RF1_ECOLI
ID RF1_ECOLI Reviewed; 360 AA.
AC P0A7I0; P07011; P77340;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Peptide chain release factor RF1;
DE Short=RF-1;
GN Name=prfA; Synonyms=sueB, uar; OrderedLocusNames=b1211, JW1202;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3889910; DOI=10.1073/pnas.82.11.3616;
RA Craigen W.J., Cook R.G., Tate W.P., Caskey C.T.;
RT "Bacterial peptide chain release factors: conserved primary structure and
RT possible frameshift regulation of release factor 2.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:3616-3620(1985).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=3049538; DOI=10.1128/jb.170.10.4537-4541.1988;
RA Lee C.C., Kohara Y., Akiyama K., Smith C.L., Craigen W.J., Caskey C.T.;
RT "Rapid and precise mapping of the Escherichia coli release factor genes by
RT two physical approaches.";
RL J. Bacteriol. 170:4537-4541(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=7543480; DOI=10.1128/jb.177.15.4488-4500.1995;
RA Strohmaier H., Remler P., Renner W., Hoegenauer G.;
RT "Expression of genes kdsA and kdsB involved in 3-deoxy-D-manno-octulosonic
RT acid metabolism and biosynthesis of enterobacterial lipopolysaccharide is
RT growth phase regulated primarily at the transcriptional level in
RT Escherichia coli K-12.";
RL J. Bacteriol. 177:4488-4500(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-91.
RC STRAIN=K12;
RX PubMed=2684779; DOI=10.1016/0378-1119(89)90046-2;
RA Li J.-M., Russell C.S., Cosloy S.D.;
RT "Cloning and structure of the hem A gene of Escherichia coli K-12.";
RL Gene 82:209-217(1989).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
RC STRAIN=K12;
RX PubMed=2548996; DOI=10.1128/jb.171.9.4728-4735.1989;
RA Verkamp E., Chelm B.K.;
RT "Isolation, nucleotide sequence, and preliminary characterization of the
RT Escherichia coli K-12 hemA gene.";
RL J. Bacteriol. 171:4728-4735(1989).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 339-360.
RC STRAIN=K12;
RX PubMed=7883187; DOI=10.1016/0378-1119(94)00805-3;
RA Nakayashiki T., Nishimura K., Inokuchi H.;
RT "Cloning and sequencing of a previously unidentified gene that is involved
RT in the biosynthesis of heme in Escherichia coli.";
RL Gene 153:67-70(1995).
RN [10]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [11]
RP METHYLATION AT GLN-235.
RX PubMed=11118225; DOI=10.1093/emboj/19.24.6900;
RA Dincbas-Renqvist V., Engstroem A., Mora L., Heurgue-Hamard V.,
RA Buckingham R., Ehrenberg M.;
RT "A post-translational modification in the GGQ motif of RF2 from Escherichia
RT coli stimulates termination of translation.";
RL EMBO J. 19:6900-6907(2000).
RN [12]
RP METHYLATION AT GLN-235 BY PRMC, AND MUTAGENESIS OF GLN-235.
RC STRAIN=K12;
RX PubMed=11847124; DOI=10.1093/emboj/21.4.769;
RA Heurgue-Hamard V., Champ S., Engstroem A., Ehrenberg M., Buckingham R.H.;
RT "The hemK gene in Escherichia coli encodes the N(5)-glutamine
RT methyltransferase that modifies peptide release factors.";
RL EMBO J. 21:769-778(2002).
RN [13]
RP METHYLATION BY PRMC.
RC STRAIN=K12;
RX PubMed=11805295; DOI=10.1073/pnas.032488499;
RA Nakahigashi K., Kubo N., Narita S., Shimaoka T., Goto S., Oshima T.,
RA Mori H., Maeda M., Wada C., Inokuchi H.;
RT "HemK, a class of protein methyl transferase with similarity to DNA methyl
RT transferases, methylates polypeptide chain release factors, and hemK
RT knockout induces defects in translational termination.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:1473-1478(2002).
RN [14]
RP PTM, AND EFFECT OF METHYLATION.
RC STRAIN=K12;
RX PubMed=17932046; DOI=10.1074/jbc.m706076200;
RA Mora L., Heurgue-Hamard V., de Zamaroczy M., Kervestin S., Buckingham R.H.;
RT "Methylation of bacterial release factors RF1 and RF2 is required for
RT normal translation termination in vivo.";
RL J. Biol. Chem. 282:35638-35645(2007).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH METHYLTRANSFERASE
RP PRMC.
