AC   MF_00471;
DC   Protein; auto
TR   HAMAP; MF_00471; -; 1; level=0
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Names: RraA
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ID   RRAA
DE   RecName: Full=Regulator of ribonuclease activity A;
GN   Name=rraA;
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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.
CC   -!- SUBUNIT: Homotrimer. Binds to both RNA-binding sites in the C-terminal
CC       region of Rne and to RhlB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the RraA family.
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DR   Pfam; PF03737; Methyltransf_6; 1; trigger=no
DR   NCBIfam; TIGR01935; NOT-MenG; 1; trigger=no
DR   NCBIfam; TIGR02998; RraA_entero; 1; trigger=no
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KW   Cytoplasm
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GO   GO:0060698; F:endoribonuclease inhibitor activity
GO   GO:0019899; F:enzyme binding
GO   GO:0060699; P:regulation of endoribonuclease activity
GO   GO:0005737; C:cytoplasm
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FT   None
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Size: 157-173;
Related: None;
Template: P0A8R0;
Scope:
 Bacteria; Gammaproteobacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: Although it was initially thought to be a methyltransferase involved in
 the last step of the menaquinone pathway, it is not clustered with other
 enzymes of the menaquinone pathway in most bacteria, and does not have
 such enzymatic activity.
 Difficult to separate RRAA and RRAAH entries, but it seems that RRAA entries have
 [DN]-A-E at E.coli positions 75-77. RRAAH have G-[GD]. See PubMed:24359411
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# Revision 1.30 2023/06/01
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