RRAA_ECO55
ID RRAA_ECO55 Reviewed; 161 AA.
AC B7LA26;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=Regulator of ribonuclease activity A {ECO:0000255|HAMAP-Rule:MF_00471};
GN Name=rraA {ECO:0000255|HAMAP-Rule:MF_00471};
GN OrderedLocusNames=EC55989_4407;
OS Escherichia coli (strain 55989 / EAEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585055;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=55989 / EAEC;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928145; CAV01131.1; -; Genomic_DNA.
DR RefSeq; WP_000872908.1; NC_011748.1.
DR AlphaFoldDB; B7LA26; -.
DR SMR; B7LA26; -.
DR EnsemblBacteria; CAV01131; CAV01131; EC55989_4407.
DR GeneID; 67417558; -.
DR KEGG; eck:EC55989_4407; -.
DR HOGENOM; CLU_072626_4_0_6; -.
DR OMA; RSCDTQF; -.
DR Proteomes; UP000000746; 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_1000135491"
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