ID A0A0B0CZW3_9BACI Unreviewed; 328 AA.
AC A0A0B0CZW3;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=LD39_20335 {ECO:0000313|EMBL:KHE66897.1};
OS Halobacillus sp. BBL2006.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX NCBI_TaxID=1543706 {ECO:0000313|EMBL:KHE66897.1, ECO:0000313|Proteomes:UP000030879};
RN [1] {ECO:0000313|EMBL:KHE66897.1, ECO:0000313|Proteomes:UP000030879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BBL2006 {ECO:0000313|EMBL:KHE66897.1,
RC ECO:0000313|Proteomes:UP000030879};
RA Kirchner G., Treves D., Francis J.III.;
RT "Draft Genome Sequence of the Halophilic Bacterium Halobacillus sp. Strain
RT BBL2006.";
RL Submitted (SEP-2014) 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|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:KHE66897.1}.
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DR EMBL; JRNX01000844; KHE66897.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B0CZW3; -.
DR Proteomes; UP000030879; 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:UP000030879}.
FT DOMAIN 205..221
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT COILED 23..76
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 241..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 328 AA; 37647 MW; 7C59750489FEC337 CRC64;
MTAPGFWEDQ KTAQKVIDEV NGLKSLVHTL EEHEETHENL EVSYELVKEE EDEDLLVDLE
DQIQQLVKDL NQFELNILLS EPYDKNNAIL ELHPGAGGTE SQDWASMLLR MYTRWAEKKG
FKVETMDYLP GEEAGVKSVT LLIKGHNAYG YLKAEKGVHR LVRISPFDSS GRRHTSFVSC
EVMPEFNDEI EIDVRTEDLK IDTYRSSGAG GQHVNTTDSA VRITHTPTNT VVTCQSERSQ
IKNREQAMKM LKSKLYQLEI ERQQQELDDI RGEQKEIGWG SQIRSYVFHP YSMVKDHRTN
TEIGNTQGVM DGDLDKFINS YLRSQMDN
//
