DEAD_ECO57
ID DEAD_ECO57 Reviewed; 629 AA.
AC Q8XA87;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=ATP-dependent RNA helicase DeaD {ECO:0000255|HAMAP-Rule:MF_00964};
DE EC=3.6.4.13 {ECO:0000255|HAMAP-Rule:MF_00964};
DE AltName: Full=Cold-shock DEAD box protein A {ECO:0000255|HAMAP-Rule:MF_00964};
GN Name=deaD {ECO:0000255|HAMAP-Rule:MF_00964};
GN Synonyms=csdA {ECO:0000255|HAMAP-Rule:MF_00964};
GN OrderedLocusNames=Z4523, ECs4043;
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., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA 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., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: DEAD-box RNA helicase involved in various cellular processes
CC at low temperature, including ribosome biogenesis, mRNA degradation and
CC translation initiation. {ECO:0000255|HAMAP-Rule:MF_00964}.
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_00964};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00964}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DeaD/CsdA
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00964}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG58298.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB37466.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE005174; AAG58298.1; ALT_INIT; Genomic_DNA.
DR EMBL; BA000007; BAB37466.1; ALT_INIT; Genomic_DNA.
DR PIR; C91134; C91134.
DR PIR; F85979; F85979.
DR RefSeq; NP_312070.2; NC_002695.1.
DR RefSeq; WP_001301504.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; Q8XA87; -.
DR SMR; Q8XA87; -.
DR STRING; 155864.EDL933_4391; -.
DR EnsemblBacteria; AAG58298; AAG58298; Z4523.
DR EnsemblBacteria; BAB37466; BAB37466; ECs_4043.
DR GeneID; 916119; -.
DR KEGG; ece:Z4523; -.
DR KEGG; ecs:ECs_4043; -.
DR PATRIC; fig|386585.9.peg.4222; -.
DR eggNOG; COG0513; Bacteria.
DR HOGENOM; CLU_003041_21_1_6; -.
DR OMA; LPQGMPK; -.
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:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0070417; P:cellular response to cold; IEA:InterPro.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IEA:UniProtKB-UniRule.
DR GO; GO:0006401; P:RNA catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd12499; RRM_EcCsdA_like; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_00964; DEAD_helicase_DeaD; 1.
DR InterPro; IPR021046; Cold-shock_DEAD_Abox_C.
DR InterPro; IPR034415; CsdA_RRM.
DR InterPro; IPR005580; DbpA/CsdA_RNA-bd_dom.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR028618; DEAD_helicase_DeaD.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR Pfam; PF03880; DbpA; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF12343; DeaD_C; 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; Cytoplasm; Helicase; Hydrolase; Nucleotide-binding;
KW Reference proteome; RNA-binding; Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..629
FT /note="ATP-dependent RNA helicase DeaD"
FT /id="PRO_0000055102"
FT DOMAIN 37..208
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00964"
FT DOMAIN 232..379
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00964"
FT REGION 438..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 6..34
FT /note="Q motif"
FT MOTIF 156..159
FT /note="DEAD box"
FT COMPBIAS 446..481
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..629
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 50..57
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00964"
SQ SEQUENCE 629 AA; 70576 MW; 9DB689A2C74E117C CRC64;
MAEFETTFAD LGLKAPILEA LNDLGYEKPS PIQAECIPHL LNGRDVLGMA QTGSGKTAAF
SLPLLQNLDP ELKAPQILVL APTRELAVQV AEAMTDFSKH MRGVNVVALY GGQRYDVQLR
ALRQGPQIVV GTPGRLLDHL KRGTLDLSKL SGLVLDEADE MLRMGFIEDV ETIMAQIPEG
HQTALFSATM PEAIRRITRR FMKEPQEVRI QSSVTTRPDI SQSYWTVWGM RKNEALVRFL
EAEDFDAAII FVRTKNATLE VAEALERNGY NSAALNGDMN QALREQTLER LKDGRLDILI
ATDVAARGLD VERISLVVNY DIPMDSESYV HRIGRTGRAG RAGRALLFVE NRERRLLRNI
ERTMKLTIPE VELPNAELLG KRRLEKFAAK VQQQLESSDL DQYRALLSKI QPTAEGEELD
LETLAAALLK MAQGERTLIV PPDAPMRPKR EFRDRDDRGP RDRNDRGPRG DREDRPRRER
RDVGDMQLYR IEVGRDDGVE VRHIVGAIAN EGDISSRYIG NIKLFASHST IELPKGMPGE
VLQHFTRTRI LNKPMNMQLL GDAQPHTGGE RRGGGRGFSG ERREGGRNFS GERREGGRGD
GRRFSGERRE GRAPRRDDST GRRRFGGDA
