ID F8FWJ2_PSEP6 Unreviewed; 62 AA. AC F8FWJ2; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 28-FEB-2018, entry version 38. 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 ORFNames=PPS_3816 {ECO:0000313|EMBL:AEJ14357.1}; OS Pseudomonas putida (strain S16). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1042876 {ECO:0000313|EMBL:AEJ14357.1, ECO:0000313|Proteomes:UP000000502}; RN [1] {ECO:0000313|EMBL:AEJ14357.1, ECO:0000313|Proteomes:UP000000502} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S16 {ECO:0000313|EMBL:AEJ14357.1, RC ECO:0000313|Proteomes:UP000000502}; RX PubMed=21914868; DOI=10.1128/JB.05663-11; RA Yu H., Tang H., Wang L., Yao Y., Wu G., Xu P.; RT "Complete genome sequence of the nicotine-degrading Pseudomonas putida RT strain S16."; RL J. Bacteriol. 193:5541-5542(2011). CC -!- FUNCTION: A key translational regulator that binds mRNA to CC regulate translation initiation and/or mRNA stability. Mediates CC global changes in gene expression, shifting from rapid growth to CC stress survival by linking envelope stress, the stringent response CC and the catabolite repression systems. Usually binds in the 5'- CC UTR; binding at or near the Shine-Dalgarno sequence prevents CC ribosome-binding, repressing translation, binding elsewhere in the CC 5'-UTR can activate translation and/or stabilize the mRNA. Its CC function is antagonized by small RNA(s). {ECO:0000256|HAMAP- CC Rule:MF_00167}. CC -!- SUBUNIT: Homodimer; the beta-strands of each monomer intercalate CC to form a hydrophobic core, while the alpha-helices form wings CC that extend away from the core. {ECO:0000256|HAMAP-Rule:MF_00167, CC ECO:0000256|SAAS:SAAS00970188}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00167, CC ECO:0000256|SAAS:SAAS00970186}. CC -!- SIMILARITY: Belongs to the CsrA/RsmA family. {ECO:0000256|HAMAP- CC Rule:MF_00167, ECO:0000256|SAAS:SAAS00970183}. 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; CP002870; AEJ14357.1; -; Genomic_DNA. DR RefSeq; WP_003254503.1; NC_015733.1. DR ProteinModelPortal; F8FWJ2; -. DR STRING; 1042876.PPS_3816; -. DR EnsemblBacteria; AEJ14357; AEJ14357; PPS_3816. DR GeneID; 32806911; -. DR KEGG; ppt:PPS_3816; -. DR eggNOG; COG1551; LUCA. DR KO; K03563; -. DR Proteomes; UP000000502; 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 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 ProDom; PD009007; CsrA; 1. DR SUPFAM; SSF117130; SSF117130; 1. DR TIGRFAMs; TIGR00202; csrA; 1. PE 3: Inferred from homology; KW Activator {ECO:0000256|HAMAP-Rule:MF_00167, KW ECO:0000256|SAAS:SAAS00970192}; KW Complete proteome {ECO:0000313|Proteomes:UP000000502}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00167, KW ECO:0000256|SAAS:SAAS00970182}; KW Repressor {ECO:0000256|HAMAP-Rule:MF_00167, KW ECO:0000256|SAAS:SAAS00970189}; KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_00167, KW ECO:0000256|SAAS:SAAS00702517}; KW Translation regulation {ECO:0000256|HAMAP-Rule:MF_00167, KW ECO:0000256|SAAS:SAAS00970191}. SQ SEQUENCE 62 AA; 6902 MW; C8F9A722DC8D68CC CRC64; MLILTRRCAE SLIIGDGEIT VTVLGVKGNQ VRIGVSAPKE VAVHREEIYL RIKKEKDEEP SL //