RRAA_PECCP
ID RRAA_PECCP Reviewed; 161 AA.
AC C6DHM4;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Regulator of ribonuclease activity A {ECO:0000255|HAMAP-Rule:MF_00471};
GN Name=rraA {ECO:0000255|HAMAP-Rule:MF_00471}; OrderedLocusNames=PC1_0163;
OS Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=561230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC1;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Balakrishnan V., Glasner J., Perna N.T.;
RT "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL Submitted (JUL-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; CP001657; ACT11224.1; -; Genomic_DNA.
DR RefSeq; WP_010281528.1; NC_012917.1.
DR AlphaFoldDB; C6DHM4; -.
DR SMR; C6DHM4; -.
DR STRING; 561230.PC1_0163; -.
DR PRIDE; C6DHM4; -.
DR EnsemblBacteria; ACT11224; ACT11224; PC1_0163.
DR GeneID; 51387603; -.
DR GeneID; 57242477; -.
DR GeneID; 61346074; -.
DR KEGG; pct:PC1_0163; -.
DR eggNOG; COG0684; Bacteria.
DR HOGENOM; CLU_072626_4_0_6; -.
DR OMA; RSCDTQF; -.
DR OrthoDB; 1614890at2; -.
DR Proteomes; UP000002736; 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_1000206351"
SQ SEQUENCE 161 AA; 17314 MW; 8E1E209618182497 CRC64;
MKYDTSELCD IYHEEVNVVE PLFSNFGGRT SFGGKITTVK CFEDNGLLFD LLEENGLGRV
LLVDGGGSVR RALINAEIAR LATQNEWEGI VVYGAVRQVD DLAELDIGIQ AMAAIPVGAG
SEGIGESDIR VNFGGVTFFS GDHLYADNTG IILAEDPLDI E