RRF_AQUAE
ID RRF_AQUAE Reviewed; 184 AA.
AC O66928;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Ribosome-recycling factor {ECO:0000255|HAMAP-Rule:MF_00040};
DE Short=RRF {ECO:0000255|HAMAP-Rule:MF_00040};
DE AltName: Full=Ribosome-releasing factor {ECO:0000255|HAMAP-Rule:MF_00040};
GN Name=frr {ECO:0000255|HAMAP-Rule:MF_00040}; OrderedLocusNames=aq_712;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
CC -!- FUNCTION: Responsible for the release of ribosomes from messenger RNA
CC at the termination of protein biosynthesis. May increase the efficiency
CC of translation by recycling ribosomes from one round of translation to
CC another. {ECO:0000255|HAMAP-Rule:MF_00040}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00040}.
CC -!- SIMILARITY: Belongs to the RRF family. {ECO:0000255|HAMAP-
CC Rule:MF_00040}.
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DR EMBL; AE000657; AAC06886.1; -; Genomic_DNA.
DR PIR; D70362; D70362.
DR RefSeq; NP_213488.1; NC_000918.1.
DR RefSeq; WP_010880426.1; NC_000918.1.
DR PDB; 1GE9; NMR; -; A=1-184.
DR PDBsum; 1GE9; -.
DR AlphaFoldDB; O66928; -.
DR SMR; O66928; -.
DR STRING; 224324.aq_712; -.
DR EnsemblBacteria; AAC06886; AAC06886; aq_712.
DR KEGG; aae:aq_712; -.
DR PATRIC; fig|224324.8.peg.570; -.
DR eggNOG; COG0233; Bacteria.
DR HOGENOM; CLU_073981_2_1_0; -.
DR InParanoid; O66928; -.
DR OMA; FNPMNNG; -.
DR OrthoDB; 1674344at2; -.
DR EvolutionaryTrace; O66928; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0043023; F:ribosomal large subunit binding; IBA:GO_Central.
DR GO; GO:0002184; P:cytoplasmic translational termination; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR CDD; cd00520; RRF; 1.
DR Gene3D; 1.10.132.20; -; 1.
DR HAMAP; MF_00040; RRF; 1.
DR InterPro; IPR002661; Ribosome_recyc_fac.
DR InterPro; IPR023584; Ribosome_recyc_fac_dom.
DR InterPro; IPR036191; RRF_sf.
DR PANTHER; PTHR20982; PTHR20982; 1.
DR Pfam; PF01765; RRF; 1.
DR SUPFAM; SSF55194; SSF55194; 1.
DR TIGRFAMs; TIGR00496; frr; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Protein biosynthesis; Reference proteome.
FT CHAIN 1..184
FT /note="Ribosome-recycling factor"
FT /id="PRO_0000167400"
FT HELIX 5..29
FT /evidence="ECO:0007829|PDB:1GE9"
FT TURN 37..39
FT /evidence="ECO:0007829|PDB:1GE9"
FT STRAND 45..49
FT /evidence="ECO:0007829|PDB:1GE9"
FT TURN 54..57
FT /evidence="ECO:0007829|PDB:1GE9"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:1GE9"
FT STRAND 63..71
FT /evidence="ECO:0007829|PDB:1GE9"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:1GE9"
FT HELIX 77..89
FT /evidence="ECO:0007829|PDB:1GE9"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:1GE9"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:1GE9"
FT HELIX 109..143
FT /evidence="ECO:0007829|PDB:1GE9"
FT HELIX 149..181
FT /evidence="ECO:0007829|PDB:1GE9"
SQ SEQUENCE 184 AA; 21494 MW; 7FADEBAB9B48498F CRC64;
MIKELEDIFK EAEKDMKKAV EYYKNEIAGL RTSRASTALV EEIKVEYYGS KVPIKQLGTI
SVPEHNQIVI QVWDQNAVPA IEKAIREELN LNPTVQGNVI RVTLPPLTEE RRRELVRLLH
KITEEARVRV RNVRREAKEM IEELEGISED EKKRALERLQ KLTDKYIDEI NKLMEAKEKE
IMSV