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CSRA_BORDL
ID   CSRA_BORDL              Reviewed;          78 AA.
AC   B5RL10;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Translational regulator CsrA {ECO:0000255|HAMAP-Rule:MF_00167};
GN   Name=csrA {ECO:0000255|HAMAP-Rule:MF_00167}; OrderedLocusNames=BDU_183;
OS   Borrelia duttonii (strain Ly).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borrelia.
OX   NCBI_TaxID=412419;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ly;
RX   PubMed=18787695; DOI=10.1371/journal.pgen.1000185;
RA   Lescot M., Audic S., Robert C., Nguyen T.T., Blanc G., Cutler S.J.,
RA   Wincker P., Couloux A., Claverie J.-M., Raoult D., Drancourt M.;
RT   "The genome of Borrelia recurrentis, the agent of deadly louse-borne
RT   relapsing fever, is a degraded subset of tick-borne Borrelia duttonii.";
RL   PLoS Genet. 4:E1000185-E1000185(2008).
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; CP000976; ACH93139.1; -; Genomic_DNA.
DR   RefSeq; WP_012537951.1; NC_011229.1.
DR   AlphaFoldDB; B5RL10; -.
DR   SMR; B5RL10; -.
DR   STRING; 412419.BDU_183; -.
DR   EnsemblBacteria; ACH93139; ACH93139; BDU_183.
DR   KEGG; bdu:BDU_183; -.
DR   eggNOG; COG1551; Bacteria.
DR   HOGENOM; CLU_164837_0_2_12; -.
DR   OMA; IHRKEVY; -.
DR   Proteomes; UP000000611; 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; Repressor; RNA-binding;
KW   Translation regulation.
FT   CHAIN           1..78
FT                   /note="Translational regulator CsrA"
FT                   /id="PRO_1000097479"
SQ   SEQUENCE   78 AA;  9129 MW;  3B98D9DEE8C865F3 CRC64;
     MLVLSRKANE SIKIDSNIEI SILEIKKDSV KIAIKAPENI KILRSEIYDI IKEENKKSIL
     QDKNNIHKIK KLFDYFSK
 
 
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