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RRAA_YERPE
ID   RRAA_YERPE              Reviewed;         161 AA.
AC   Q8ZJJ7; Q0WKJ5;
DT   06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 125.
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=YPO0103, y0292, YP_0105;
OS   Yersinia pestis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=632;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CO-92 / Biovar Orientalis;
RX   PubMed=11586360; DOI=10.1038/35097083;
RA   Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA   Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA   Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA   Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA   Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA   Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA   Stevens K., Whitehead S., Barrell B.G.;
RT   "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL   Nature 413:523-527(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KIM10+ / Biovar Mediaevalis;
RX   PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA   Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA   Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA   Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA   Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT   "Genome sequence of Yersinia pestis KIM.";
RL   J. Bacteriol. 184:4601-4611(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=91001 / Biovar Mediaevalis;
RX   PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA   Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA   Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA   Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA   Wang J., Huang P., Yang R.;
RT   "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT   avirulent to humans.";
RL   DNA Res. 11:179-197(2004).
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; AL590842; CAL18791.1; -; Genomic_DNA.
DR   EMBL; AE009952; AAM83884.1; -; Genomic_DNA.
DR   EMBL; AE017042; AAS60384.1; -; Genomic_DNA.
DR   PIR; AF0013; AF0013.
DR   RefSeq; WP_002208945.1; NZ_WUCM01000087.1.
DR   RefSeq; YP_002345193.1; NC_003143.1.
DR   AlphaFoldDB; Q8ZJJ7; -.
DR   SMR; Q8ZJJ7; -.
DR   IntAct; Q8ZJJ7; 3.
DR   STRING; 214092.YPO0103; -.
DR   PaxDb; Q8ZJJ7; -.
DR   DNASU; 1145239; -.
DR   EnsemblBacteria; AAM83884; AAM83884; y0292.
DR   EnsemblBacteria; AAS60384; AAS60384; YP_0105.
DR   GeneID; 66843512; -.
DR   KEGG; ype:YPO0103; -.
DR   KEGG; ypk:y0292; -.
DR   KEGG; ypm:YP_0105; -.
DR   PATRIC; fig|214092.21.peg.329; -.
DR   eggNOG; COG0684; Bacteria.
DR   HOGENOM; CLU_072626_4_0_6; -.
DR   OMA; RSCDTQF; -.
DR   Proteomes; UP000000815; Chromosome.
DR   Proteomes; UP000001019; Chromosome.
DR   Proteomes; UP000002490; Chromosome.
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..161
FT                   /note="Regulator of ribonuclease activity A"
FT                   /id="PRO_0000209650"
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
 
 
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