RRAB_CROTZ
ID RRAB_CROTZ Reviewed; 140 AA.
AC C9XUB3;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 2.
DT 25-MAY-2022, entry version 57.
DE RecName: Full=Regulator of ribonuclease activity B {ECO:0000255|HAMAP-Rule:MF_01888};
GN Name=rraB {ECO:0000255|HAMAP-Rule:MF_01888}; OrderedLocusNames=Ctu_04960;
OS Cronobacter turicensis (strain DSM 18703 / CCUG 55852 / LMG 23827 / z3032).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cronobacter.
OX NCBI_TaxID=693216;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18703 / CCUG 55852 / LMG 23827 / z3032;
RX PubMed=21037008; DOI=10.1128/jb.01162-10;
RA Stephan R., Lehner A., Tischler P., Rattei T.;
RT "Complete genome sequence of Cronobacter turicensis LMG 23827, a food-borne
RT pathogen causing deaths in neonates.";
RL J. Bacteriol. 193:309-310(2011).
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. {ECO:0000255|HAMAP-Rule:MF_01888}.
CC -!- SUBUNIT: Interacts with the C-terminal region of Rne.
CC {ECO:0000255|HAMAP-Rule:MF_01888}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01888}.
CC -!- SIMILARITY: Belongs to the RraB family. {ECO:0000255|HAMAP-
CC Rule:MF_01888}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CBA27575.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; FN543093; CBA27575.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041923131.1; NC_013282.2.
DR AlphaFoldDB; C9XUB3; -.
DR SMR; C9XUB3; -.
DR EnsemblBacteria; CBA27575; CBA27575; CTU_04960.
DR GeneID; 60372182; -.
DR KEGG; ctu:CTU_04960; -.
DR PATRIC; fig|693216.3.peg.475; -.
DR HOGENOM; CLU_128640_0_0_6; -.
DR Proteomes; UP000002069; 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 Gene3D; 3.30.70.970; -; 1.
DR HAMAP; MF_01888; RraB; 1.
DR InterPro; IPR016716; RraB.
DR InterPro; IPR036701; RraB-like_sf.
DR InterPro; IPR009671; RraB_dom.
DR Pfam; PF06877; RraB; 1.
DR PIRSF; PIRSF018193; UCP018193; 1.
DR SUPFAM; SSF89946; SSF89946; 1.
PE 3: Inferred from homology;
KW Cytoplasm.
FT CHAIN 1..140
FT /note="Regulator of ribonuclease activity B"
FT /id="PRO_0000404306"
FT REGION 113..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..133
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 140 AA; 15901 MW; ED6257FB8A6A2DC6 CRC64;
MANPELLEEQ REETRLIIEE LLEDGSDPEA LYTIEHHFSA DDFDTLEKLA VEVFKLGYEV
TDPEELELEE GGETVICCDA LSECALNAEL IDAQVEQLMN MAEKFNVEYD GWGTYFEDPD
GEGEDEDDEG MDEDDDGVRH