RX PubMed=16364916; DOI=10.1016/j.molcel.2005.10.025;
RA Graille M., Heurgue-Hamard V., Champ S., Mora L., Scrima N., Ulryck N.,
RA van Tilbeurgh H., Buckingham R.H.;
RT "Molecular basis for bacterial class I release factor methylation by
RT PrmC.";
RL Mol. Cell 20:917-927(2005).
CC -!- FUNCTION: Peptide chain release factor 1 directs the termination of
CC translation in response to the peptide chain termination codons UAG and
CC UAA.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- PTM: Methylated by PrmC. Methylation increases the termination
CC efficiency of RF1. {ECO:0000269|PubMed:11118225,
CC ECO:0000269|PubMed:11805295, ECO:0000269|PubMed:11847124}.
CC -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC family. {ECO:0000305}.
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DR EMBL; M11519; AAA24519.1; -; Genomic_DNA.
DR EMBL; U18555; AAC43437.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74295.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA36069.1; -; Genomic_DNA.
DR EMBL; M30785; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M25323; AAA23955.1; -; Genomic_DNA.
DR EMBL; D28567; BAA05914.1; -; Genomic_DNA.
DR PIR; H64867; FCECR1.
DR RefSeq; NP_415729.1; NC_000913.3.
DR RefSeq; WP_000804726.1; NZ_STEB01000023.1.
DR PDB; 2B3T; X-ray; 3.10 A; B=1-360.
DR PDB; 5J30; X-ray; 3.20 A; QY/XY=1-360.
DR PDB; 5J3C; X-ray; 3.04 A; QY/XY=1-360.
DR PDB; 5J4D; X-ray; 3.10 A; JA/OC=1-360.
DR PDB; 5O2R; EM; 3.40 A; v=110-351.
DR PDB; 6GWT; EM; 3.80 A; v=104-351.
DR PDB; 6GXM; EM; 3.80 A; v=104-351.
DR PDB; 6GXN; EM; 3.90 A; v=2-351.
DR PDB; 6GXO; EM; 3.90 A; v=104-351.
DR PDB; 6ORL; EM; 3.50 A; A=100-356.
DR PDBsum; 2B3T; -.
DR PDBsum; 5J30; -.
DR PDBsum; 5J3C; -.
DR PDBsum; 5J4D; -.
DR PDBsum; 5O2R; -.
DR PDBsum; 6GWT; -.
DR PDBsum; 6GXM; -.
DR PDBsum; 6GXN; -.
DR PDBsum; 6GXO; -.
DR PDBsum; 6ORL; -.
DR AlphaFoldDB; P0A7I0; -.
DR SMR; P0A7I0; -.
DR BioGRID; 4260107; 60.
DR DIP; DIP-35936N; -.
DR IntAct; P0A7I0; 13.
DR STRING; 511145.b1211; -.
DR iPTMnet; P0A7I0; -.
DR jPOST; P0A7I0; -.
DR PaxDb; P0A7I0; -.
DR PRIDE; P0A7I0; -.
DR EnsemblBacteria; AAC74295; AAC74295; b1211.
DR EnsemblBacteria; BAA36069; BAA36069; BAA36069.
DR GeneID; 66674969; -.
DR GeneID; 949002; -.
DR KEGG; ecj:JW1202; -.
DR KEGG; eco:b1211; -.
DR PATRIC; fig|1411691.4.peg.1073; -.
DR EchoBASE; EB0754; -.
DR eggNOG; COG0216; Bacteria.
DR HOGENOM; CLU_036856_0_1_6; -.
DR InParanoid; P0A7I0; -.
DR OMA; ISDHRVG; -.
DR PhylomeDB; P0A7I0; -.
DR BioCyc; EcoCyc:EG10761-MON; -.
DR EvolutionaryTrace; P0A7I0; -.
DR PRO; PR:P0A7I0; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0043022; F:ribosome binding; IDA:EcoCyc.
DR GO; GO:0016149; F:translation release factor activity, codon specific; IDA:EcoCyc.
DR GO; GO:0006415; P:translational termination; IMP:EcoCyc.
