PRMB_YERPE
ID PRMB_YERPE Reviewed; 310 AA.
AC Q0WDE1; Q74SY9; Q8D0U7;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=50S ribosomal protein L3 glutamine methyltransferase {ECO:0000255|HAMAP-Rule:MF_02125};
DE Short=L3 MTase {ECO:0000255|HAMAP-Rule:MF_02125};
DE EC=2.1.1.298 {ECO:0000255|HAMAP-Rule:MF_02125};
DE AltName: Full=N5-glutamine methyltransferase PrmB {ECO:0000255|HAMAP-Rule:MF_02125};
GN Name=prmB {ECO:0000255|HAMAP-Rule:MF_02125};
GN OrderedLocusNames=YPO2750, y1584, YP_2413;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
CC -!- FUNCTION: Specifically methylates the 50S ribosomal protein L3 on a
CC specific glutamine residue. {ECO:0000255|HAMAP-Rule:MF_02125}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutaminyl-[ribosomal protein uL3] + S-adenosyl-L-methionine
CC = H(+) + N(5)-methyl-L-glutaminyl-[ribosomal protein uL3] + S-
CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:45020, Rhea:RHEA-COMP:11063,
CC Rhea:RHEA-COMP:11064, ChEBI:CHEBI:15378, ChEBI:CHEBI:30011,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61891;
CC EC=2.1.1.298; Evidence={ECO:0000255|HAMAP-Rule:MF_02125};
CC -!- SIMILARITY: Belongs to the protein N5-glutamine methyltransferase
CC family. PrmB subfamily. {ECO:0000255|HAMAP-Rule:MF_02125}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM85153.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAS62618.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL590842; CAL21369.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM85153.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE017042; AAS62618.1; ALT_INIT; Genomic_DNA.
DR PIR; AF0335; AF0335.
DR RefSeq; WP_002209710.1; NZ_WUCM01000012.1.
DR RefSeq; YP_002347697.1; NC_003143.1.
DR AlphaFoldDB; Q0WDE1; -.
DR SMR; Q0WDE1; -.
DR IntAct; Q0WDE1; 4.
DR STRING; 214092.YPO2750; -.
DR PaxDb; Q0WDE1; -.
DR DNASU; 1146531; -.
DR EnsemblBacteria; AAM85153; AAM85153; y1584.
DR EnsemblBacteria; AAS62618; AAS62618; YP_2413.
DR GeneID; 66844946; -.
DR KEGG; ype:YPO2750; -.
DR KEGG; ypk:y1584; -.
DR KEGG; ypm:YP_2413; -.
DR PATRIC; fig|1028802.3.peg.1708; -.
DR eggNOG; COG2890; Bacteria.
DR HOGENOM; CLU_018398_5_1_6; -.
DR OMA; IYYGHGT; -.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0036009; F:protein-glutamine N-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:InterPro.
DR GO; GO:0018364; P:peptidyl-glutamine methylation; IBA:GO_Central.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_02125; L3_methyltr_PrmB; 1.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR004556; HemK-like.
DR InterPro; IPR017127; Ribosome_L3_Gln-N5_MeTrfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR007848; Small_mtfrase_dom.
DR Pfam; PF05175; MTS; 1.
DR PIRSF; PIRSF037167; Mtase_YfcB_prd; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00536; hemK_fam; 1.
DR TIGRFAMs; TIGR03533; L3_gln_methyl; 1.
PE 3: Inferred from homology;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..310
FT /note="50S ribosomal protein L3 glutamine
FT methyltransferase"
FT /id="PRO_0000414185"
SQ SEQUENCE 310 AA; 35296 MW; A2CC87125E3F0483 CRC64;
MDKIFVDEAV NELHTIQDML RWTVSRFNAA NIFYGHGTDN PWDEAVQLVF PSLFLPLDIP
EDIRSSRLTS SERHRIVERV IRRVNERIPV AYLTNKAWFC GMEYYVDERV LVPRSPIGEL
IENRFDGLIH HQPNHILDMC TGSGCIAIAC AYAFPDAEVD AVDISNDVLA VTEHNIQQHG
MEHQVTPIRS DLFRDLPPIK YDLIVTNPPY VDAEDMADLP QEFRFEPELG LAAGSDGLKL
ARRILACAPD FLQDDGVLIC EVGNSMVHLM DQYPDVPFTW LEFEKGGDGV FMLTKQQLID
CAAHFSMYRD
