RF3_ECOLI
ID RF3_ECOLI Reviewed; 529 AA.
AC P0A7I4; P33998; Q2M5U3;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Peptide chain release factor RF3;
DE Short=RF-3;
GN Name=prfC; Synonyms=miaD, tos; OrderedLocusNames=b4375, JW5873;
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 PROTEIN SEQUENCE OF 2-10.
RC STRAIN=K12;
RX PubMed=8016068; DOI=10.1073/pnas.91.13.5798;
RA Mikuni O., Ito K., Mofatt J., Matsumura K., McCaughan K., Nobukuni T.,
RA Tate W., Nakamura Y.;
RT "Identification of the prfC gene, which encodes peptide-chain-release
RT factor 3 of Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:5798-5802(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-13.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8016077; DOI=10.1073/pnas.91.13.5848;
RA Grentzmann G., Brechemier-Baey D., Heurgue V., Mora L., Buckingham R.H.;
RT "Localization and characterization of the gene encoding release factor RF3
RT in Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:5848-5852(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [4]
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 [5]
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 [6]
RP PROTEIN SEQUENCE OF 2-19.
RX PubMed=8575429; DOI=10.1111/j.1432-1033.1995.732_a.x;
RA Mortensen K.K., Hansen H.F., Grentzmann G., Buckingham R.H.,
RA Sperling-Petersen H.U.;
RT "Osmo-expression and fast two-step purification of Escherichia coli
RT translation termination factor RF-3.";
RL Eur. J. Biochem. 234:732-736(1995).
RN [7]
RP CHARACTERIZATION.
RX PubMed=7737996; DOI=10.1074/jbc.270.18.10595;
RA Grentzmann G., Brechemier-Baey D., Heurgue-Hamard V., Buckingham R.H.;
RT "Function of polypeptide chain release factor RF-3 in Escherichia coli. RF-
RT 3 action in termination is predominantly at UGA-containing stop signals.";
RL J. Biol. Chem. 270:10595-10600(1995).
CC -!- FUNCTION: Increases the formation of ribosomal termination complexes
CC and stimulates activities of RF-1 and RF-2. It binds guanine
CC nucleotides and has strong preference for UGA stop codons. It may
CC interact directly with the ribosome. The stimulation of RF-1 and RF-2
CC is significantly reduced by GTP and GDP, but not by GMP.
CC -!- INTERACTION:
CC P0A7I4; P0A796: pfkA; NbExp=2; IntAct=EBI-556252, EBI-554405;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. PrfC subfamily.
CC {ECO:0000305}.
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DR EMBL; D17724; BAA04578.1; -; Genomic_DNA.
DR EMBL; Z26313; CAA81223.1; -; Genomic_DNA.
DR EMBL; U14003; AAA97271.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77328.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78363.1; -; Genomic_DNA.
DR PIR; I59305; I59305.
DR RefSeq; NP_418792.1; NC_000913.3.
DR RefSeq; WP_000175940.1; NZ_SSUV01000012.1.
DR PDB; 2H5E; X-ray; 2.80 A; A/B=1-529.
DR PDB; 2O0F; EM; 15.50 A; A=1-529.
DR PDB; 4V85; X-ray; 3.20 A; AW=1-529.
DR PDB; 4V89; X-ray; 3.70 A; AW=1-529.
DR PDB; 4V8O; X-ray; 3.80 A; AY=1-529.
DR PDB; 6GXM; EM; 3.80 A; w=1-529.
DR PDB; 6GXN; EM; 3.90 A; w=1-529.
DR PDB; 6GXO; EM; 3.90 A; w=1-529.
DR PDB; 6GXP; EM; 4.40 A; w=1-529.
DR PDBsum; 2H5E; -.
DR PDBsum; 2O0F; -.
DR PDBsum; 4V85; -.
DR PDBsum; 4V89; -.
DR PDBsum; 4V8O; -.
DR PDBsum; 6GXM; -.
DR PDBsum; 6GXN; -.
DR PDBsum; 6GXO; -.
