RRF_ECOLI
ID RRF_ECOLI Reviewed; 185 AA.
AC P0A805; P16174;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 142.
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}; Synonyms=rrf;
GN OrderedLocusNames=b0172, JW0167;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=MRE-600;
RX PubMed=2684966; DOI=10.1016/s0021-9258(19)47217-7;
RA Ichikawa S., Kaji A.;
RT "Molecular cloning and expression of ribosome releasing factor.";
RL J. Biol. Chem. 264:20054-20059(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1447125; DOI=10.1128/jb.174.23.7517-7526.1992;
RA Yamanaka K., Ogura T., Niki H., Hiraga S.;
RT "Identification and characterization of the smbA gene, a suppressor of the
RT mukB null mutant of Escherichia coli.";
RL J. Bacteriol. 174:7517-7526(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8202364; DOI=10.1093/nar/22.9.1637;
RA Fujita N., Mori H., Yura T., Ishihama A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-
RT 4.1 min (110,917-193,643 bp) region.";
RL Nucleic Acids Res. 22:1637-1639(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T.,
RA Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S.,
RA Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 4.0
RT - 6.0 min (189,987 - 281,416bp) region.";
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [8]
RP PROTEIN SEQUENCE OF 1-12.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [9]
RP PROTEIN SEQUENCE OF 1-11.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Pasquali C., Sanchez J.-C., Ravier F., Golaz O., Hughes G.J., Frutiger S.,
RA Paquet N., Wilkins M., Appel R.D., Bairoch A., Hochstrasser D.F.;
RL Submitted (SEP-1994) to UniProtKB.
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-5.
RX PubMed=1860827; DOI=10.1128/jb.173.16.5181-5187.1991;
RA Shimizu I., Kaji A.;
RT "Identification of the promoter region of the ribosome-releasing factor
RT cistron (frr).";
RL J. Bacteriol. 173:5181-5187(1991).
RN [11]
RP CHARACTERIZATION.
RX PubMed=8183897; DOI=10.1073/pnas.91.10.4249;
RA Janosi L., Shimizu I., Kaji A.;
RT "Ribosome recycling factor (ribosome releasing factor) is essential for
RT bacterial growth.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:4249-4253(1994).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-162, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
RX PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200;
RA Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
RA Grishin N.V., Zhao Y.;
RT "Lysine acetylation is a highly abundant and evolutionarily conserved
RT modification in Escherichia coli.";
RL Mol. Cell. Proteomics 8:215-225(2009).
RN [13]
RP STRUCTURE BY ELECTRON MICROSCOPY (12.0 ANGSTROMS).
RX PubMed=15178758; DOI=10.1073/pnas.0401904101;
RA Agrawal R.K., Sharma M.R., Kiel M.C., Hirokawa G., Booth T.M., Spahn C.M.,
RA Grassucci R.A., Kaji A., Frank J.;
RT "Visualization of ribosome-recycling factor on the Escherichia coli 70S
RT ribosome: functional implications.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:8900-8905(2004).
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 -!- INTERACTION:
CC P0A805; P0AD49: raiA; NbExp=4; IntAct=EBI-1114349, EBI-1129692;
CC P0A805; P0A7J7: rplK; NbExp=2; IntAct=EBI-1114349, EBI-547288;
CC P0A805; P0A8E1: ycfP; NbExp=2; IntAct=EBI-1114349, EBI-9129402;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the RRF family. {ECO:0000255|HAMAP-
CC Rule:MF_00040}.
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DR EMBL; J05113; AAA24607.1; -; Genomic_DNA.
DR EMBL; D13334; BAA02599.1; -; Genomic_DNA.
DR EMBL; U70214; AAB08601.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73283.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96748.1; -; Genomic_DNA.
DR EMBL; M69029; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A34495; A34495.
DR RefSeq; NP_414714.1; NC_000913.3.
DR RefSeq; WP_000622418.1; NZ_STEB01000032.1.
DR PDB; 1EK8; X-ray; 2.30 A; A=1-185.
DR PDB; 1ISE; X-ray; 2.20 A; A=1-185.
