RRAA_SALTY
ID RRAA_SALTY Reviewed; 161 AA.
AC P67651; Q8XEL8;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Regulator of ribonuclease activity A {ECO:0000255|HAMAP-Rule:MF_00471};
GN Name=rraA {ECO:0000255|HAMAP-Rule:MF_00471}; OrderedLocusNames=STM4089;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
CC -!- FUNCTION: Globally modulates RNA abundance by binding to RNase E (Rne)
CC and regulating its endonucleolytic activity. Can modulate Rne action in
CC a substrate-dependent manner by altering the composition of the
CC degradosome. Modulates RNA-binding and helicase activities of the
CC degradosome. {ECO:0000255|HAMAP-Rule:MF_00471}.
CC -!- SUBUNIT: Homotrimer. Binds to both RNA-binding sites in the C-terminal
CC region of Rne and to RhlB. {ECO:0000255|HAMAP-Rule:MF_00471}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00471}.
CC -!- SIMILARITY: Belongs to the RraA family. {ECO:0000255|HAMAP-
CC Rule:MF_00471}.
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DR EMBL; AE006468; AAL22929.1; -; Genomic_DNA.
DR RefSeq; NP_462970.1; NC_003197.2.
DR RefSeq; WP_000872918.1; NC_003197.2.
DR AlphaFoldDB; P67651; -.
DR SMR; P67651; -.
DR STRING; 99287.STM4089; -.
DR PaxDb; P67651; -.
DR EnsemblBacteria; AAL22929; AAL22929; STM4089.
DR GeneID; 1255616; -.
DR KEGG; stm:STM4089; -.
DR PATRIC; fig|99287.12.peg.4310; -.
DR HOGENOM; CLU_072626_4_0_6; -.
DR OMA; RSCDTQF; -.
DR PhylomeDB; P67651; -.
DR BioCyc; SENT99287:STM4089-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0060698; F:endoribonuclease inhibitor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019899; F:enzyme binding; IEA:UniProtKB-UniRule.
DR GO; GO:0060702; P:negative regulation of endoribonuclease activity; IBA:GO_Central.
DR GO; GO:1902369; P:negative regulation of RNA catabolic process; IBA:GO_Central.
DR CDD; cd16841; RraA_family; 1.
DR HAMAP; MF_00471; RraA; 1.
DR InterPro; IPR010203; RraA.
DR InterPro; IPR005493; RraA/RraA-like.
DR InterPro; IPR036704; RraA/RraA-like_sf.
DR InterPro; IPR014339; RraA_gpbac.
DR Pfam; PF03737; RraA-like; 1.
DR SUPFAM; SSF89562; SSF89562; 1.
DR TIGRFAMs; TIGR01935; NOT-MenG; 1.
DR TIGRFAMs; TIGR02998; RraA_entero; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Reference proteome.
FT CHAIN 1..161
FT /note="Regulator of ribonuclease activity A"
FT /id="PRO_0000209635"
SQ SEQUENCE 161 AA; 17374 MW; FAD0D79978F2FC3B CRC64;
MKYDTSELCD IYQEDVNVVE PLFSNFGGRS SFGGQIITVK CFEDNGLLYD LLEQNGRGRV
LLVDGGGSVR RALVDAELAR LATQNEWEGL VIYGAVRQVD DLEELDIGIQ AIAAIPVGAA
GEGIGESDVR VNFGGVTFFS GDHLYADNTG IILSEDPLDI E