ID I3Y726_THIV6 Unreviewed; 72 AA.
AC I3Y726;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Translational regulator CsrA {ECO:0000256|HAMAP-Rule:MF_00167};
DE AltName: Full=Carbon storage regulator {ECO:0000256|HAMAP-Rule:MF_00167};
GN Name=csrA {ECO:0000256|HAMAP-Rule:MF_00167};
GN OrderedLocusNames=Thivi_0742 {ECO:0000313|EMBL:AFL72794.1};
OS Thiocystis violascens (strain ATCC 17096 / DSM 198 / 6111) (Chromatium
OS violascens).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thiocystis.
OX NCBI_TaxID=765911 {ECO:0000313|EMBL:AFL72794.1, ECO:0000313|Proteomes:UP000006062};
RN [1] {ECO:0000313|EMBL:AFL72794.1, ECO:0000313|Proteomes:UP000006062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17096 / DSM 198 / 6111
RC {ECO:0000313|Proteomes:UP000006062};
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., Vogl K., Liu Z.,
RA Frigaard N.-U., Bryant D., Woyke T.;
RT "Complete sequence of Thiocystis violascens DSM 198.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: A key translational regulator that binds mRNA to regulate
CC translation initiation and/or mRNA stability. Mediates global changes
CC in gene expression, shifting from rapid growth to stress survival by
CC linking envelope stress, the stringent response and the catabolite
CC repression systems. Usually binds in the 5'-UTR; binding at or near the
CC Shine-Dalgarno sequence prevents ribosome-binding, repressing
CC translation, binding elsewhere in the 5'-UTR can activate translation
CC and/or stabilize the mRNA. Its function is antagonized by small RNA(s).
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}.
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DR EMBL; CP003154; AFL72794.1; -; Genomic_DNA.
DR AlphaFoldDB; I3Y726; -.
DR STRING; 765911.Thivi_0742; -.
DR KEGG; tvi:Thivi_0742; -.
DR eggNOG; COG1551; Bacteria.
DR HOGENOM; CLU_164837_2_1_6; -.
DR OrthoDB; 9809061at2; -.
DR Proteomes; UP000006062; 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:0006402; P:mRNA catabolic process; IEA:InterPro.
DR GO; GO:0045947; P:negative regulation of translational initiation; IEA:UniProtKB-UniRule.
DR GO; GO:0045948; P:positive regulation of translational initiation; IEA:UniProtKB-UniRule.
DR GO; GO:0006109; P:regulation of carbohydrate metabolic process; IEA:UniProtKB-UniRule.
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 Activator {ECO:0000256|ARBA:ARBA00023159, ECO:0000256|HAMAP-Rule:MF_00167};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00167};
KW Reference proteome {ECO:0000313|Proteomes:UP000006062};
KW Repressor {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 72 AA; 8008 MW; 2D2ED800BAE1EAF5 CRC64;
MLILTRRVGE TLMIGDEVTV TVLGVKGNQV RIGVNAPREV SVHREEIYER IKREQADVGQ
GVIPMEHAGQ LD
//
