ID   RRAA_YERPN              Reviewed;         161 AA.
AC   Q1CD53; D1Q2A6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Regulator of ribonuclease activity A {ECO:0000255|HAMAP-Rule:MF_00471};
GN   Name=rraA {ECO:0000255|HAMAP-Rule:MF_00471}; OrderedLocusNames=YPN_3750;
GN   ORFNames=YP516_4265;
OS   Yersinia pestis bv. Antiqua (strain Nepal516).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=377628;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nepal516;
RX   PubMed=16740952; DOI=10.1128/jb.00124-06;
RA   Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M.,
RA   Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516:
RT   evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nepal516;
RA   Plunkett G. III, Anderson B.D., Baumler D.J., Burland V., Cabot E.L.,
RA   Glasner J.D., Mau B., Neeno-Eckwall E., Perna N.T., Munk A.C., Tapia R.,
RA   Green L.D., Rogers Y.C., Detter J.C., Bruce D.C., Brettin T.S.;
RT   "Yersinia pestis Nepal516A whole genome shotgun sequencing project.";
RL   Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
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; CP000305; ABG20077.1; -; Genomic_DNA.
DR   EMBL; ACNQ01000019; EEO74659.1; -; Genomic_DNA.
DR   RefSeq; WP_002208945.1; NZ_ACNQ01000019.1.
DR   AlphaFoldDB; Q1CD53; -.
DR   SMR; Q1CD53; -.
DR   EnsemblBacteria; ABG20077; ABG20077; YPN_3750.
DR   GeneID; 66843512; -.
DR   KEGG; ypn:YPN_3750; -.
DR   HOGENOM; CLU_072626_4_0_6; -.
DR   OMA; RSCDTQF; -.
DR   Proteomes; UP000008936; 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_1000013883"
SQ   SEQUENCE   161 AA;  17315 MW;  C325EF41BFEA938B CRC64;
     MKYDTSDLCD IYHEEVNVVE PLFSNFGGRT SFGGKITTVK CFEDNGLLFD LLEENGLGRV
     LVVDGGGSVR RALINAELAE LALKNEWEGI VVYGAVRQVD DLAELDIGIQ AMAAIPVGAA
     DEGVGESDIR VNFGGVTFFS GDHLYADNTG IILSEDPLDI E