DR PDBsum; 6GXP; -.
DR AlphaFoldDB; P0A7I4; -.
DR SMR; P0A7I4; -.
DR BioGRID; 4260996; 56.
DR BioGRID; 853174; 1.
DR DIP; DIP-39402N; -.
DR IntAct; P0A7I4; 5.
DR STRING; 511145.b4375; -.
DR jPOST; P0A7I4; -.
DR PaxDb; P0A7I4; -.
DR PRIDE; P0A7I4; -.
DR EnsemblBacteria; AAC77328; AAC77328; b4375.
DR EnsemblBacteria; BAE78363; BAE78363; BAE78363.
DR GeneID; 60903174; -.
DR GeneID; 948897; -.
DR KEGG; ecj:JW5873; -.
DR KEGG; eco:b4375; -.
DR PATRIC; fig|1411691.4.peg.2313; -.
DR EchoBASE; EB2037; -.
DR eggNOG; COG4108; Bacteria.
DR HOGENOM; CLU_002794_2_1_6; -.
DR InParanoid; P0A7I4; -.
DR OMA; GFVFKIH; -.
DR PhylomeDB; P0A7I4; -.
DR BioCyc; EcoCyc:EG12114-MON; -.
DR EvolutionaryTrace; P0A7I4; -.
DR PRO; PR:P0A7I4; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0019003; F:GDP binding; IDA:EcoCyc.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IDA:EcoCyc.
DR GO; GO:0097216; F:guanosine tetraphosphate binding; IDA:EcoCyc.
DR GO; GO:0016150; F:translation release factor activity, codon nonspecific; IDA:EcoCyc.
DR GO; GO:0016149; F:translation release factor activity, codon specific; IEA:UniProtKB-UniRule.
DR GO; GO:0006449; P:regulation of translational termination; IEA:UniProtKB-UniRule.
DR GO; GO:0006415; P:translational termination; IDA:EcoCyc.
DR CDD; cd04169; RF3; 1.
DR Gene3D; 3.30.70.3280; -; 1.
DR Gene3D; 3.40.50.300; -; 3.
DR HAMAP; MF_00072; Rel_fac_3; 1.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004548; PrfC.
DR InterPro; IPR032090; RF3_C.
DR InterPro; IPR038467; RF3_dom_3_sf.
DR InterPro; IPR041732; RF3_GTP-bd.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR PANTHER; PTHR43556; PTHR43556; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF16658; RF3_C; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54980; SSF54980; 1.
DR TIGRFAMs; TIGR00503; prfC; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; GTP-binding;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8016068,
FT ECO:0000269|PubMed:8016077, ECO:0000269|PubMed:8575429"
FT CHAIN 2..529
FT /note="Peptide chain release factor RF3"
FT /id="PRO_0000210938"
FT DOMAIN 11..280
FT /note="tr-type G"
FT BINDING 20..27
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 88..92
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 142..145
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT CONFLICT 315
FT /note="V -> L (in Ref. 2; CAA81223)"
FT /evidence="ECO:0000305"
FT HELIX 6..11
FT /evidence="ECO:0007829|PDB:2H5E"
FT STRAND 13..20
FT /evidence="ECO:0007829|PDB:2H5E"
FT HELIX 26..35
FT /evidence="ECO:0007829|PDB:2H5E"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:2H5E"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:2H5E"
FT HELIX 97..101
FT /evidence="ECO:0007829|PDB:2H5E"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:2H5E"
FT STRAND 107..114