DR PDB; 1Y69; X-ray; 3.33 A; 8=1-30, 8=106-185.
DR PDB; 1ZN0; EM; 15.50 A; A=1-185.
DR PDB; 1ZN1; EM; 14.10 A; A=1-185.
DR PDB; 2RDO; EM; 9.10 A; 8=1-185.
DR PDB; 4V9C; X-ray; 3.30 A; CY=1-185.
DR PDB; 4V9D; X-ray; 3.00 A; AY=2-183.
DR PDB; 4WOI; X-ray; 3.00 A; AV=1-185.
DR PDBsum; 1EK8; -.
DR PDBsum; 1ISE; -.
DR PDBsum; 1Y69; -.
DR PDBsum; 1ZN0; -.
DR PDBsum; 1ZN1; -.
DR PDBsum; 2RDO; -.
DR PDBsum; 4V9C; -.
DR PDBsum; 4V9D; -.
DR PDBsum; 4WOI; -.
DR AlphaFoldDB; P0A805; -.
DR SMR; P0A805; -.
DR BioGRID; 4259750; 60.
DR BioGRID; 850482; 31.
DR DIP; DIP-48120N; -.
DR IntAct; P0A805; 37.
DR STRING; 511145.b0172; -.
DR DrugBank; DB04082; Decyloxy-Methanol.
DR iPTMnet; P0A805; -.
DR SWISS-2DPAGE; P0A805; -.
DR jPOST; P0A805; -.
DR PaxDb; P0A805; -.
DR PRIDE; P0A805; -.
DR EnsemblBacteria; AAC73283; AAC73283; b0172.
DR EnsemblBacteria; BAB96748; BAB96748; BAB96748.
DR GeneID; 67416248; -.
DR GeneID; 946122; -.
DR KEGG; ecj:JW0167; -.
DR KEGG; eco:b0172; -.
DR PATRIC; fig|1411691.4.peg.2108; -.
DR EchoBASE; EB0331; -.
DR eggNOG; COG0233; Bacteria.
DR HOGENOM; CLU_073981_2_1_6; -.
DR InParanoid; P0A805; -.
DR OMA; FNPMNNG; -.
DR PhylomeDB; P0A805; -.
DR BioCyc; EcoCyc:EG10335-MON; -.
DR EvolutionaryTrace; P0A805; -.
DR PRO; PR:P0A805; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoCyc.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0043023; F:ribosomal large subunit binding; IDA:EcoCyc.
DR GO; GO:0002184; P:cytoplasmic translational termination; IDA:EcoCyc.
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; Acetylation; Cytoplasm; Direct protein sequencing;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..185
FT /note="Ribosome-recycling factor"
FT /id="PRO_0000167454"
FT MOD_RES 162
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00040,
FT ECO:0000269|PubMed:18723842"
FT HELIX 3..24
FT /evidence="ECO:0007829|PDB:1ISE"
FT HELIX 34..37
FT /evidence="ECO:0007829|PDB:1ISE"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:1ISE"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:1ISE"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:1ISE"
FT STRAND 55..61
FT /evidence="ECO:0007829|PDB:1ISE"
FT STRAND 64..71
FT /evidence="ECO:0007829|PDB:1ISE"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:1ISE"
FT HELIX 75..83
FT /evidence="ECO:0007829|PDB:1ISE"
FT STRAND 92..101
FT /evidence="ECO:0007829|PDB:1ISE"
FT HELIX 107..145
FT /evidence="ECO:0007829|PDB:1ISE"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:1ISE"
FT HELIX 150..184
FT /evidence="ECO:0007829|PDB:1ISE"
SQ SEQUENCE 185 AA; 20639 MW; CBFB9675AAD0CFD8 CRC64;
MISDIRKDAE VRMDKCVEAF KTQISKIRTG RASPSLLDGI VVEYYGTPTP LRQLASVTVE
DSRTLKINVF DRSMSPAVEK AIMASDLGLN PNSAGSDIRV PLPPLTEERR KDLTKIVRGE
AEQARVAVRN VRRDANDKVK ALLKDKEISE DDDRRSQDDV QKLTDAAIKK IEAALADKEA
ELMQF
