ID   RF2_BACSU               Reviewed;         366 AA.
AC   P28367; O34444;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Peptide chain release factor 2;
DE            Short=RF-2;
GN   Name=prfB; OrderedLocusNames=BSU35290;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9696765; DOI=10.1128/jb.180.16.4166-4170.1998;
RA   Karow M.L., Rogers E.J., Lovett P.S., Piggot P.J.;
RT   "Suppression of TGA mutations in the Bacillus subtilis spoIIR gene by prfB
RT   mutations.";
RL   J. Bacteriol. 180:4166-4170(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Lazarevic V., Soldo B., Rivolta C., Reynolds S., Mauel C., Karamata D.;
RT   "Nucleotide sequence of the 300-304 chromosomal segment of Bacillus
RT   subtilis.";
RL   Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-338.
RC   STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC   3610 / NRRL NRS-744 / VKM B-501;
RX   PubMed=1901557; DOI=10.1016/0378-1119(91)90110-w;
RA   Sadaie Y., Takamatsu H., Nakamura K., Yamane K.;
RT   "Sequencing reveals similarity of the wild-type div+ gene of Bacillus
RT   subtilis to the Escherichia coli secA gene.";
RL   Gene 98:101-105(1991).
RN   [5]
RP   PROBABLE FUNCTION, AND RIBOSOMAL FRAMESHIFT.
RX   PubMed=1408743; DOI=10.1093/nar/20.17.4423;
RA   Pel H.J., Rep M., Grivell L.A.;
RT   "Sequence comparison of new prokaryotic and mitochondrial members of the
RT   polypeptide chain release factor family predicts a five-domain model for
RT   release factor structure.";
RL   Nucleic Acids Res. 20:4423-4428(1992).
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.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- PTM: Methylated by PrmC. Methylation increases the termination
CC       efficiency of RF2 (By similarity). {ECO:0000250}.
CC   -!- MISCELLANEOUS: The gene for this protein contains a UGA in-frame
CC       termination codon after Leu-24; a naturally occurring frameshift
CC       enables complete translation of RF-2. This provides a mechanism for the
CC       protein to regulate its own production.
CC   -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA01123.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF013188; AAC97534.1; -; Genomic_DNA.
DR   EMBL; AF017113; AAC67303.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15546.1; -; Genomic_DNA.
DR   EMBL; D10279; BAA01123.1; ALT_INIT; Genomic_DNA.
DR   PIR; H69681; JN0146.
DR   RefSeq; NP_391409.1; NC_000964.3.
DR   RefSeq; WP_010886623.1; NZ_JNCM01000033.1.
DR   PDB; 6SZS; EM; 3.06 A; z=5-366.
DR   PDBsum; 6SZS; -.
DR   AlphaFoldDB; P28367; -.
DR   SMR; P28367; -.
DR   STRING; 224308.BSU35290; -.
DR   PaxDb; P28367; -.
DR   PRIDE; P28367; -.
DR   EnsemblBacteria; CAB15546; CAB15546; BSU_35290.
DR   GeneID; 936692; -.
DR   KEGG; bsu:BSU35290; -.
DR   PATRIC; fig|224308.43.peg.3694; -.
DR   eggNOG; COG1186; Bacteria.
DR   InParanoid; P28367; -.
DR   OMA; YVFHPYQ; -.
DR   PhylomeDB; P28367; -.
DR   BioCyc; BSUB:BSU35290-MON; -.
DR   Proteomes; UP000001570; 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   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Methylation; Protein biosynthesis;
KW   Reference proteome; Ribosomal frameshifting.
FT   CHAIN           1..366
FT                   /note="Peptide chain release factor 2"
FT                   /id="PRO_0000166803"
FT   MOD_RES         251
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        338
FT                   /note="T -> D (in Ref. 4; BAA01123)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   366 AA;  42073 MW;  FB42BE654541D6E2 CRC64;
     MELSEIRAEL ENMASRLADF RGSLDLESKE ARIAELDEQM ADPEFWNDQQ KAQTVINEAN
     GLKDYVNSYK KLNESHEELQ MTHDLLKEEP DTDLQLELEK ELKSLTKEFN EFELQLLLSE
     PYDKNNAILE LHPGAGGTES QDWGSMLLRM YTRWGERRGF KVETLDYLPG DEAGIKSVTL
     LIKGHNAYGY LKAEKGVHRL VRISPFDSSG RRHTSFVSCE VMPEFNDEID IDIRTEDIKV
     DTYRASGAGG QHVNTTDSAV RITHLPTNVV VTCQTERSQI KNRERAMKML KAKLYQRRIE
     EQQAELDEIR GEQKEIGWGS QIRSYVFHPY SMVKDHRTNT EMGNVQAVMD GDIDTFIDAY
     LRSKLS