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CSHA_LISMO
ID   CSHA_LISMO              Reviewed;         520 AA.
AC   Q8Y8N0;
DT   03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=ATP-dependent RNA helicase CshA;
DE            EC=3.6.4.13 {ECO:0000255|HAMAP-Rule:MF_01493};
GN   Name=cshA {ECO:0000255|HAMAP-Rule:MF_01493}; OrderedLocusNames=lmo0866;
OS   Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=169963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-679 / EGD-e;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA   Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA   Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA   Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA   Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA   Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA   Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
RN   [2]
RP   FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC BAA-679 / EGD-e;
RX   PubMed=22820328; DOI=10.1128/aem.01526-12;
RA   Markkula A., Lindstrom M., Johansson P., Bjorkroth J., Korkeala H.;
RT   "Roles of four putative DEAD-box RNA helicase genes in growth of Listeria
RT   monocytogenes EGD-e under heat, pH, osmotic, ethanol, and oxidative stress
RT   conditions.";
RL   Appl. Environ. Microbiol. 78:6875-6882(2012).
RN   [3]
RP   FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC BAA-679 / EGD-e;
RX   PubMed=22564273; DOI=10.1111/j.1462-2920.2012.02761.x;
RA   Markkula A., Mattila M., Lindstrom M., Korkeala H.;
RT   "Genes encoding putative DEAD-box RNA helicases in Listeria monocytogenes
RT   EGD-e are needed for growth and motility at 3 degrees C.";
RL   Environ. Microbiol. 14:2223-2232(2012).
CC   -!- FUNCTION: DEAD-box RNA helicase possibly involved in RNA degradation.
CC       Unwinds dsRNA in both 5'- and 3'-directions, has RNA-dependent ATPase
CC       activity (By similarity). Involved in cold tolerance, motility and
CC       alcohol tolerance. {ECO:0000255|HAMAP-Rule:MF_01493,
CC       ECO:0000269|PubMed:22564273, ECO:0000269|PubMed:22820328}.
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_01493};
CC   -!- SUBUNIT: Oligomerizes, may be a member of the RNA degradosome.
CC       {ECO:0000255|HAMAP-Rule:MF_01493}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01493}.
CC   -!- INDUCTION: By growth at 3 degrees Celsius (PubMed:22564273), repressed
CC       by 6% NaCl (PubMed:22820328). {ECO:0000269|PubMed:22564273,
CC       ECO:0000269|PubMed:22820328}.
CC   -!- DISRUPTION PHENOTYPE: Growth rate decreased at 37 and 25 degrees
CC       Celsius, completely stopped at 3 degrees Celsius. No motility at 25 or
CC       3 degrees Celsius (PubMed:22564273). Decreased growth in the presence
CC       of ethanol (PubMed:22820328). {ECO:0000269|PubMed:22564273,
CC       ECO:0000269|PubMed:22820328}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. CshA subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01493}.
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DR   EMBL; AL591977; CAC98944.1; -; Genomic_DNA.
DR   PIR; AB1183; AB1183.
DR   RefSeq; NP_464392.1; NC_003210.1.
DR   RefSeq; WP_003732374.1; NZ_CP023861.1.
DR   AlphaFoldDB; Q8Y8N0; -.
DR   SMR; Q8Y8N0; -.
DR   STRING; 169963.lmo0866; -.
DR   PaxDb; Q8Y8N0; -.
DR   EnsemblBacteria; CAC98944; CAC98944; CAC98944.
DR   GeneID; 984613; -.
DR   KEGG; lmo:lmo0866; -.
DR   PATRIC; fig|169963.11.peg.890; -.
DR   eggNOG; COG0513; Bacteria.
DR   HOGENOM; CLU_003041_21_1_9; -.
DR   OMA; EHKDGQR; -.
DR   PhylomeDB; Q8Y8N0; -.
DR   BioCyc; LMON169963:LMO0866-MON; -.
DR   PHI-base; PHI:6510; -.
DR   PHI-base; PHI:7620; -.
DR   Proteomes; UP000000817; 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:0000027; P:ribosomal large subunit assembly; IBA:GO_Central.
DR   GO; GO:0006401; P:RNA catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0010501; P:RNA secondary structure unwinding; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 2.
DR   HAMAP; MF_01493; DEAD_helicase_CshA; 1.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR030880; DEAD_helicase_CshA.
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; 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   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Helicase; Hydrolase; Nucleotide-binding;
KW   Reference proteome; RNA-binding; Stress response.
FT   CHAIN           1..520
FT                   /note="ATP-dependent RNA helicase CshA"
FT                   /id="PRO_0000430102"
FT   DOMAIN          33..203
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01493"
FT   DOMAIN          214..374
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01493"
FT   REGION          428..520
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           2..30
FT                   /note="Q motif"
FT   MOTIF           151..154
FT                   /note="DEAD box"
FT   BINDING         46..53
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01493"
SQ   SEQUENCE   520 AA;  57309 MW;  A6CEA7439DC3212E CRC64;
     MTKFSEFGLD EKIVKSVNRM GFEEATPIQE KTIPLGLEGK DLIGQAQTGT GKTAAFGLPM
     IHKIDQKSNN VQALIIAPTR ELAIQVSEEL YKLSYDKHVR VLAVYGGSDI SRQIRSLKKN
     PQIVVGTPGR ILDHINRRTL KLDHVETLVL DEADEMLNMG FIDDIETILK EVPAERQTLL
     FSATMPDPIR RIGERFMHSP ELIRIKAKEM TALLIEQFFV KVHEKEKFDV LSRLLDVQAP
     ELAIVFGRTK RRVDELSRAL DMRGYVAEGI HGDLTQAKRM SVLRKFKEGK IDVLVATDVA
     ARGLDISGVT HVYNYDIPQD PESYVHRIGR TGRAGKEGMA ITFVQPREMG YLRIVEETTK
     KRMQPLQAPT WDEAFAGQLR VATEKIQEAI TEENLADYKT FANELLEKYD ATDIAAAMLK
     MLAKEPDKTP VHITEERPLP SRGGGGYKGK NGKGGKGGGY RGGSGKGGSY RDRNNSGKGR
     RSGGGSGGGS GSGGGGNRDR RGGGEQRSGG NKGNYSQKSK
 
 
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