ID A0A448VNF7_9NEIS Unreviewed; 367 AA.
AC A0A448VNF7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
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:VEJ51293.1};
GN ORFNames=NCTC12742_01172 {ECO:0000313|EMBL:VEJ51293.1};
OS Neisseria weaveri.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=28091 {ECO:0000313|EMBL:VEJ51293.1, ECO:0000313|Proteomes:UP000272771};
RN [1] {ECO:0000313|EMBL:VEJ51293.1, ECO:0000313|Proteomes:UP000272771}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC12742 {ECO:0000313|EMBL:VEJ51293.1,
RC ECO:0000313|Proteomes:UP000272771};
RG Pathogen Informatics;
RL Submitted (DEC-2018) 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; LR134533; VEJ51293.1; -; Genomic_DNA.
DR RefSeq; WP_004284533.1; NZ_LT571436.1.
DR AlphaFoldDB; A0A448VNF7; -.
DR STRING; 28091.SAMEA3174300_01795; -.
DR KEGG; nwe:SAMEA3174300_1795; -.
DR OrthoDB; 9806673at2; -.
DR Proteomes; UP000272771; Chromosome 1.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000272771}.
FT DOMAIN 247..263
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT MOD_RES 254
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00094"
SQ SEQUENCE 367 AA; 41751 MW; C437FB78E8C28EAE CRC64;
MEAEVINQLN NTLTDLESRS REIRVYLDYD GKKDRLEEVV GLSEDPDLWN DPKKAQEIGK
ERKVLEGIVL TLDNIAAGID DNRELLEMVV EENDEEGFAA VQADIANLEK QMGELEFKRM
FNQPADVNNC FIDITAGAGG TEAEDWAGML YRMYLRYAER KGFKVEVLEE DEGDIAGINR
ATIKLEGEYA YGLLRTETGI HRLVRYSPFD SNNKRHTSFC SVFVYPEVDD SFEVEINPAD
LRIDTYRASG AGGQHINKTD SAVRITHNPT GIVVQCQNDR SQHRNRDEAM NMLKAKLFEL
EMRKRNEEKQ SLEDSKSDVG WGHQIRSYVF DQSRIKDLRT SYEVGNIKAV MDGDLDGFIE
ASLKQGV
//
