ID   RRAA_PSET1              Reviewed;         165 AA.
AC   Q3IJD2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Regulator of ribonuclease activity A {ECO:0000255|HAMAP-Rule:MF_00471};
GN   Name=rraA {ECO:0000255|HAMAP-Rule:MF_00471}; OrderedLocusNames=PSHAa2734;
OS   Pseudoalteromonas translucida (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G., Ho C.,
RA   Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica bacterium
RT   Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
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; CR954246; CAI87782.1; -; Genomic_DNA.
DR   RefSeq; WP_011329377.1; NC_007481.1.
DR   AlphaFoldDB; Q3IJD2; -.
DR   SMR; Q3IJD2; -.
DR   STRING; 326442.PSHAa2734; -.
DR   EnsemblBacteria; CAI87782; CAI87782; PSHAa2734.
DR   KEGG; pha:PSHAa2734; -.
DR   eggNOG; COG0684; Bacteria.
DR   HOGENOM; CLU_072626_4_0_6; -.
DR   OMA; RSCDTQF; -.
DR   OrthoDB; 1614890at2; -.
DR   BioCyc; PHAL326442:PSHA_RS13445-MON; -.
DR   Proteomes; UP000006843; Chromosome I.
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; Reference proteome.
FT   CHAIN           1..165
FT                   /note="Regulator of ribonuclease activity A"
FT                   /id="PRO_1000013860"
SQ   SEQUENCE   165 AA;  17912 MW;  C3572FC11BC1FDE1 CRC64;
     MDYSTSDLCD HFADVVDVLE PMFINFGGRH SFGGRIKTVK CFENNELIRE LLSQDGTDLV
     LLIDGGGSTR RALIDIELAE LALENNWQGI IVYGAVRHVD EIEELDLGIQ AIASIPVAAD
     SQGAGEDGIG VNFAGVSFFD DDFIYADSTG IVLSAEELEL EIVEI