ID   RF2_LEPIN               Reviewed;         367 AA.
AC   Q8EZT4;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 96.
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=LA_3767;
OS   Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain
OS   56601).
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=189518;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=56601;
RX   PubMed=12712204; DOI=10.1038/nature01597;
RA   Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X.,
RA   Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X.,
RA   Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., Zhang Y., Zhu G.-F.,
RA   Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y.,
RA   Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I.,
RA   Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.;
RT   "Unique physiological and pathogenic features of Leptospira interrogans
RT   revealed by whole-genome sequencing.";
RL   Nature 422:888-893(2003).
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; AE010300; AAN50965.1; -; Genomic_DNA.
DR   RefSeq; NP_713947.1; NC_004342.2.
DR   RefSeq; WP_000453255.1; NC_004342.2.
DR   AlphaFoldDB; Q8EZT4; -.
DR   SMR; Q8EZT4; -.
DR   STRING; 189518.LA_3767; -.
DR   EnsemblBacteria; AAN50965; AAN50965; LA_3767.
DR   KEGG; lil:LA_3767; -.
DR   PATRIC; fig|189518.3.peg.3739; -.
DR   HOGENOM; CLU_036856_6_0_12; -.
DR   InParanoid; Q8EZT4; -.
DR   OMA; YVFHPYQ; -.
DR   Proteomes; UP000001408; Chromosome I.
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_0000166826"
FT   MOD_RES         254
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00094"
SQ   SEQUENCE   367 AA;  42032 MW;  B0325CD288E0A3B5 CRC64;
     MEVKSAKELK RISKELQENF LNRWKLLNLE QDKDRLKSLT EKAEDPNLWN NPEEARLVSQ
     KKNELEKKLN PWFTIQQDIL DFPDLVDLTL DEKGENGVGE LSSEYNRLQE KFEELELLGA
     LKNPEDLKPA FLNIHPGAGG TESQDWAEML LRMYTRYFEK KGYQYSLIDV QAGDGAGIKN
     ATLHVIGDFA FGFLKGENGV HRLVRISPFD ANKRRHTSFV SVHVSPEIDD DIDIKIEEKD
     IRVDVYRSSG AGGQHVNTTD SAVRITHMPS GIVVACQNER SQIKNRDTAF KMLKARLYEL
     EQEKAKEELE KKSGEKKDIA WGSQIRSYVF HPYNLVKDHR TDHETGNVAA VMDGDIEPFI
     LAYLKTL