(data stored in ACNUC7421 zone)

SWISSPROT: RRAA_HISS2

ID   RRAA_HISS2              Reviewed;         166 AA.
AC   B0UV42;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   11-DEC-2019, entry version 70.
DE   RecName: Full=Regulator of ribonuclease activity A {ECO:0000255|HAMAP-Rule:MF_00471};
GN   Name=rraA {ECO:0000255|HAMAP-Rule:MF_00471}; OrderedLocusNames=HSM_0084;
OS   Histophilus somni (strain 2336) (Haemophilus somnus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Histophilus.
OX   NCBI_TaxID=228400;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2336;
RG   US DOE Joint Genome Institute;
RA   Siddaramappa S., Duncan A.J., Challacombe J.F., Rainey D., Gillaspy A.F.,
RA   Carson M., Gipson J., Gipson M., Bruce D., Detter J.C., Han C.S., Land M.,
RA   Tapia R., Thompson L.S., Orvis J., Zaitshik J., Barnes G., Brettin T.S.,
RA   Dyer D.W., Inzana T.J.;
RT   "Complete sequence of Haemophilus somnus 2336.";
RL   Submitted (FEB-2008) 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}.
DR   EMBL; CP000947; ACA32512.1; -; Genomic_DNA.
DR   RefSeq; WP_012341649.1; NC_010519.1.
DR   SMR; B0UV42; -.
DR   EnsemblBacteria; ACA32512; ACA32512; HSM_0084.
DR   GeneID; 31486361; -.
DR   KEGG; hsm:HSM_0084; -.
DR   HOGENOM; HOG000252803; -.
DR   KO; K02553; -.
DR   OMA; RSCDTQF; -.
DR   OrthoDB; 1614890at2; -.
DR   BioCyc; HSOM228400:G1GB8-87-MONOMER; -.
DR   Proteomes; UP000008543; 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;
DR   PRODOM; B0UV42.
DR   SWISS-2DPAGE; B0UV42.
KW   Cytoplasm; Reference proteome.
FT   CHAIN           1..166
FT                   /note="Regulator of ribonuclease activity A"
FT                   /id="PRO_1000081207"
SQ   SEQUENCE   166 AA;  18036 MW;  2A106D6EC31B68CE CRC64;
     MYIDTAELCD IYLDQIDVVE PIFSSFGGKS TFFGKITTIK CFENNGLISE ILEENGEGRV
     LLIDGGGAVR RALIDANLAQ LAADNGWEGI IVYGAIRQLQ QLENINIGIQ ALAPIPVGSD
     EQSIGETDVP VNFGGVTFFP DDYIYADLTG IILSQEPLDL EEFDSL
//

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