PRMC_CHLT2
ID PRMC_CHLT2 Reviewed; 290 AA.
AC B0B9D1; Q6J519;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Release factor glutamine methyltransferase;
DE Short=RF MTase;
DE EC=2.1.1.297;
DE AltName: Full=N5-glutamine methyltransferase PrmC;
DE AltName: Full=Protein-(glutamine-N5) MTase PrmC;
DE AltName: Full=Protein-glutamine N-methyltransferase PrmC;
GN Name=prmC; OrderedLocusNames=CTL0279;
OS Chlamydia trachomatis serovar L2 (strain 434/Bu / ATCC VR-902B).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=471472;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=434/Bu / ATCC VR-902B;
RX PubMed=15629922; DOI=10.1128/jb.187.2.507-511.2005;
RA Pannekoek Y., Heurgue-Hamard V., Langerak A.A., Speijer D.,
RA Buckingham R.H., van der Ende A.;
RT "The N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase
RT PrmC/HemK in Chlamydia trachomatis methylates class 1 release factors.";
RL J. Bacteriol. 187:507-511(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=434/Bu / ATCC VR-902B;
RX PubMed=18032721; DOI=10.1101/gr.7020108;
RA Thomson N.R., Holden M.T.G., Carder C., Lennard N., Lockey S.J., Marsh P.,
RA Skipp P., O'Connor C.D., Goodhead I., Norbertzcak H., Harris B., Ormond D.,
RA Rance R., Quail M.A., Parkhill J., Stephens R.S., Clarke I.N.;
RT "Chlamydia trachomatis: genome sequence analysis of lymphogranuloma
RT venereum isolates.";
RL Genome Res. 18:161-171(2008).
CC -!- FUNCTION: Methylates the class 1 translation termination release
CC factors RF1/PrfA and RF2/PrfB on the glutamine residue of the
CC universally conserved GGQ motif. {ECO:0000269|PubMed:15629922}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-
CC methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release
CC factor] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:42896, Rhea:RHEA-
CC COMP:10271, Rhea:RHEA-COMP:10272, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30011, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:61891; EC=2.1.1.297;
CC Evidence={ECO:0000269|PubMed:15629922};
CC -!- SIMILARITY: Belongs to the protein N5-glutamine methyltransferase
CC family. PrmC subfamily. {ECO:0000305}.
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DR EMBL; AY600244; AAT35566.1; -; Genomic_DNA.
DR EMBL; AM884176; CAP03718.1; -; Genomic_DNA.
DR RefSeq; WP_009873502.1; NC_010287.1.
DR RefSeq; YP_001654363.1; NC_010287.1.
DR AlphaFoldDB; B0B9D1; -.
DR SMR; B0B9D1; -.
DR EnsemblBacteria; CAP03718; CAP03718; CTL0279.
DR KEGG; ctb:CTL0279; -.
DR PATRIC; fig|471472.4.peg.303; -.
DR HOGENOM; CLU_018398_3_1_0; -.
DR OMA; FDARYWE; -.
DR BRENDA; 2.1.1.297; 1315.
DR Proteomes; UP000000795; Chromosome.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008276; F:protein methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0102559; F:protein-(glutamine-N5) methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0036009; F:protein-glutamine N-methyltransferase activity; IGI:UniProtKB.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0018364; P:peptidyl-glutamine methylation; IGI:UniProtKB.
DR GO; GO:0006479; P:protein methylation; IDA:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_02126; RF_methyltr_PrmC; 1.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR004556; HemK-like.
DR InterPro; IPR040758; PrmC_N.
DR InterPro; IPR019874; Release_fac_Glu-N5_MeTfrase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR007848; Small_mtfrase_dom.
DR Pfam; PF05175; MTS; 1.
DR Pfam; PF17827; PrmC_N; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00536; hemK_fam; 1.
DR TIGRFAMs; TIGR03534; RF_mod_PrmC; 1.
PE 1: Evidence at protein level;
KW Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..290
FT /note="Release factor glutamine methyltransferase"
FT /id="PRO_0000414509"
FT BINDING 140
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 181..184
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
SQ SEQUENCE 290 AA; 32772 MW; 0230007284D58217 CRC64;
MKKLLREASE YLLSRGIRFP QREAEDILMD LLEISSRSAL HQAKLSSEEQ SLYWKRLRKR
GDRCPTAYIH GKVHFLGVEL QVTPQVLIPR QETEIFVEQI IGYLQMHKEK TTFYDVCCGS
GCIGLAVRKH CPHVRVTLSD ISPEALAIAE SNARSNALAV DFLLGDLFDP FSFPADVLVC
NPPYLSYKEF FESDPEVRCH EPWKALVGGV SGLEFYHRIA THIHKILVSG GVGWLEIGST
QGEDVKQIFH AKGIRGRVLK DYAQLDRFFF LENQANDAVS SGEVSGFSER
