RRF_VIBPA
ID RRF_VIBPA Reviewed; 185 AA.
AC Q8GRF5;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 109.
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=VP2315;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND X-RAY CRYSTALLOGRAPHY (2.2
RP ANGSTROMS).
RX PubMed=12411440; DOI=10.1074/jbc.m208098200;
RA Nakano H., Yoshida T., Uchiyama S., Kawachi M., Matsuo H., Kato T.,
RA Ohshima A., Yamaichi Y., Honda T., Kato H., Yamagata Y., Ohkubo T.,
RA Kobayashi Y.;
RT "Structure and binding mode of a ribosome recycling factor (RRF) from
RT mesophilic bacterium.";
RL J. Biol. Chem. 278:3427-3436(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
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.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the RRF family. {ECO:0000255|HAMAP-
CC Rule:MF_00040}.
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DR EMBL; AB064319; BAC16794.1; -; Genomic_DNA.
DR EMBL; BA000031; BAC60578.1; -; Genomic_DNA.
DR RefSeq; NP_798694.1; NC_004603.1.
DR RefSeq; WP_005456723.1; NC_004603.1.
DR PDB; 1IS1; X-ray; 2.20 A; A=1-185.
DR PDBsum; 1IS1; -.
DR AlphaFoldDB; Q8GRF5; -.
DR SMR; Q8GRF5; -.
DR STRING; 223926.28807313; -.
DR EnsemblBacteria; BAC60578; BAC60578; BAC60578.
DR GeneID; 1189828; -.
DR KEGG; vpa:VP2315; -.
DR PATRIC; fig|223926.6.peg.2217; -.
DR eggNOG; COG0233; Bacteria.
DR HOGENOM; CLU_073981_2_1_6; -.
DR OMA; FNPMNNG; -.
DR EvolutionaryTrace; Q8GRF5; -.
DR Proteomes; UP000002493; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0006415; P:translational termination; IEA:UniProtKB-UniRule.
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..185
FT /note="Ribosome-recycling factor"
FT /id="PRO_0000167576"
FT HELIX 2..24
FT /evidence="ECO:0007829|PDB:1IS1"
FT HELIX 34..37
FT /evidence="ECO:0007829|PDB:1IS1"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:1IS1"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:1IS1"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:1IS1"
FT STRAND 55..61
FT /evidence="ECO:0007829|PDB:1IS1"
FT STRAND 64..71
FT /evidence="ECO:0007829|PDB:1IS1"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:1IS1"
FT HELIX 75..84
FT /evidence="ECO:0007829|PDB:1IS1"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:1IS1"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:1IS1"
FT HELIX 107..144
FT /evidence="ECO:0007829|PDB:1IS1"
FT HELIX 150..183
FT /evidence="ECO:0007829|PDB:1IS1"
SQ SEQUENCE 185 AA; 20603 MW; 42E505C1FD183D03 CRC64;
MINEIKKDAQ ERMDKSVEAL KNNLSKVRTG RAHPSLLSGI SVEYYGAATP LNQVANVVAE
DARTLAITVF DKELTQKVEK AIMMSDLGLN PMSAGTIIRV PLPPLTEERR KDLVKIVRGE
AEGGRVAVRN IRRDANNDLK ALLKDKEISE DEDRKAQEEI QKLTDVAVKK IDEVLAAKEK
ELMEV
