ID A0A061P9R5_9BACL Unreviewed; 329 AA.
AC A0A061P9R5;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Peptide chain release factor 2 {ECO:0000256|ARBA:ARBA00019192, 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=JCM19039_1359 {ECO:0000313|EMBL:GAK11651.1};
OS Geomicrobium sp. JCM 19039.
OC Bacteria; Bacillota; Bacilli; Bacillales; Geomicrobium.
OX NCBI_TaxID=1460636 {ECO:0000313|EMBL:GAK11651.1, ECO:0000313|Proteomes:UP000027177};
RN [1] {ECO:0000313|EMBL:GAK11651.1, ECO:0000313|Proteomes:UP000027177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 19039 {ECO:0000313|EMBL:GAK11651.1,
RC ECO:0000313|Proteomes:UP000027177};
RA Kudo T., Nakahara T., Zhang X., Taniyama S., Arakawa O., Murase S.,
RA Nakata H., Oshima K., Suda W., Kitamura K., Iida T., Oshida Y., Inoue T.,
RA Hongoh Y., Hattori M., Ohkuma M.;
RT "Draft Genome Sequences of Geomicrobium sp. Strains JCM 19037, JCM 19038,
RT JCM 19039, and JCM 19055, Isolated from Aquatic Samples.";
RL Genome Announc. 2:e00622-14(2014).
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|ARBA:ARBA00002613, 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAK11651.1}.
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DR EMBL; BAXB01000004; GAK11651.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061P9R5; -.
DR Proteomes; UP000027177; Unassembled WGS sequence.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00094};
KW Methylation {ECO:0000256|ARBA:ARBA00022481, ECO:0000256|HAMAP-
KW Rule:MF_00094};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00094}; Reference proteome {ECO:0000313|Proteomes:UP000027177}.
FT DOMAIN 205..221
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT COILED 30..76
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 234..273
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 212
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00094"
SQ SEQUENCE 329 AA; 37613 MW; 0AFCF0FF72F34BBE CRC64;
MTEPGFWDDQ NESKKVIDES NGLKEITVTF SELAEELENQ EVSYELLQEE EDDDLQQDLE
KSLKLLGERI NQFELQMLLS EPHDRKNAIL ELHPGAGGTE SQDWAEMLLR MYTRWAEKRK
FSVETMDYLP GDEAGVKSVT LLIKGLNAYG YLKAEKGVHR LVRISPFDSS GRRHTSFVSC
DVMPEMDDDV AVDINTEDLK IDTYRASGAG GQHVNTTDSA VRITHLPTNT VVQCQNERSQ
IKNREQAMKM LKARLYQLEI EKQQKEIDEL RGDQGDIGWG NQIRSYVFHP YNMVKDHRTN
FEVGNTGGVM DGGIDPFIDE YLRSTLENK
//
