ID A0A4V6I646_9HELI Unreviewed; 367 AA.
AC A0A4V6I646;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
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 ECO:0000313|EMBL:TLE10802.1};
GN ORFNames=LS79_004615 {ECO:0000313|EMBL:TLE10802.1};
OS Helicobacter bilis.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=37372 {ECO:0000313|EMBL:TLE10802.1, ECO:0000313|Proteomes:UP000029857};
RN [1] {ECO:0000313|EMBL:TLE10802.1, ECO:0000313|Proteomes:UP000029857}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49320 {ECO:0000313|EMBL:TLE10802.1,
RC ECO:0000313|Proteomes:UP000029857};
RX PubMed=25428971;
RA Sheh A., Shen Z., Fox J.G.;
RT "Draft genome sequences of eight enterohepatic helicobacter species
RT isolated from both laboratory and wild rodents.";
RL Genome Announc. 2:e01218-e01214(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|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:TLE10802.1}.
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DR EMBL; JRPJ02000012; TLE10802.1; -; Genomic_DNA.
DR RefSeq; WP_034580083.1; NZ_JRPJ02000012.1.
DR AlphaFoldDB; A0A4V6I646; -.
DR Proteomes; UP000029857; 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}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00094}.
FT DOMAIN 244..260
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT COILED 62..115
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 251
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00094"
SQ SEQUENCE 367 AA; 41338 MW; 6123FE247DDA3150 CRC64;
MDSYEYGELL KTLQNKAQNI AKILNPDSLQ KRLDEINELE SHQEFWNDAK KAGEITKEKR
KCERILSTYA EMKAELDDAK ELFEIAESEG DSSTLELLFE NVESLQSHIQ KVEIEVMLSG
EFDSSNAIIT IQPGAGGTES QDWASMLYRM YLRWSERRGF KVELLDYQDG EEAGIKGAAF
IIKGENAYGY AKSENGVHRL VRISPFDANA KRHTSFASVQ VSPELSEDID IEILDKDIRI
DTYRASGAGG QHVNKTESAI RITHFPTGIV VQCQNDRSQH KNKATAMKML QSKLYELERL
KQSEGVANAE KSEIGWGHQI RSYVLAPYQQ VKDLRSNYAT SDTEGVLDGD IDDLIESVLV
LGENKGE
//