ID   CSRA_DESVM              Reviewed;          79 AA.
AC   B8DQY7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Translational regulator CsrA {ECO:0000255|HAMAP-Rule:MF_00167};
GN   Name=csrA {ECO:0000255|HAMAP-Rule:MF_00167}; OrderedLocusNames=DvMF_2526;
OS   Desulfovibrio vulgaris (strain DSM 19637 / Miyazaki F).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=883;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19637 / Miyazaki F;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Hazen T.C.,
RA   Richardson P.;
RT   "Complete sequence of Desulfovibrio vulgaris str. 'Miyazaki F'.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP001197; ACL09465.1; -; Genomic_DNA.
DR   RefSeq; WP_007526389.1; NC_011769.1.
DR   AlphaFoldDB; B8DQY7; -.
DR   SMR; B8DQY7; -.
DR   STRING; 883.DvMF_2526; -.
DR   EnsemblBacteria; ACL09465; ACL09465; DvMF_2526.
DR   KEGG; dvm:DvMF_2526; -.
DR   eggNOG; COG1551; Bacteria.
DR   HOGENOM; CLU_164837_0_2_7; -.
DR   OMA; IHRKEVY; -.
DR   OrthoDB; 2032250at2; -.
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; Repressor; RNA-binding;
KW   Translation regulation.
FT   CHAIN           1..79
FT                   /note="Translational regulator CsrA"
FT                   /id="PRO_1000118233"
SQ   SEQUENCE   79 AA;  9120 MW;  EF8B5EF5E501047A CRC64;
     MLILTRRPGE SLYLGDNIRI TILGMQGKQV KIGLDVPGDM VVYREEVYRR VMEENRMALE
     TSNADLLAAT QIWHDRTKE