ID R4KES3_9FIRM Unreviewed; 77 AA.
AC R4KES3;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Translational regulator CsrA {ECO:0000256|HAMAP-Rule:MF_00167};
GN Name=csrA {ECO:0000256|HAMAP-Rule:MF_00167};
GN ORFNames=Desgi_2276 {ECO:0000313|EMBL:AGL01698.1};
OS Desulfoscipio gibsoniae DSM 7213.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfallaceae;
OC Desulfoscipio.
OX NCBI_TaxID=767817 {ECO:0000313|EMBL:AGL01698.1, ECO:0000313|Proteomes:UP000013520};
RN [1] {ECO:0000313|EMBL:AGL01698.1, ECO:0000313|Proteomes:UP000013520}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7213 {ECO:0000313|EMBL:AGL01698.1,
RC ECO:0000313|Proteomes:UP000013520};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Parshina S.,
RA Plugge C., Muyzer G., Kuever J., Ivanova A., Nazina T., Klenk H.-P.,
RA Brambilla E., Spring S., Stams A.F., Woyke T.;
RT "Complete sequence of Desulfotomaculum gibsoniae DSM 7213.";
RL Submitted (JAN-2012) 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:0000256|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:0000256|HAMAP-Rule:MF_00167}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00167}.
CC -!- SIMILARITY: Belongs to the CsrA/RsmA family. {ECO:0000256|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; CP003273; AGL01698.1; -; Genomic_DNA.
DR RefSeq; WP_006522137.1; NC_021184.1.
DR AlphaFoldDB; R4KES3; -.
DR STRING; 767817.Desgi_2276; -.
DR KEGG; dgi:Desgi_2276; -.
DR eggNOG; COG1551; Bacteria.
DR HOGENOM; CLU_164837_0_2_9; -.
DR OrthoDB; 9809061at2; -.
DR Proteomes; UP000013520; 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; Translational regulator CsrA; 1.
DR HAMAP; MF_00167; CsrA; 1.
DR InterPro; IPR003751; CsrA.
DR InterPro; IPR036107; CsrA_sf.
DR NCBIfam; TIGR00202; csrA; 1.
DR PANTHER; PTHR34984; CARBON STORAGE REGULATOR; 1.
DR PANTHER; PTHR34984:SF1; CARBON STORAGE REGULATOR; 1.
DR Pfam; PF02599; CsrA; 1.
DR SUPFAM; SSF117130; CsrA-like; 1.
PE 3: Inferred from homology;
KW Bacterial flagellum biogenesis {ECO:0000256|ARBA:ARBA00022795,
KW ECO:0000256|HAMAP-Rule:MF_00167};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00167};
KW Reference proteome {ECO:0000313|Proteomes:UP000013520};
KW Repressor {ECO:0000256|ARBA:ARBA00022491, ECO:0000256|HAMAP-Rule:MF_00167};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_00167};
KW Translation regulation {ECO:0000256|ARBA:ARBA00022845, ECO:0000256|HAMAP-
KW Rule:MF_00167}.
SQ SEQUENCE 77 AA; 8480 MW; 056F69D8B13F9B6A CRC64;
MLVLTRKKKQ GIMLGDNISI TILEIGEDTI KIGIEAPKDV TILRSELYQA VKEENITAIT
SDHNAVDALK KIFANKG
//
