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CSRA_XANCP
ID   CSRA_XANCP              Reviewed;          70 AA.
AC   Q8P9W9;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 94.
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=XCC1725;
OS   Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS   528 / LMG 568 / P 25).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=190485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX   PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA   Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA   Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA   Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA   Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA   Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA   Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA   Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA   Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA   Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA   Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA   Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA   Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT   specificities.";
RL   Nature 417:459-463(2002).
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; AE008922; AAM41019.1; -; Genomic_DNA.
DR   RefSeq; NP_637095.1; NC_003902.1.
DR   RefSeq; WP_011036902.1; NC_003902.1.
DR   AlphaFoldDB; Q8P9W9; -.
DR   SMR; Q8P9W9; -.
DR   STRING; 340.xcc-b100_2534; -.
DR   EnsemblBacteria; AAM41019; AAM41019; XCC1725.
DR   KEGG; xcc:XCC1725; -.
DR   PATRIC; fig|190485.4.peg.1842; -.
DR   eggNOG; COG1551; Bacteria.
DR   HOGENOM; CLU_164837_2_1_6; -.
DR   OMA; IHRKEVY; -.
DR   Proteomes; UP000001010; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0048027; F:mRNA 5'-UTR binding; IBA:GO_Central.
DR   GO; GO:0006402; P:mRNA catabolic process; IEA:InterPro.
DR   GO; GO:0045947; P:negative regulation of translational initiation; IBA:GO_Central.
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..70
FT                   /note="Translational regulator CsrA"
FT                   /id="PRO_0000177101"
SQ   SEQUENCE   70 AA;  7680 MW;  45B15FE348082398 CRC64;
     MLILTRRVGE TLMIGDLVTV TVLGVKGNQV RIGIDAPKDV AVHREEIYQR IQRGDEPVAS
     GAHHNDDCSD
 
 
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