FT /evidence="ECO:0007829|PDB:2H5E"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:2H5E"
FT HELIX 121..130
FT /evidence="ECO:0007829|PDB:2H5E"
FT TURN 131..134
FT /evidence="ECO:0007829|PDB:2H5E"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:2H5E"
FT HELIX 151..162
FT /evidence="ECO:0007829|PDB:2H5E"
FT STRAND 165..174
FT /evidence="ECO:0007829|PDB:2H5E"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:2H5E"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:2H5E"
FT TURN 185..188
FT /evidence="ECO:0007829|PDB:2H5E"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:2H5E"
FT HELIX 213..219
FT /evidence="ECO:0007829|PDB:2H5E"
FT HELIX 221..237
FT /evidence="ECO:0007829|PDB:2H5E"
FT HELIX 243..247
FT /evidence="ECO:0007829|PDB:2H5E"
FT STRAND 250..256
FT /evidence="ECO:0007829|PDB:2H5E"
FT TURN 259..262
FT /evidence="ECO:0007829|PDB:2H5E"
FT HELIX 265..275
FT /evidence="ECO:0007829|PDB:2H5E"
FT STRAND 282..286
FT /evidence="ECO:0007829|PDB:2H5E"
FT STRAND 297..303
FT /evidence="ECO:0007829|PDB:2H5E"
FT STRAND 309..312
FT /evidence="ECO:0007829|PDB:2H5E"
FT STRAND 316..323
FT /evidence="ECO:0007829|PDB:2H5E"
FT STRAND 330..333
FT /evidence="ECO:0007829|PDB:2H5E"
FT TURN 334..336
FT /evidence="ECO:0007829|PDB:2H5E"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:2H5E"
FT STRAND 364..367
FT /evidence="ECO:0007829|PDB:2H5E"
FT STRAND 378..382
FT /evidence="ECO:0007829|PDB:2H5E"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:2H5E"
FT STRAND 396..404
FT /evidence="ECO:0007829|PDB:2H5E"
FT HELIX 412..421
FT /evidence="ECO:0007829|PDB:2H5E"
FT STRAND 426..430
FT /evidence="ECO:0007829|PDB:2H5E"
FT STRAND 436..442
FT /evidence="ECO:0007829|PDB:2H5E"
FT HELIX 444..456
FT /evidence="ECO:0007829|PDB:2H5E"
FT STRAND 461..464
FT /evidence="ECO:0007829|PDB:2H5E"
FT STRAND 469..475
FT /evidence="ECO:0007829|PDB:2H5E"
FT HELIX 479..488
FT /evidence="ECO:0007829|PDB:2H5E"
FT HELIX 490..492
FT /evidence="ECO:0007829|PDB:2H5E"
FT STRAND 493..495
FT /evidence="ECO:0007829|PDB:2H5E"
FT STRAND 501..507
FT /evidence="ECO:0007829|PDB:2H5E"
FT HELIX 508..517
FT /evidence="ECO:0007829|PDB:2H5E"
FT STRAND 521..528
FT /evidence="ECO:0007829|PDB:2H5E"
SQ SEQUENCE 529 AA; 59574 MW; 2A1E6AE984C6B1C6 CRC64;
MTLSPYLQEV AKRRTFAIIS HPDAGKTTIT EKVLLFGQAI QTAGTVKGRG SNQHAKSDWM
EMEKQRGISI TTSVMQFPYH DCLVNLLDTP GHEDFSEDTY RTLTAVDCCL MVIDAAKGVE
DRTRKLMEVT RLRDTPILTF MNKLDRDIRD PMELLDEVEN ELKIGCAPIT WPIGCGKLFK
GVYHLYKDET YLYQSGKGHT IQEVRIVKGL NNPDLDAAVG EDLAQQLRDE LELVKGASNE
FDKELFLAGE ITPVFFGTAL GNFGVDHMLD GLVEWAPAPM PRQTDTRTVE ASEDKFTGFV
FKIQANMDPK HRDRVAFMRV VSGKYEKGMK LRQVRTAKDV VISDALTFMA GDRSHVEEAY
PGDILGLHNH GTIQIGDTFT QGEMMKFTGI PNFAPELFRR IRLKDPLKQK QLLKGLVQLS
EEGAVQVFRP ISNNDLIVGA VGVLQFDVVV ARLKSEYNVE AVYESVNVAT ARWVECADAK
KFEEFKRKNE SQLALDGGDN LAYIATSMVN LRLAQERYPD VQFHQTREH
