RF1_STRMU
ID RF1_STRMU Reviewed; 359 AA.
AC Q8DU64;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 118.
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=SMU_1085;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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; AE014133; AAN58783.1; -; Genomic_DNA.
DR RefSeq; NP_721477.1; NC_004350.2.
DR RefSeq; WP_002262255.1; NC_004350.2.
DR PDB; 1ZBT; X-ray; 2.34 A; A=1-359.
DR PDBsum; 1ZBT; -.
DR AlphaFoldDB; Q8DU64; -.
DR SMR; Q8DU64; -.
DR STRING; 210007.SMU_1085; -.
DR PRIDE; Q8DU64; -.
DR DNASU; 1029399; -.
DR EnsemblBacteria; AAN58783; AAN58783; SMU_1085.
DR KEGG; smu:SMU_1085; -.
DR PATRIC; fig|210007.7.peg.972; -.
DR eggNOG; COG0216; Bacteria.
DR HOGENOM; CLU_036856_0_1_9; -.
DR OMA; ISDHRVG; -.
DR PhylomeDB; Q8DU64; -.
DR EvolutionaryTrace; Q8DU64; -.
DR Proteomes; UP000002512; Chromosome.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methylation; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..359
FT /note="Peptide chain release factor 1"
FT /id="PRO_0000177751"
FT MOD_RES 236
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
FT HELIX 3..16
FT /evidence="ECO:0007829|PDB:1ZBT"
FT HELIX 40..65
FT /evidence="ECO:0007829|PDB:1ZBT"
FT HELIX 75..99
FT /evidence="ECO:0007829|PDB:1ZBT"
FT TURN 100..102
FT /evidence="ECO:0007829|PDB:1ZBT"
FT TURN 107..110
FT /evidence="ECO:0007829|PDB:1ZBT"
FT STRAND 113..119
FT /evidence="ECO:0007829|PDB:1ZBT"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:1ZBT"
FT HELIX 124..144
FT /evidence="ECO:0007829|PDB:1ZBT"
FT STRAND 147..155
FT /evidence="ECO:0007829|PDB:1ZBT"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:1ZBT"
FT STRAND 161..170
FT /evidence="ECO:0007829|PDB:1ZBT"
FT HELIX 173..177
FT /evidence="ECO:0007829|PDB:1ZBT"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:1ZBT"
FT STRAND 182..188
FT /evidence="ECO:0007829|PDB:1ZBT"
FT STRAND 199..209
FT /evidence="ECO:0007829|PDB:1ZBT"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:1ZBT"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:1ZBT"
FT STRAND 223..228
FT /evidence="ECO:0007829|PDB:1ZBT"
FT STRAND 244..249
FT /evidence="ECO:0007829|PDB:1ZBT"
FT TURN 250..253
FT /evidence="ECO:0007829|PDB:1ZBT"
FT STRAND 254..258
FT /evidence="ECO:0007829|PDB:1ZBT"
FT STRAND 260..263
FT /evidence="ECO:0007829|PDB:1ZBT"
FT HELIX 264..290
FT /evidence="ECO:0007829|PDB:1ZBT"
FT STRAND 306..312
FT /evidence="ECO:0007829|PDB:1ZBT"
FT TURN 313..316
FT /evidence="ECO:0007829|PDB:1ZBT"
FT STRAND 317..320
FT /evidence="ECO:0007829|PDB:1ZBT"
FT TURN 321..324
FT /evidence="ECO:0007829|PDB:1ZBT"
FT STRAND 325..328
FT /evidence="ECO:0007829|PDB:1ZBT"
FT HELIX 330..334
FT /evidence="ECO:0007829|PDB:1ZBT"
FT HELIX 339..356
FT /evidence="ECO:0007829|PDB:1ZBT"
SQ SEQUENCE 359 AA; 40651 MW; 02F272F87858A1CC CRC64;
MNIYDQLQAV EDRYEELGEL LSDPDVVSDT KRFMELSREE ANSRETVAVY REYKQVVQNI
ADAQEMIKDA SGDPELEEMA KEELKNSKVA KEEYEEKLRF LLLPKDPNDD KNIILEIRGA
AGGDEAALFA GDLLNMYQKY AENQGWKFEV MEASANGVGG LKEVVAMVSG QSVYSKLKYE
SGAHRVQRVP VTESQGRVHT STATVLVMPE VEEVEYEIDP KDLRVDIYHA SGAGGQNVNK
VATAVRIIHL PTNIKVEMQE ERTQQKNRDK AMKIIRARVA DHFAQIAQDE QDAERKSTVG
TGDRSERIRT YNFPQNRVTD HRIGLTLQKL DSILSGKLDE VIDALILYDQ TQKLEELNK
