CSRA_CAMJE
ID CSRA_CAMJE Reviewed; 75 AA.
AC Q0P9F1;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Translational regulator CsrA {ECO:0000255|HAMAP-Rule:MF_00167};
GN Name=csrA {ECO:0000255|HAMAP-Rule:MF_00167}; OrderedLocusNames=Cj1103;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
RN [2]
RP FUNCTION AS A TRANSLATION REPRESSOR, INTERACTION WITH FLIW, INDUCTION,
RP DISRUPTION PHENOTYPE, AND RNA-BINDING.
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=27229370; DOI=10.1038/ncomms11667;
RA Dugar G., Svensson S.L., Bischler T., Waeldchen S., Reinhardt R., Sauer M.,
RA Sharma C.M.;
RT "The CsrA-FliW network controls polar localization of the dual-function
RT flagellin mRNA in Campylobacter jejuni.";
RL Nat. Commun. 7:11667-11667(2016).
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. Binds mRNA; 77% of enriched bound RNA is
CC for flagellin A (flaA) while another 13% encodes other flagellar or
CC motility-related genes. Binds mRNA in 5'-UTR or intergenic regions,
CC binds consensus 5'-AAGGA-3' in the loop of a predicted stem-loop
CC structure. Binds at least 2 sites in the 5'-UTR of flaA mRNA and
CC represses its translation; mutation of the binding sites abolishes
CC binding and leads to increased amounts of FlaA protein. Translation
CC repression is antagonized by FliW, probably by its direct binding to
CC CsrA, which allows translation of FlaA and probably other flagellar
CC proteins (PubMed:27229370). Influences the localization of flaA
CC transcripts to poles of short, probably elongating, cells.
CC {ECO:0000269|PubMed:27229370}.
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 (By similarity). Binds to FliW (PubMed:27229370).
CC {ECO:0000250|UniProtKB:O69078, ECO:0000269|PubMed:27229370}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00167}.
CC -!- INDUCTION: Constitutively expressed (at protein level).
CC {ECO:0000269|PubMed:27229370}.
CC -!- DISRUPTION PHENOTYPE: No visible growth phenotype, increased expression
CC of the flagellin A (flaA) the major flagellar filament component.
CC Flagella appear normal, the average swimming distance decreases about
CC 20%. Expression of other flagellar genes is not visibly affected unless
CC flaA is also mutated, when an increase in their expression is then
CC seen. mRNA for flaA remain localized to the cell pole. A double csrA-
CC fliW deletion expresses the same amount of flagellin A as the csrA
CC deletion, has 2 wild-type length flagella, a wild-type swimming
CC distance and restored cell pole localization of flaA mRNA.
CC {ECO:0000269|PubMed:27229370}.
CC -!- SIMILARITY: Belongs to the CsrA/RsmA family. {ECO:0000255|HAMAP-
CC Rule:MF_00167}.
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DR EMBL; AL111168; CAL35220.1; -; Genomic_DNA.
DR PIR; B81314; B81314.
DR RefSeq; WP_002852854.1; NC_002163.1.
DR RefSeq; YP_002344496.1; NC_002163.1.
DR AlphaFoldDB; Q0P9F1; -.
DR SMR; Q0P9F1; -.
DR IntAct; Q0P9F1; 54.
DR STRING; 192222.Cj1103; -.
DR PaxDb; Q0P9F1; -.
DR PRIDE; Q0P9F1; -.
DR EnsemblBacteria; CAL35220; CAL35220; Cj1103.
DR GeneID; 905394; -.
DR KEGG; cje:Cj1103; -.
DR PATRIC; fig|192222.6.peg.1085; -.
DR eggNOG; COG1551; Bacteria.
DR HOGENOM; CLU_164837_0_2_7; -.
DR OMA; RDESIMI; -.
DR PHI-base; PHI:6341; -.
DR Proteomes; UP000000799; 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 1: Evidence at protein level;
KW Bacterial flagellum biogenesis; Cytoplasm; Reference proteome; Repressor;
KW RNA-binding; Translation regulation.
FT CHAIN 1..75
FT /note="Translational regulator CsrA"
FT /id="PRO_0000442647"
SQ SEQUENCE 75 AA; 8441 MW; B353436EC460C031 CRC64;
MLILSRKENE SIIIGEGIEI KVVQTGKGYA KIGIEAPKSL MILRKELVQQ VKDENLHSVV
QNDIKLDDLS KKLIK
