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CSHB_BACCR
ID   CSHB_BACCR              Reviewed;         436 AA.
AC   Q818H2;
DT   03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=DEAD-box ATP-dependent RNA helicase CshB {ECO:0000255|HAMAP-Rule:MF_01494};
DE            EC=3.6.4.13 {ECO:0000255|HAMAP-Rule:MF_01494};
GN   Name=cshB {ECO:0000255|HAMAP-Rule:MF_01494}; OrderedLocusNames=BC_4283;
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   FUNCTION, 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: Probable DEAD-box RNA helicase. May work in conjunction with
CC       the cold shock proteins to ensure proper initiation of transcription at
CC       low and optimal temperatures. Unwinds dsRNA in both 5'- and 3'-
CC       directions and shows RNA-dependent ATPase activity (By similarity).
CC       Probably has a somewhat redundant function with CshA, as cshA can
CC       partially complement the growth effects of a cshB deletion.
CC       {ECO:0000255|HAMAP-Rule:MF_01494, ECO:0000269|PubMed:21705526}.
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_01494};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01494}.
CC   -!- INDUCTION: Induced at 10 degrees Celsius. {ECO:0000269|PubMed:20709848,
CC       ECO:0000269|PubMed:21705526}.
CC   -!- DISRUPTION PHENOTYPE: Longer lag phase at 20 degrees Celsius, wild-type
CC       growth rate at 30 degrees Celsius, impaired growth at 10 degrees
CC       Celsius. At 12 degrees Celsius cells form very long filaments, with
CC       incompletely divided, thickened internal membranes. Effects on growth
CC       at reduced temperature are partially complemented by cshA, suggesting
CC       the 2 genes have a partially redundant function. Decreased growth in
CC       the presence of H(2)O(2) and diamide. {ECO:0000269|PubMed:20709848,
CC       ECO:0000269|PubMed:21705526}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. CshB subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01494}.
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DR   EMBL; AE016877; AAP11197.1; -; Genomic_DNA.
DR   RefSeq; NP_833996.1; NC_004722.1.
DR   RefSeq; WP_000194021.1; NC_004722.1.
DR   AlphaFoldDB; Q818H2; -.
DR   SMR; Q818H2; -.
DR   STRING; 226900.BC_4283; -.
DR   EnsemblBacteria; AAP11197; AAP11197; BC_4283.
DR   KEGG; bce:BC4283; -.
DR   PATRIC; fig|226900.8.peg.4427; -.
DR   HOGENOM; CLU_003041_1_3_9; -.
DR   OMA; IKPICRK; -.
DR   Proteomes; UP000001417; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0009409; P:response to cold; IEA:InterPro.
DR   GO; GO:0000027; P:ribosomal large subunit assembly; IBA:GO_Central.
DR   GO; GO:0006401; P:RNA catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.300; -; 2.
DR   HAMAP; MF_01494; DEAD_helicase_CshB; 1.
DR   InterPro; IPR030881; CshB.
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; 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; 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; RNA-binding; Stress response.
FT   CHAIN           1..436
FT                   /note="DEAD-box ATP-dependent RNA helicase CshB"
FT                   /id="PRO_0000430109"
FT   DOMAIN          35..209
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01494"
FT   DOMAIN          240..388
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01494"
FT   REGION          385..436
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           4..32
FT                   /note="Q motif"
FT   MOTIF           157..160
FT                   /note="DEAD box"
FT   COMPBIAS        385..406
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         48..55
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01494"
SQ   SEQUENCE   436 AA;  50065 MW;  90073DAFDF5C084A CRC64;
     MTQQTFTQYD FKPFLIDAVR ELRFTEPTGI QQKIFPVVKK GVSVIGQSQT GSGKTHAYLL
     PTLNRINASR EEVQLVITAP TRELAQQIYE EIVKLTKFCA EDQMITARCL IGGTDKQRSI
     EKLKKQPHIV VGTPGRIKDL VEEQALFVHK ANTIIVDEAD LMLDMGFIHD VDKIAARMPK
     NLQMLVFSAT IPQKLKPFLK KYMENPEHIH INPKQVAAGN IEHYLVPSKH RNKIDLVHKM
     LLQFKPYLAV VFTNTKKMAD QVADGLMERG LKVGRIHGDL SPRDRKKMMK QIRDLEFQYI
     VATDLAARGI DIQGISHVIN YQPPSDLDFF VHRVARTARA GHSGIAVTIY DPANEEALDS
     LEKQRHIEFK HVDLRGDEWA DLGERRRRKS RKKPNDELDV MATKVIKKPK KVKPNYKRKL
     ATERDKVKRK YSNKKR
 
 
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