RRAA_ECOL6
ID RRAA_ECOL6 Reviewed; 161 AA.
AC P0A8R1; P32165;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Regulator of ribonuclease activity A {ECO:0000255|HAMAP-Rule:MF_00471};
GN Name=rraA {ECO:0000255|HAMAP-Rule:MF_00471}; Synonyms=menG;
GN OrderedLocusNames=c4881;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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; AE014075; AAN83309.1; -; Genomic_DNA.
DR RefSeq; WP_000872908.1; NC_004431.1.
DR AlphaFoldDB; P0A8R1; -.
DR SMR; P0A8R1; -.
DR STRING; 199310.c4881; -.
DR EnsemblBacteria; AAN83309; AAN83309; c4881.
DR GeneID; 67417558; -.
DR KEGG; ecc:c4881; -.
DR eggNOG; COG0684; Bacteria.
DR HOGENOM; CLU_072626_4_0_6; -.
DR OMA; RSCDTQF; -.
DR BioCyc; ECOL199310:C4881-MON; -.
DR Proteomes; UP000001410; 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_0000209612"
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