ID   RF2_ACHLI               Reviewed;         365 AA.
AC   A9NF23;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Peptide chain release factor 2 {ECO:0000255|HAMAP-Rule:MF_00094};
DE            Short=RF-2 {ECO:0000255|HAMAP-Rule:MF_00094};
GN   Name=prfB {ECO:0000255|HAMAP-Rule:MF_00094}; OrderedLocusNames=ACL_0331;
OS   Acholeplasma laidlawii (strain PG-8A).
OC   Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC   Acholeplasma.
OX   NCBI_TaxID=441768;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PG-8A;
RX   PubMed=21784942; DOI=10.1128/jb.05059-11;
RA   Lazarev V.N., Levitskii S.A., Basovskii Y.I., Chukin M.M., Akopian T.A.,
RA   Vereshchagin V.V., Kostrjukova E.S., Kovaleva G.Y., Kazanov M.D.,
RA   Malko D.B., Vitreschak A.G., Sernova N.V., Gelfand M.S., Demina I.A.,
RA   Serebryakova M.V., Galyamina M.A., Vtyurin N.N., Rogov S.I., Alexeev D.G.,
RA   Ladygina V.G., Govorun V.M.;
RT   "Complete genome and proteome of Acholeplasma laidlawii.";
RL   J. Bacteriol. 193:4943-4953(2011).
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:0000255|HAMAP-Rule:MF_00094}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00094}.
CC   -!- PTM: Methylated by PrmC. Methylation increases the termination
CC       efficiency of RF2. {ECO:0000255|HAMAP-Rule:MF_00094}.
CC   -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC       family. {ECO:0000255|HAMAP-Rule:MF_00094}.
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DR   EMBL; CP000896; ABX80953.1; -; Genomic_DNA.
DR   RefSeq; WP_012242284.1; NC_010163.1.
DR   AlphaFoldDB; A9NF23; -.
DR   SMR; A9NF23; -.
DR   STRING; 441768.ACL_0331; -.
DR   EnsemblBacteria; ABX80953; ABX80953; ACL_0331.
DR   GeneID; 66293327; -.
DR   KEGG; acl:ACL_0331; -.
DR   eggNOG; COG1186; Bacteria.
DR   HOGENOM; CLU_036856_6_0_14; -.
DR   OMA; YVFHPYQ; -.
DR   OrthoDB; 928964at2; -.
DR   Proteomes; UP000008558; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016149; F:translation release factor activity, codon specific; IEA:UniProtKB-UniRule.
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   Pfam; PF03462; PCRF; 1.
DR   Pfam; PF00472; RF-1; 1.
DR   SMART; SM00937; PCRF; 1.
DR   SUPFAM; SSF75620; SSF75620; 1.
DR   TIGRFAMs; TIGR00020; prfB; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methylation; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..365
FT                   /note="Peptide chain release factor 2"
FT                   /id="PRO_1000075522"
FT   MOD_RES         249
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00094"
SQ   SEQUENCE   365 AA;  41587 MW;  43F43F321EE4F7D5 CRC64;
     MEKYEVNKTL ELFETKIKDL ENALDLDAIN NRLKEIEPIM ANPNFWNDSN QAKKISQELN
     QLTEKKQTIT SIQNQYEDAL MWLEEAKEGT ESWDILEAEI DSLQKKISEF EIEVLLNGEY
     DHNNAILELH PGAGGTESMD WCGILMRMYE RFAGYKGYKV EILNYLAGEE AGVKSVTLRI
     SGPYAYGNLK SERGVHRLVR ISPFDSNKRR HTSFVSCDVA PEIDETSEVE LKDDDIRMDT
     FQSSGAGGQS VNTTYSAVRL THIPTGIVVN IQNERSQIKN KEAAMQILKS KLIQKELEEK
     QAKLNALKGE KSDIGWGSQI RSYVFQPYQM VKDHRTNYEV GNIQSVMDGD IDGFINAYLK
     SKAYE