ID A0A1P8FKU5_9PROT Unreviewed; 342 AA.
AC A0A1P8FKU5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Peptide chain release factor 2 {ECO:0000256|HAMAP-Rule:MF_00094};
DE Short=RF-2 {ECO:0000256|HAMAP-Rule:MF_00094};
GN Name=prfB {ECO:0000256|HAMAP-Rule:MF_00094};
GN ORFNames=BWI17_14170 {ECO:0000313|EMBL:APV50732.1};
OS Betaproteobacteria bacterium GR16-43.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1904640 {ECO:0000313|EMBL:APV50732.1, ECO:0000313|Proteomes:UP000185830};
RN [1] {ECO:0000313|EMBL:APV50732.1, ECO:0000313|Proteomes:UP000185830}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GR16-43 {ECO:0000313|EMBL:APV50732.1,
RC ECO:0000313|Proteomes:UP000185830};
RA Choi A.;
RT "Complete genome sequence of betaproteobacterium GR16-43, isolated from a
RT freshwater pond in South Korea.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Peptide chain release factor 2 directs the termination of
CC translation in response to the peptide chain termination codons UGA and
CC UAA. {ECO:0000256|HAMAP-Rule:MF_00094}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00094}.
CC -!- PTM: Methylated by PrmC. Methylation increases the termination
CC efficiency of RF2. {ECO:0000256|HAMAP-Rule:MF_00094}.
CC -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC family. {ECO:0000256|ARBA:ARBA00010835, ECO:0000256|HAMAP-
CC Rule:MF_00094}.
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DR EMBL; CP019169; APV50732.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1P8FKU5; -.
DR STRING; 1904640.BWI17_14170; -.
DR KEGG; beba:BWI17_14170; -.
DR Proteomes; UP000185830; 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 Gene3D; 3.30.160.20; -; 1.
DR Gene3D; 3.30.70.1660; -; 1.
DR Gene3D; 1.20.58.410; Release factor; 1.
DR HAMAP; MF_00094; Rel_fac_2; 1.
DR InterPro; IPR005139; PCRF.
DR InterPro; IPR000352; Pep_chain_release_fac_I.
DR InterPro; IPR045853; Pep_chain_release_fac_I_sf.
DR InterPro; IPR004374; PrfB.
DR NCBIfam; TIGR00020; prfB; 1.
DR PANTHER; PTHR43116; PEPTIDE CHAIN RELEASE FACTOR 2; 1.
DR PANTHER; PTHR43116:SF3; RF_PROK_I DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF03462; PCRF; 1.
DR Pfam; PF00472; RF-1; 1.
DR SMART; SM00937; PCRF; 1.
DR SUPFAM; SSF75620; Release factor; 1.
DR PROSITE; PS00745; RF_PROK_I; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00094};
KW Methylation {ECO:0000256|ARBA:ARBA00022481, ECO:0000256|HAMAP-
KW Rule:MF_00094}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00094}.
FT DOMAIN 222..238
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT MOD_RES 229
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00094"
SQ SEQUENCE 342 AA; 38260 MW; 855B09E6624B6CDE CRC64;
MFDYDTKKQR LVEVGKALED PGVWNDSKRA QDLGKERSAL EATVNTLERV ESGLKDSAEL
FGLAKAEGDD DTLVSVRNDV NATGKLVEDL EFQRMFSHPM DPNNCFMDIN AGQGGTEAQD
WTAMLLRMYL KYCDKKGFKA EVLEESDGEV AGLKSASIKI SGAYAYGYLR TETGIHRLVR
KSPFDSNARR HTSFSAVFVY PEVDDTIEIE INPADLRIDT YRASGAGGQH VNKTDSAVRI
THLPTNIVVS SQNDRSQHRN RAEAFAMLKA KLYELELRKQ NDAKQKMEDA KTDIGWGHQI
RSYVLDQSRI KDLRTNHEVG NTQSVLDGDL DDFISASLKQ GV
//
