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Database: UniProt
Entry: Q8XAT4
LinkDB: Q8XAT4
Original site: Q8XAT4 
ID   RHLB_ECO57              Reviewed;         421 AA.
AC   Q8XAT4;
DT   27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-OCT-2019, entry version 110.
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};
GN   OrderedLocusNames=Z5290, ECs4713;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: DEAD-box RNA helicase involved in RNA degradation. Has
CC       RNA-dependent ATPase activity and unwinds double-stranded RNA.
CC       {ECO:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_00661}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00661}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. RhlB
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00661}.
DR   EMBL; AE005174; AAG58974.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB38136.1; -; Genomic_DNA.
DR   PIR; A91218; A91218.
DR   PIR; B86064; B86064.
DR   RefSeq; NP_312740.1; NC_002695.1.
DR   RefSeq; WP_000047490.1; NZ_SDVX01000004.1.
DR   SMR; Q8XAT4; -.
DR   STRING; 155864.EDL933_5100; -.
DR   EnsemblBacteria; AAG58974; AAG58974; Z5290.
DR   EnsemblBacteria; BAB38136; BAB38136; BAB38136.
DR   GeneID; 915257; -.
DR   KEGG; ece:Z5290; -.
DR   KEGG; ecs:ECs4713; -.
DR   PATRIC; fig|386585.9.peg.4917; -.
DR   eggNOG; ENOG4105C1J; Bacteria.
DR   eggNOG; COG0513; LUCA.
DR   HOGENOM; HOG000268807; -.
DR   KO; K03732; -.
DR   BioCyc; ECOO157:RHLB-MONOMER; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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   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   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Cytoplasm; Helicase; Hydrolase;
KW   Nucleotide-binding; Reference proteome; RNA-binding.
FT   INIT_MET      1      1       Removed. {ECO:0000250}.
FT   CHAIN         2    421       ATP-dependent RNA helicase RhlB.
FT                                /FTId=PRO_0000200770.
FT   DOMAIN       40    219       Helicase ATP-binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00661}.
FT   DOMAIN      245    390       Helicase C-terminal. {ECO:0000255|HAMAP-
FT                                Rule:MF_00661}.
FT   NP_BIND      53     60       ATP. {ECO:0000255|HAMAP-Rule:MF_00661}.
FT   MOTIF         9     37       Q motif.
FT   MOTIF       165    168       DEAD box.
SQ   SEQUENCE   421 AA;  47093 MW;  25B76A29271D75D5 CRC64;
     MSKTHLTEQK FSDFALHPKV VEALEKKGFH NCTPIQALAL PLTLAGRDVA GQAQTGTGKT
     MAFLTSTFHC 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 GANGHSISLA
     CEEYALNLPA IETYIGHSIP VSKYNPDALM TDLPKPLRLT RPRTGNGPRR TGAPRNRRRS
     G
//
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