.
DR PhylomeDB; P0A8J8; -.
DR BioCyc; EcoCyc:EG10844-MON; -.
DR BioCyc; MetaCyc:EG10844-MON; -.
DR PRO; PR:P0A8J8; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:1990061; C:bacterial degradosome; IPI:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003724; F:RNA helicase activity; IDA:CAFA.
DR GO; GO:0006401; P:RNA catabolic process; IMP:EcoCyc.
DR GO; GO:0006396; P:RNA processing; IC:ComplexPortal.
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 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Direct protein sequencing; Helicase; Hydrolase;
KW Nucleotide-binding; Reference proteome; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8610017"
FT CHAIN 2..421
FT /note="ATP-dependent RNA helicase RhlB"
FT /id="PRO_0000200769"
FT DOMAIN 40..219
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00661"
FT DOMAIN 245..390
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00661"
FT REGION 392..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 9..37
FT /note="Q motif"
FT MOTIF 165..168
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"
FT CONFLICT 72
FT /note="L -> H (in Ref. 1; X56310)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="Y -> S (in Ref. 1; X56310)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 421 AA; 47126 MW; 48E1ADD025CBFA1A CRC64;
MSKTHLTEQK FSDFALHPKV VEALEKKGFH NCTPIQALAL PLTLAGRDVA GQAQTGTGKT
MAFLTSTFHY LLSHPAIADR KVNQPRALIM APTRELAVQI HADAEPLAEA TGLKLGLAYG
GDGYDKQLKV LESGVDILIG TTGRLIDYAK QNHINLGAIQ VVVLDEADRM YDLGFIKDIR
WLFRRMPPAN QRLNMLFSAT LSYRVRELAF EQMNNAEYIE VEPEQKTGHR IKEELFYPSN
EEKMRLLQTL IEEEWPDRAI IFANTKHRCE EIWGHLAADG HRVGLLTGDV AQKKRLRILD
EFTRGDLDIL VATDVAARGL HIPAVTHVFN YDLPDDCEDY VHRIGRTGRA GASGHSISLA
CEEYALNLPA IETYIGHSIP VSKYNPDALM TDLPKPLRLT RPRTGNGPRR TGAPRNRRRS
G
