ID   RRAA_VIBCH              Reviewed;         171 AA.
AC   Q9KNQ9;
DT   02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Regulator of ribonuclease activity A {ECO:0000255|HAMAP-Rule:MF_00471};
GN   Name=rraA {ECO:0000255|HAMAP-Rule:MF_00471}; OrderedLocusNames=VC_2672;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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; AE003852; AAF95813.1; -; Genomic_DNA.
DR   PIR; B82049; B82049.
DR   RefSeq; NP_232300.1; NC_002505.1.
DR   RefSeq; WP_000456236.1; NZ_LT906614.1.
DR   AlphaFoldDB; Q9KNQ9; -.
DR   SMR; Q9KNQ9; -.
DR   STRING; 243277.VC_2672; -.
DR   DNASU; 2615500; -.
DR   EnsemblBacteria; AAF95813; AAF95813; VC_2672.
DR   GeneID; 57741268; -.
DR   KEGG; vch:VC_2672; -.
DR   PATRIC; fig|243277.26.peg.2547; -.
DR   eggNOG; COG0684; Bacteria.
DR   HOGENOM; CLU_072626_4_0_6; -.
DR   OMA; RSCDTQF; -.
DR   BioCyc; VCHO:VC2672-MON; -.
DR   Proteomes; UP000000584; Chromosome 1.
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..171
FT                   /note="Regulator of ribonuclease activity A"
FT                   /id="PRO_0000209641"
SQ   SEQUENCE   171 AA;  18445 MW;  42559174CA872C75 CRC64;
     MEYNTSALCD IYLDQVDVVE PMFSNFGGCA SFAGQITTIK CYEDNGLIRE TLEQDGLGRI
     LLIDGGGSLR RALIDAELAA LAEENEWEGI VVYGSVREVD ELEEMSIGIQ AIASIPVGAT
     SQGIGEVDIP VNFGGVTFLP EDYLYADNTG IIISQEPLSA DLGEEEEDEL L