ID   CSRA_TREPS              Reviewed;          73 AA.
AC   B2S3P6;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Translational regulator CsrA {ECO:0000255|HAMAP-Rule:MF_00167};
GN   Name=csrA {ECO:0000255|HAMAP-Rule:MF_00167}; OrderedLocusNames=TPASS_0657;
OS   Treponema pallidum subsp. pallidum (strain SS14).
OC   Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX   NCBI_TaxID=455434;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS14;
RX   PubMed=18482458; DOI=10.1186/1471-2180-8-76;
RA   Matejkova P., Strouhal M., Smajs D., Norris S.J., Palzkill T.,
RA   Petrosino J.F., Sodergren E., Norton J.E., Singh J., Richmond T.A.,
RA   Molla M.N., Albert T.J., Weinstock G.M.;
RT   "Complete genome sequence of Treponema pallidum ssp. pallidum strain SS14
RT   determined with oligonucleotide arrays.";
RL   BMC Microbiol. 8:76-76(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; CP000805; ACD71075.1; -; Genomic_DNA.
DR   RefSeq; WP_010882102.1; NC_021508.1.
DR   AlphaFoldDB; B2S3P6; -.
DR   SMR; B2S3P6; -.
DR   EnsemblBacteria; ACD71075; ACD71075; TPASS_0657.
DR   GeneID; 57879180; -.
DR   KEGG; tpp:TPASS_0657; -.
DR   PATRIC; fig|455434.6.peg.650; -.
DR   OMA; IHRKEVY; -.
DR   Proteomes; UP000001202; 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..73
FT                   /note="Translational regulator CsrA"
FT                   /id="PRO_1000097514"
FT   REGION          54..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   73 AA;  8336 MW;  45FA16B082FF25FF CRC64;
     MLILSRKTNQ KIFIGDSIEL TIIEIRGDQV KVGVEAPRSV KIFRQEVYEE IQRENRAASD
     SPWSPNSLPQ LPV