ID   CSRA_THEAB              Reviewed;          73 AA.
AC   B7IFV7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Translational regulator CsrA {ECO:0000255|HAMAP-Rule:MF_00167};
GN   Name=csrA {ECO:0000255|HAMAP-Rule:MF_00167}; OrderedLocusNames=THA_480;
OS   Thermosipho africanus (strain TCF52B).
OC   Bacteria; Thermotogae; Thermotogales; Fervidobacteriaceae; Thermosipho.
OX   NCBI_TaxID=484019;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TCF52B;
RX   PubMed=19124572; DOI=10.1128/jb.01448-08;
RA   Nesboe C.L., Bapteste E., Curtis B., Dahle H., Lopez P., Macleod D.,
RA   Dlutek M., Bowman S., Zhaxybayeva O., Birkeland N.-K., Doolittle W.F.;
RT   "The genome of Thermosipho africanus TCF52B: lateral genetic connections to
RT   the Firmicutes and Archaea.";
RL   J. Bacteriol. 191:1974-1978(2009).
CC   -!- FUNCTION: A translational regulator that binds mRNA to regulate
CC       translation initiation and/or mRNA stability. Usually binds in the 5'-
CC       UTR at or near the Shine-Dalgarno sequence preventing ribosome-binding,
CC       thus repressing translation. Its main target seems to be the major
CC       flagellin gene, while its function is anatagonized by FliW.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001185; ACJ74971.1; -; Genomic_DNA.
DR   RefSeq; WP_004104262.1; NC_011653.1.
DR   AlphaFoldDB; B7IFV7; -.
DR   SMR; B7IFV7; -.
DR   STRING; 484019.THA_480; -.
DR   EnsemblBacteria; ACJ74971; ACJ74971; THA_480.
DR   KEGG; taf:THA_480; -.
DR   eggNOG; COG1551; Bacteria.
DR   HOGENOM; CLU_164837_0_1_0; -.
DR   OMA; IHRKEVY; -.
DR   Proteomes; UP000002453; 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:0044781; P:bacterial-type flagellum organization; IEA:UniProtKB-KW.
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:1902208; P:regulation of bacterial-type flagellum assembly; IEA:UniProtKB-UniRule.
DR   GO; GO:0006109; P:regulation of carbohydrate metabolic process; IEA:InterPro.
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   Bacterial flagellum biogenesis; Cytoplasm; Reference proteome; Repressor;
KW   RNA-binding; Translation regulation.
FT   CHAIN           1..73
FT                   /note="Translational regulator CsrA"
FT                   /id="PRO_1000118242"
SQ   SEQUENCE   73 AA;  8337 MW;  01A58461F87EF30D CRC64;
     MLVLSRKIGQ SIIIGNDIEI KILKIDGGEI KIGIEAPKDV KVLRKELYEE LLKENKEAVK
     FDIKNLPGFF KKK