CSRA_DICNV
ID CSRA_DICNV Reviewed; 64 AA.
AC A5EWA3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 25-MAY-2022, entry version 77.
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=DNO_0284;
OS Dichelobacter nodosus (strain VCS1703A).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Cardiobacteriales;
OC Cardiobacteriaceae; Dichelobacter.
OX NCBI_TaxID=246195;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VCS1703A;
RX PubMed=17468768; DOI=10.1038/nbt1302;
RA Myers G.S.A., Parker D., Al-Hasani K., Kennan R.M., Seemann T., Ren Q.,
RA Badger J.H., Selengut J.D., Deboy R.T., Tettelin H., Boyce J.D.,
RA McCarl V.P., Han X., Nelson W.C., Madupu R., Mohamoud Y., Holley T.,
RA Fedorova N., Khouri H., Bottomley S.P., Whittington R.J., Adler B.,
RA Songer J.G., Rood J.I., Paulsen I.T.;
RT "Genome sequence and identification of candidate vaccine antigens from the
RT animal pathogen Dichelobacter nodosus.";
RL Nat. Biotechnol. 25:569-575(2007).
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; CP000513; ABQ13329.1; -; Genomic_DNA.
DR RefSeq; WP_012030628.1; NC_009446.1.
DR AlphaFoldDB; A5EWA3; -.
DR SMR; A5EWA3; -.
DR STRING; 246195.DNO_0284; -.
DR EnsemblBacteria; ABQ13329; ABQ13329; DNO_0284.
DR KEGG; dno:DNO_0284; -.
DR eggNOG; COG1551; Bacteria.
DR HOGENOM; CLU_164837_2_1_6; -.
DR OMA; KDVQVHR; -.
DR OrthoDB; 2032250at2; -.
DR Proteomes; UP000000248; 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..64
FT /note="Translational regulator CsrA"
FT /id="PRO_1000023379"
SQ SEQUENCE 64 AA; 7240 MW; 550EC3E95078391B CRC64;
MLILTRRVGE TIIIDDQIKV TVLAVKGNQV RLGVQAPDEI AIHREEIYHR LMNGVGDDAE
MEKK