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CSRA_IDILO
ID   CSRA_IDILO              Reviewed;          62 AA.
AC   Q5QUV8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=Translational regulator CsrA {ECO:0000255|HAMAP-Rule:MF_00167};
DE   AltName: Full=Carbon storage regulator {ECO:0000255|HAMAP-Rule:MF_00167};
GN   Name=csrA {ECO:0000255|HAMAP-Rule:MF_00167}; OrderedLocusNames=IL1737;
OS   Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae; Idiomarina.
OX   NCBI_TaxID=283942;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-735 / DSM 15497 / L2-TR;
RX   PubMed=15596722; DOI=10.1073/pnas.0407638102;
RA   Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y.,
RA   Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S.,
RA   Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S.,
RA   Denery J., Aizawa S., Shibata S., Malahoff A., Alam M.;
RT   "Genome sequence of the deep-sea gamma-proteobacterium Idiomarina
RT   loihiensis reveals amino acid fermentation as a source of carbon and
RT   energy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004).
CC   -!- FUNCTION: A key translational regulator that binds mRNA to regulate
CC       translation initiation and/or mRNA stability. Mediates global changes
CC       in gene expression, shifting from rapid growth to stress survival by
CC       linking envelope stress, the stringent response and the catabolite
CC       repression systems. Usually binds in the 5'-UTR; binding at or near the
CC       Shine-Dalgarno sequence prevents ribosome-binding, repressing
CC       translation, binding elsewhere in the 5'-UTR can activate translation
CC       and/or stabilize the mRNA. Its function is antagonized by small RNA(s).
CC       {ECO:0000255|HAMAP-Rule:MF_00167}.
CC   -!- SUBUNIT: Homodimer; the beta-strands of each monomer intercalate to
CC       form a hydrophobic core, while the alpha-helices form wings that extend
CC       away from the core. {ECO:0000255|HAMAP-Rule:MF_00167}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00167}.
CC   -!- SIMILARITY: Belongs to the CsrA/RsmA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00167}.
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DR   EMBL; AE017340; AAV82570.1; -; Genomic_DNA.
DR   RefSeq; WP_011234973.1; NC_006512.1.
DR   AlphaFoldDB; Q5QUV8; -.
DR   SMR; Q5QUV8; -.
DR   STRING; 283942.IL1737; -.
DR   EnsemblBacteria; AAV82570; AAV82570; IL1737.
DR   KEGG; ilo:IL1737; -.
DR   eggNOG; COG1551; Bacteria.
DR   HOGENOM; CLU_164837_2_1_6; -.
DR   OMA; IHRKEVY; -.
DR   OrthoDB; 2032250at2; -.
DR   Proteomes; UP000001171; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0048027; F:mRNA 5'-UTR binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006402; P:mRNA catabolic process; IEA:InterPro.
DR   GO; GO:0045947; P:negative regulation of translational initiation; IEA:UniProtKB-UniRule.
DR   GO; GO:0045948; P:positive regulation of translational initiation; IEA:UniProtKB-UniRule.
DR   GO; GO:0006109; P:regulation of carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.60.40.4380; -; 1.
DR   HAMAP; MF_00167; CsrA; 1.
DR   InterPro; IPR003751; CsrA.
DR   InterPro; IPR036107; CsrA_sf.
DR   PANTHER; PTHR34984; PTHR34984; 1.
DR   Pfam; PF02599; CsrA; 1.
DR   SUPFAM; SSF117130; SSF117130; 1.
DR   TIGRFAMs; TIGR00202; csrA; 1.
PE   3: Inferred from homology;
KW   Activator; Cytoplasm; Reference proteome; Repressor; RNA-binding;
KW   Translation regulation.
FT   CHAIN           1..62
FT                   /note="Translational regulator CsrA"
FT                   /id="PRO_1000023391"
SQ   SEQUENCE   62 AA;  7012 MW;  C749959A0E6F5E5A CRC64;
     MLILTRRVGE TLMIGDDVSV TVLGVKGNQV RIGVNAPKDV SVHREEIYMR IQSEKDDEQD
     KE
 
 
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