ID   CSRA_YERE8              Reviewed;          61 AA.
AC   A1JK11;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Translational regulator CsrA {ECO:0000255|HAMAP-Rule:MF_00167};
DE   AltName: Full=Carbon storage regulator {ECO:0000255|HAMAP-Rule:MF_00167};
DE   AltName: Full=Post-transcriptional regulator RsmA {ECO:0000303|PubMed:16359708};
GN   Name=csrA {ECO:0000255|HAMAP-Rule:MF_00167};
GN   Synonyms=rsmA {ECO:0000303|PubMed:16359708}; OrderedLocusNames=YE0835;
OS   Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS   8081).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=393305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 13174 / 8081;
RX   PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA   Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA   Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA   Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA   Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA   Prentice M.B.;
RT   "The complete genome sequence and comparative genome analysis of the high
RT   pathogenicity Yersinia enterocolitica strain 8081.";
RL   PLoS Genet. 2:2039-2051(2006).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS).
RC   STRAIN=NCTC 13174 / 8081;
RX   PubMed=16359708; DOI=10.1016/j.jmb.2005.11.045;
RA   Heeb S., Kuehne S.A., Bycroft M., Crivii S., Allen M.D., Haas D.,
RA   Camara M., Williams P.;
RT   "Functional analysis of the post-transcriptional regulator RsmA reveals a
RT   novel RNA-binding site.";
RL   J. Mol. Biol. 355:1026-1036(2006).
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 (PubMed:16359708). {ECO:0000255|HAMAP-Rule:MF_00167,
CC       ECO:0000269|PubMed:16359708}.
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; AM286415; CAL10935.1; -; Genomic_DNA.
DR   RefSeq; WP_002209449.1; NC_008800.1.
DR   RefSeq; YP_001005173.1; NC_008800.1.
DR   PDB; 2BTI; X-ray; 2.00 A; A/B=1-61.
DR   PDBsum; 2BTI; -.
DR   AlphaFoldDB; A1JK11; -.
DR   SMR; A1JK11; -.
DR   STRING; 393305.YE0835; -.
DR   EnsemblBacteria; CAL10935; CAL10935; YE0835.
DR   GeneID; 7959308; -.
DR   KEGG; yen:YE0835; -.
DR   PATRIC; fig|393305.7.peg.929; -.
DR   eggNOG; COG1551; Bacteria.
DR   HOGENOM; CLU_164837_2_1_6; -.
DR   OMA; IHRKEVY; -.
DR   PRO; PR:A1JK11; -.
DR   Proteomes; UP000000642; 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   1: Evidence at protein level;
KW   3D-structure; Activator; Cytoplasm; Repressor; RNA-binding;
KW   Translation regulation.
FT   CHAIN           1..61
FT                   /note="Translational regulator CsrA"
FT                   /id="PRO_1000023442"
FT   STRAND          1..7
FT                   /evidence="ECO:0007829|PDB:2BTI"
FT   STRAND          11..14
FT                   /evidence="ECO:0007829|PDB:2BTI"
FT   TURN            15..17
FT                   /evidence="ECO:0007829|PDB:2BTI"
FT   STRAND          18..26
FT                   /evidence="ECO:0007829|PDB:2BTI"
FT   STRAND          29..36
FT                   /evidence="ECO:0007829|PDB:2BTI"
FT   STRAND          42..44
FT                   /evidence="ECO:0007829|PDB:2BTI"
FT   HELIX           45..55
FT                   /evidence="ECO:0007829|PDB:2BTI"
SQ   SEQUENCE   61 AA;  6853 MW;  16349BD4C2670E1C CRC64;
     MLILTRRVGE TLMIGDEVTV TVLGVKGNQV RIGVNAPKEV SVHREEIYQR IQAEKSQPTT
     Y