DR HAMAP; MF_00093; Rel_fac_1; 1.
DR InterPro; IPR005139; PCRF.
DR InterPro; IPR000352; Pep_chain_release_fac_I.
DR InterPro; IPR045853; Pep_chain_release_fac_I_sf.
DR InterPro; IPR004373; RF-1.
DR Pfam; PF03462; PCRF; 1.
DR Pfam; PF00472; RF-1; 1.
DR SMART; SM00937; PCRF; 1.
DR SUPFAM; SSF75620; SSF75620; 1.
DR TIGRFAMs; TIGR00019; prfA; 1.
DR PROSITE; PS00745; RF_PROK_I; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methylation; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..360
FT /note="Peptide chain release factor RF1"
FT /id="PRO_0000177668"
FT REGION 284..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 235
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000269|PubMed:11118225,
FT ECO:0000269|PubMed:11847124"
FT MUTAGEN 235
FT /note="Q->E,A: Loss of methylation."
FT /evidence="ECO:0000269|PubMed:11847124"
FT CONFLICT 72..91
FT /note="PEMREMAQDELREAKEKSEQ -> LRYLLYLRLFVVLFRHVVGD (in
FT Ref. 7; M30785)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="D -> E (in Ref. 3; AAC43437)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="D -> G (in Ref. 1; AAA24519)"
FT /evidence="ECO:0000305"
FT HELIX 10..26
FT /evidence="ECO:0007829|PDB:2B3T"
FT HELIX 35..55
FT /evidence="ECO:0007829|PDB:2B3T"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:2B3T"
FT STRAND 111..117
FT /evidence="ECO:0007829|PDB:2B3T"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:2B3T"
FT HELIX 122..141
FT /evidence="ECO:0007829|PDB:2B3T"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:2B3T"
FT STRAND 157..166
FT /evidence="ECO:0007829|PDB:2B3T"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:2B3T"
FT HELIX 172..175
FT /evidence="ECO:0007829|PDB:2B3T"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:2B3T"
FT STRAND 180..186
FT /evidence="ECO:0007829|PDB:2B3T"
FT STRAND 197..204
FT /evidence="ECO:0007829|PDB:2B3T"
FT TURN 211..213
FT /evidence="ECO:0007829|PDB:2B3T"
FT STRAND 219..226
FT /evidence="ECO:0007829|PDB:2B3T"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:2B3T"
FT STRAND 240..248
FT /evidence="ECO:0007829|PDB:2B3T"
FT TURN 249..251
FT /evidence="ECO:0007829|PDB:2B3T"
FT STRAND 254..261
FT /evidence="ECO:0007829|PDB:2B3T"
FT HELIX 263..278
FT /evidence="ECO:0007829|PDB:2B3T"
FT TURN 279..284
FT /evidence="ECO:0007829|PDB:2B3T"
FT STRAND 306..311
FT /evidence="ECO:0007829|PDB:2B3T"
FT TURN 312..315
FT /evidence="ECO:0007829|PDB:2B3T"
FT STRAND 316..319
FT /evidence="ECO:0007829|PDB:2B3T"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:2B3T"
FT STRAND 324..327
FT /evidence="ECO:0007829|PDB:2B3T"
FT HELIX 329..334
FT /evidence="ECO:0007829|PDB:2B3T"
FT HELIX 338..352
FT /evidence="ECO:0007829|PDB:2B3T"
SQ SEQUENCE 360 AA; 40517 MW; 47B3B77705A71954 CRC64;
MKPSIVAKLE ALHERHEEVQ ALLGDAQTIA DQERFRALSR EYAQLSDVSR CFTDWQQVQE
DIETAQMMLD DPEMREMAQD ELREAKEKSE QLEQQLQVLL LPKDPDDERN AFLEVRAGTG
GDEAALFAGD LFRMYSRYAE ARRWRVEIMS ASEGEHGGYK EIIAKISGDG VYGRLKFESG
GHRVQRVPAT ESQGRIHTSA CTVAVMPELP DAELPDINPA DLRIDTFRSS GAGGQHVNTT
DSAIRITHLP TGIVVECQDE RSQHKNKAKA LSVLGARIHA AEMAKRQQAE ASTRRNLLGS
GDRSDRNRTY NFPQGRVTDH RINLTLYRLD EVMEGKLDML IEPIIQEHQA DQLAALSEQE
