CSRA_STRM5
ID CSRA_STRM5 Reviewed; 67 AA.
AC B4SRB3;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Translational regulator CsrA {ECO:0000255|HAMAP-Rule:MF_00167};
DE AltName: Full=Carbon storage regulator {ECO:0000255|HAMAP-Rule:MF_00167};
GN Name=csrA {ECO:0000255|HAMAP-Rule:MF_00167}; OrderedLocusNames=Smal_1479;
OS Stenotrophomonas maltophilia (strain R551-3).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX NCBI_TaxID=391008;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R551-3;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Taghavi S.,
RA Monchy S., Newman L., Vangronsveld J., van der Lelie D., Richardson P.;
RT "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL Submitted (JUN-2008) 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: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; CP001111; ACF51184.1; -; Genomic_DNA.
DR RefSeq; WP_004152909.1; NC_011071.1.
DR AlphaFoldDB; B4SRB3; -.
DR SMR; B4SRB3; -.
DR STRING; 391008.Smal_1479; -.
DR EnsemblBacteria; ACF51184; ACF51184; Smal_1479.
DR GeneID; 61465579; -.
DR KEGG; smt:Smal_1479; -.
DR eggNOG; COG1551; Bacteria.
DR HOGENOM; CLU_164837_2_1_6; -.
DR OMA; IHRKEVY; -.
DR OrthoDB; 2032250at2; -.
DR BioCyc; SMAL391008:SMAL_RS07615-MON; -.
DR Proteomes; UP000001867; 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; -; 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 Activator; Cytoplasm; Repressor; RNA-binding; Translation regulation.
FT CHAIN 1..67
FT /note="Translational regulator CsrA"
FT /id="PRO_1000097511"
SQ SEQUENCE 67 AA; 7180 MW; A195D5CD0F7A398B CRC64;
MLILTRRVGE TLMIGDSVSV TVLGVKGNQV RIGITAPKDV AVHREEIYQR IQRGDEAGGT
GSENSAE