RF2_NEIMB
ID RF2_NEIMB Reviewed; 367 AA.
AC Q9JXB3;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 110.
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=NMB2138;
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC58;
RX PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA Moxon E.R., Rappuoli R., Venter J.C.;
RT "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT MC58.";
RL Science 287:1809-1815(2000).
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; AE002098; AAF42446.1; -; Genomic_DNA.
DR PIR; H81001; H81001.
DR RefSeq; NP_275123.1; NC_003112.2.
DR RefSeq; WP_002225736.1; NC_003112.2.
DR AlphaFoldDB; Q9JXB3; -.
DR SMR; Q9JXB3; -.
DR STRING; 122586.NMB2138; -.
DR PaxDb; Q9JXB3; -.
DR EnsemblBacteria; AAF42446; AAF42446; NMB2138.
DR KEGG; nme:NMB2138; -.
DR PATRIC; fig|122586.8.peg.2729; -.
DR HOGENOM; CLU_036856_6_0_4; -.
DR OMA; YVFHPYQ; -.
DR Proteomes; UP000000425; 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_0000166835"
FT MOD_RES 254
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00094"
SQ SEQUENCE 367 AA; 41489 MW; DC5D4417C6FAC72B CRC64;
MEAEVINQLN NTLNDLEKRS EDIRVYMDYQ GKKDRLEEVI GLSEDPELWN DPKRAQEIGK
ERKILEGIVL TLDNIASGIE DNRMLIEMTV EENDEEGFAA VQEDVAGLEK QMADLEFKRM
FNQPADPNNC FIDITAGAGG TEAEDWAGML FRMYSRYAER KGFRIEILEE DDGEIAGINR
ATIRVEGEYA YGLLRTETGV HRLVRYSPFD SNNKRHTSFA SVFVYPEIDD SIEIEINPAD
LRIDTYRASG AGGQHINKTD SAVRITHEPT GIVVQCQNDR SQHANKAAAM EMLKSKLYEL
EMRKRNEEKQ ALEEGKSDVG WGSQIRSYVL DSSRIKDLRT GYEVGNTKAV LDGDLDGFIE
ASLKQGV