RF1_LACDB
ID RF1_LACDB Reviewed; 361 AA.
AC Q04BB3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Peptide chain release factor 1 {ECO:0000255|HAMAP-Rule:MF_00093};
DE Short=RF-1 {ECO:0000255|HAMAP-Rule:MF_00093};
GN Name=prfA {ECO:0000255|HAMAP-Rule:MF_00093}; OrderedLocusNames=LBUL_0633;
OS Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC BAA-365 / Lb-18).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=321956;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-365 / Lb-18;
RX PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT "Comparative genomics of the lactic acid bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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. {ECO:0000255|HAMAP-Rule:MF_00093}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00093}.
CC -!- PTM: Methylated by PrmC. Methylation increases the termination
CC efficiency of RF1. {ECO:0000255|HAMAP-Rule:MF_00093}.
CC -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC family. {ECO:0000255|HAMAP-Rule:MF_00093}.
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DR EMBL; CP000412; ABJ58259.1; -; Genomic_DNA.
DR RefSeq; WP_003617391.1; NC_008529.1.
DR AlphaFoldDB; Q04BB3; -.
DR SMR; Q04BB3; -.
DR GeneID; 66399658; -.
DR KEGG; lbu:LBUL_0633; -.
DR HOGENOM; CLU_036856_0_1_9; -.
DR OMA; ISDHRVG; -.
DR BioCyc; LDEL321956:LBUL_RS03010-MON; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016149; F:translation release factor activity, codon specific; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW Cytoplasm; Methylation; Protein biosynthesis.
FT CHAIN 1..361
FT /note="Peptide chain release factor 1"
FT /id="PRO_1000004902"
FT MOD_RES 236
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ SEQUENCE 361 AA; 41210 MW; 369ED0052F31B830 CRC64;
MDNVMAQLES LEVRYEEIQE MMADPEVIAD TKRYMEITKE EADMREVVQK FRKFKADKEE
IAGNKEIIAD GSDPELVEMA KMENSELEDE ISQLEDEIKI LMLPKDPNDD KDIIMEIRGA
AGGDEASLFA GDLLRMYEKY AENQGWNVSI VDSEQTEVGG YKRVAIMITG NKVYSKLKYE
NGAHRVQRIP VTESAGRVHT STATVAVMPE YEQVDIDLDP KEIRVDVYRS SGAGGQHINK
TSSAVRMTHL PTGIVVAMQD QRSQQQNRAK AMEILKSRVY DYYESQNRDK YDAKRKNAVG
TGDRSERIRT YNYPQNRVTD HRIGLTLNKL DRIMNGELDE VIDALTVYYQ TKQLEELAEN
A