RRAA_ECOSE
ID RRAA_ECOSE Reviewed; 161 AA.
AC B6I4S2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Regulator of ribonuclease activity A {ECO:0000255|HAMAP-Rule:MF_00471};
GN Name=rraA {ECO:0000255|HAMAP-Rule:MF_00471}; OrderedLocusNames=ECSE_4218;
OS Escherichia coli (strain SE11).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=409438;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SE11;
RX PubMed=18931093; DOI=10.1093/dnares/dsn026;
RA Oshima K., Toh H., Ogura Y., Sasamoto H., Morita H., Park S.-H., Ooka T.,
RA Iyoda S., Taylor T.D., Hayashi T., Itoh K., Hattori M.;
RT "Complete genome sequence and comparative analysis of the wild-type
RT commensal Escherichia coli strain SE11 isolated from a healthy adult.";
RL DNA Res. 15:375-386(2008).
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; AP009240; BAG79742.1; -; Genomic_DNA.
DR RefSeq; WP_000872908.1; NC_011415.1.
DR AlphaFoldDB; B6I4S2; -.
DR SMR; B6I4S2; -.
DR EnsemblBacteria; BAG79742; BAG79742; ECSE_4218.
DR GeneID; 67417558; -.
DR KEGG; ecy:ECSE_4218; -.
DR HOGENOM; CLU_072626_4_0_6; -.
DR OMA; RSCDTQF; -.
DR Proteomes; UP000008199; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0060698; F:endoribonuclease inhibitor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019899; F:enzyme binding; IEA:UniProtKB-UniRule.
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.
FT CHAIN 1..161
FT /note="Regulator of ribonuclease activity A"
FT /id="PRO_1000194855"
SQ SEQUENCE 161 AA; 17360 MW; B30371B838DE21F8 CRC64;
MKYDTSELCD IYQEDVNVVE PLFSNFGGRA SFGGQIITVK CFEDNGLLYD LLEQNGRGRV
LVVDGGGSVR RALVDAELAR LAVQNEWEGL VIYGAVRQVD DLEELDIGIQ AMAAIPVGAA
GEGIGESDVR VNFGGVTFFS GDHLYADNTG IILSEDPLDI E