ID   RF2_NEIG1               Reviewed;         367 AA.
AC   Q5F5H5;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 93.
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=NGO1951;
OS   Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=242231;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700825 / FA 1090;
RA   Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F.,
RA   Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C.,
RA   Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S.,
RA   Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.;
RT   "The complete genome sequence of Neisseria gonorrhoeae.";
RL   Submitted (MAR-2003) 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: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; AE004969; AAW90562.1; -; Genomic_DNA.
DR   RefSeq; WP_003688127.1; NC_002946.2.
DR   RefSeq; YP_208974.1; NC_002946.2.
DR   AlphaFoldDB; Q5F5H5; -.
DR   SMR; Q5F5H5; -.
DR   STRING; 242231.NGO_1951; -.
DR   EnsemblBacteria; AAW90562; AAW90562; NGO_1951.
DR   GeneID; 66754167; -.
DR   KEGG; ngo:NGO_1951; -.
DR   PATRIC; fig|242231.10.peg.2349; -.
DR   HOGENOM; CLU_036856_6_0_4; -.
DR   OMA; YVFHPYQ; -.
DR   Proteomes; UP000000535; 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.
DR   PROSITE; PS00745; RF_PROK_I; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methylation; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..367
FT                   /note="Peptide chain release factor 2"
FT                   /id="PRO_0000166833"
FT   MOD_RES         254
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00094"
SQ   SEQUENCE   367 AA;  41362 MW;  84353B9B5087066D CRC64;
     MEAEVINQLN NTLNDLEKRS EDIRVYMDYQ GKKDRLEEVI GLSEDPELWN DPKRAQEIGK
     ESKILEGIVL TLDNIASGIE DNRMLIEMAV EENDEEGFAA VKEDVAGLEK QMADLEFKRM
     FNQPADPNNC FIDITAGAGG TEAEDWAGML FRMYSRYAER KGFKIEILEE DDGEIAGINR
     ATIRVEGEYA YGLLRTETGV HRLVRYSPFD SNNKRHTSFA SVFVYPEIDD SIEIEINPAD
     LRIDTYRASG AGGQHINKTD SAVRITHEPT GIVVQCQNDR SQHANKAAAM EMLKSKLYEL
     EMRKRNEEKQ ALEEGKSDVG WGSQIRSYVL DSSRIKDLRT GYEVGNTKAV LDGDLDGFIE
     ASLKQGV