ID A0A2G5K5W0_9RHOB Unreviewed; 374 AA.
AC A0A2G5K5W0;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 18-JUN-2025, entry version 24.
DE RecName: Full=Peptide chain release factor 2 {ECO:0000256|HAMAP-Rule:MF_00094, ECO:0000256|NCBIfam:TIGR00020};
DE Short=RF-2 {ECO:0000256|HAMAP-Rule:MF_00094};
GN Name=prfB {ECO:0000256|HAMAP-Rule:MF_00094};
GN ORFNames=BFP76_06360 {ECO:0000313|EMBL:PIB24795.1};
OS Paramylibacter kogurei.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Rhodobacterales; Paracoccaceae; Paramylibacter.
OX NCBI_TaxID=1889778 {ECO:0000313|EMBL:PIB24795.1, ECO:0000313|Proteomes:UP000231516};
RN [1] {ECO:0000313|EMBL:PIB24795.1, ECO:0000313|Proteomes:UP000231516}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4G11 {ECO:0000313|EMBL:PIB24795.1,
RC ECO:0000313|Proteomes:UP000231516};
RA Wong S.-K., Hamasaki K., Yoshizawa S.;
RT "Draft genome of Amylibacter sp. strain 4G11.";
RL Submitted (AUG-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}.
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:PIB24795.1}.
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DR EMBL; MDGM01000012; PIB24795.1; -; Genomic_DNA.
DR RefSeq; WP_099593462.1; NZ_MDGM01000012.1.
DR AlphaFoldDB; A0A2G5K5W0; -.
DR OrthoDB; 9806673at2; -.
DR Proteomes; UP000231516; 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 FunFam; 3.30.160.20:FF:000004; Peptide chain release factor 1; 1.
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:SF3; CLASS I PEPTIDE CHAIN RELEASE FACTOR; 1.
DR PANTHER; PTHR43116; PEPTIDE CHAIN RELEASE FACTOR 2; 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:UP000231516}.
FT DOMAIN 243..259
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT COILED 87..114
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 250
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00094"
SQ SEQUENCE 374 AA; 41720 MW; B3E03FBAC11795E6 CRC64;
MRAEIENLVG EINKSLELLK QRMDWDTAEY RMEEFNALSE NPDLWNDPAK AQKLMRERQM
LSDAIDGFKN LSQDLADNIE LIELGEMEDD QEVIDEAESA IRKVQKEAAK QEIAALLSGE
VDGNDTFLEI NAGAGGTESC DWASMLARMY VRWAEKQGYS VDEVAYNAGD EAGIKSVTYQ
IKGDNAYGWM KTESGVHRLV RISPFDSNAK RHTSFSSVWV YPVIDDNIEI EINPSDLRVD
TFRASGAGGQ HVNKTDSAVR MTHIPTGIVV QASAKSQHQN RATCMNALKS RLYEIELRKR
TEGIQEAHDN KGDAGWGNQI RSYVLQPYQM VKDLRTNVET SDSQGVLDGD LDQFMAAALA
LDVSGKTRAE AQEG
//
