位置:首页 > 蛋白库 > DBPA_BACCR
DBPA_BACCR
ID   DBPA_BACCR              Reviewed;         481 AA.
AC   Q814I2;
DT   03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=ATP-dependent RNA helicase DbpA {ECO:0000255|HAMAP-Rule:MF_00965};
DE            EC=3.6.4.13 {ECO:0000255|HAMAP-Rule:MF_00965};
GN   Name=dbpA {ECO:0000255|HAMAP-Rule:MF_00965}; Synonyms=cshD;
GN   OrderedLocusNames=BC_5451;
OS   Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS   15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC   / NCTC 2599 / NRRL B-3711;
RX   PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA   Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA   Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA   Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT   anthracis.";
RL   Nature 423:87-91(2003).
RN   [2]
RP   INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC   / NCTC 2599 / NRRL B-3711;
RX   PubMed=20709848; DOI=10.1128/aem.00782-10;
RA   Pandiani F., Brillard J., Bornard I., Michaud C., Chamot S., Nguyen-the C.,
RA   Broussolle V.;
RT   "Differential involvement of the five RNA helicases in adaptation of
RT   Bacillus cereus ATCC 14579 to low growth temperatures.";
RL   Appl. Environ. Microbiol. 76:6692-6697(2010).
RN   [3]
RP   INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC   / NCTC 2599 / NRRL B-3711;
RX   PubMed=21705526; DOI=10.1128/aem.02974-10;
RA   Pandiani F., Chamot S., Brillard J., Carlin F., Nguyen-the C.,
RA   Broussolle V.;
RT   "Role of the five RNA helicases in the adaptive response of Bacillus cereus
RT   ATCC 14579 cells to temperature, pH, and oxidative stresses.";
RL   Appl. Environ. Microbiol. 77:5604-5609(2011).
CC   -!- FUNCTION: DEAD-box RNA helicase involved in the assembly of the 50S
CC       ribosomal subunit. Has an RNA-dependent ATPase activity, which is
CC       specific for 23S rRNA, and a 3' to 5' RNA helicase activity that uses
CC       the energy of ATP hydrolysis to destabilize and unwind short rRNA
CC       duplexes. {ECO:0000255|HAMAP-Rule:MF_00965}.
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_00965};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00965}.
CC   -!- INDUCTION: Induced at 10 degrees Celsius. {ECO:0000269|PubMed:20709848,
CC       ECO:0000269|PubMed:21705526}.
CC   -!- DOMAIN: Contains an N-terminal domain that binds non-specifically to
CC       RNA and a C-terminal domain that binds specifically and tightly to
CC       hairpin 92 of 23S rRNA. {ECO:0000255|HAMAP-Rule:MF_00965}.
CC   -!- DISRUPTION PHENOTYPE: Wild-type growth rate at 10 and 30 degrees
CC       Celsius, no change upon exposure to H(2)O(2) or diamide.
CC       {ECO:0000269|PubMed:20709848, ECO:0000269|PubMed:21705526}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DbpA subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00965}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE016877; AAP12312.1; -; Genomic_DNA.
DR   RefSeq; NP_835111.1; NC_004722.1.
DR   RefSeq; WP_000039351.1; NZ_CP034551.1.
DR   AlphaFoldDB; Q814I2; -.
DR   SMR; Q814I2; -.
DR   STRING; 226900.BC_5451; -.
DR   EnsemblBacteria; AAP12312; AAP12312; BC_5451.
DR   KEGG; bce:BC5451; -.
DR   PATRIC; fig|226900.8.peg.5632; -.
DR   HOGENOM; CLU_003041_21_1_9; -.
DR   OMA; YDIELYQ; -.
DR   Proteomes; UP000001417; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0034458; F:3'-5' RNA helicase activity; IEA:UniProtKB-UniRule.
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; IBA:GO_Central.
DR   GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR   GO; GO:0033592; F:RNA strand annealing activity; IBA:GO_Central.
DR   GO; GO:0000027; P:ribosomal large subunit assembly; IBA:GO_Central.
DR   Gene3D; 3.30.70.330; -; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   HAMAP; MF_00965; DEAD_helicase_DbpA; 1.
DR   InterPro; IPR005580; DbpA/CsdA_RNA-bd_dom.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR028619; DEAD_helicase_DbpA.
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; 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   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Helicase; Hydrolase; Nucleotide-binding;
KW   Reference proteome; Ribosome biogenesis; RNA-binding.
FT   CHAIN           1..481
FT                   /note="ATP-dependent RNA helicase DbpA"
FT                   /id="PRO_0000430107"
FT   DOMAIN          35..205
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00965"
FT   DOMAIN          231..377
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00965"
FT   REGION          406..481
FT                   /note="Involved in 23S rRNA binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00965"
FT   MOTIF           4..32
FT                   /note="Q motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00965"
FT   MOTIF           153..156
FT                   /note="DEAD box"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00965"
FT   BINDING         48..55
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00965"
SQ   SEQUENCE   481 AA;  54174 MW;  BCAFAD3CE35CE7B9 CRC64;
     MSKKSFSDYK LSKEIVRALT GLGYDHPTEV QGEVIPVALQ KKDLVVKSQT GSGKTASFGI
     PLCEMVEWEE NKPQALVLTP TRELAVQVKE DITNIGRFKR IKAAAVYGKS PFARQKLELK
     QKTHIVVGTP GRVLDHIEKG TLSLECLKYL VIDEADEMLN MGFIDQVEAI IDELPTKRMT
     MLFSATLPED VEKLSRTYMN SPTHIEIKAA GITTDKIEHT LFEVIEDEKL SLLKDVTTIE
     NPDSCIIFCR TQENVDHVYR QLKRANYPCD KIHGGMVQED RFEVMDDFRK GKFRYLVATD
     VAARGIDIDN ITHVINYDIP LEKESYVHRT GRTGRAGNSG KAITFITPYE NRFLEEIEEY
     IGFEIPKAIG PSKEEVMKEK AAFEEKLHAK PIIKKDKNAD INKGIMKLYF NGGKKKKIRA
     VDFVGTIAKI KGVTAEDIGI ITIQDNVSYV EILNGKGPLV LKVMKTTTIK GKQLKVHEAI
     K
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024