PRMC_SALTY
ID PRMC_SALTY Reviewed; 277 AA.
AC P40816;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 13-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Release factor glutamine methyltransferase {ECO:0000255|HAMAP-Rule:MF_02126};
DE Short=RF MTase {ECO:0000255|HAMAP-Rule:MF_02126};
DE EC=2.1.1.297 {ECO:0000255|HAMAP-Rule:MF_02126};
DE AltName: Full=N5-glutamine methyltransferase PrmC {ECO:0000255|HAMAP-Rule:MF_02126};
DE AltName: Full=Protein-(glutamine-N5) MTase PrmC {ECO:0000255|HAMAP-Rule:MF_02126};
DE AltName: Full=Protein-glutamine N-methyltransferase PrmC {ECO:0000255|HAMAP-Rule:MF_02126};
GN Name=prmC {ECO:0000255|HAMAP-Rule:MF_02126}; Synonyms=hemK;
GN OrderedLocusNames=STM1775;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-77.
RX PubMed=2544564; DOI=10.1128/jb.171.7.3948-3960.1989;
RA Elliott T.;
RT "Cloning, genetic characterization, and nucleotide sequence of the hemA-
RT prfA operon of Salmonella typhimurium.";
RL J. Bacteriol. 171:3948-3960(1989).
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:0000255|HAMAP-Rule:MF_02126}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_02126};
CC -!- SIMILARITY: Belongs to the protein N5-glutamine methyltransferase
CC family. PrmC subfamily. {ECO:0000255|HAMAP-Rule:MF_02126}.
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DR EMBL; AE006468; AAL20690.1; -; Genomic_DNA.
DR EMBL; J04243; AAA88612.1; -; Genomic_DNA.
DR PIR; C32890; C32890.
DR RefSeq; NP_460731.1; NC_003197.2.
DR RefSeq; WP_000347310.1; NC_003197.2.
DR AlphaFoldDB; P40816; -.
DR SMR; P40816; -.
DR STRING; 99287.STM1775; -.
DR PaxDb; P40816; -.
DR EnsemblBacteria; AAL20690; AAL20690; STM1775.
DR GeneID; 1253294; -.
DR KEGG; stm:STM1775; -.
DR PATRIC; fig|99287.12.peg.1870; -.
DR HOGENOM; CLU_018398_3_1_6; -.
DR OMA; FDARYWE; -.
DR PhylomeDB; P40816; -.
DR BioCyc; SENT99287:STM1775-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0102559; F:protein-(glutamine-N5) methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0036009; F:protein-glutamine N-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0018364; P:peptidyl-glutamine methylation; IBA:GO_Central.
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; IPR025714; Methyltranfer_dom.
DR InterPro; IPR040758; PrmC_N.
DR InterPro; IPR019874; Release_fac_Glu-N5_MeTfrase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF13847; Methyltransf_31; 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 3: Inferred from homology;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..277
FT /note="Release factor glutamine methyltransferase"
FT /id="PRO_0000157157"
FT BINDING 117..121
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02126"
FT BINDING 140
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02126"
FT BINDING 168
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02126"
FT BINDING 183..186
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02126"
FT BINDING 183
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02126"
SQ SEQUENCE 277 AA; 30966 MW; 20DDBCE6261745C7 CRC64;
MDFQHWLHEA VNQLRDSDSP RRDAEILLEY VTGKGRTYIM AFGETPLTDV QQQQLADLLQ
RRKQGEPIAY LTGLREFWSL PLFVSPATLI PRPDTECLVE QALARLPVKT CRILDLGTGT
GAIALALACE RPDCEVTAVD RMPDAVALAI RNAEHLAIRN VRILQSCWFS ALSGQQFDMI
VSNPPYIDAQ DPHLSEGDVR FEPRSALVAD ENGMADLTHI IDNARQMLTP GGFLLLEHGW
QQGEAVRAVF RRSGYSDVET CRDYGGNERV TCGRFTP
