PRMA_ECOLI
ID PRMA_ECOLI Reviewed; 293 AA.
AC P0A8T1; P28637; P76680; P76681; Q2M8V6;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Ribosomal protein L11 methyltransferase {ECO:0000255|HAMAP-Rule:MF_00735, ECO:0000303|PubMed:8226664};
DE Short=L11 Mtase {ECO:0000255|HAMAP-Rule:MF_00735, ECO:0000305};
DE EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_00735, ECO:0000305|PubMed:372746, ECO:0000305|PubMed:7715456};
GN Name=prmA {ECO:0000255|HAMAP-Rule:MF_00735, ECO:0000303|PubMed:372746};
GN Synonyms=yhdI; OrderedLocusNames=b3259, JW3227;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8226664; DOI=10.1128/jb.175.22.7178-7188.1993;
RA Vanet A., Plumbridge J.A., Alix J.-H.;
RT "Cotranscription of two genes necessary for ribosomal protein L11
RT methylation (prmA) and pantothenate transport (panF) in Escherichia coli K-
RT 12.";
RL J. Bacteriol. 175:7178-7188(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-4.
RC STRAIN=K12;
RX PubMed=2193919; DOI=10.1128/jb.172.7.3842-3848.1990;
RA Jackowski S., Alix J.-H.;
RT "Cloning, sequence, and expression of the pantothenate permease (panF) gene
RT of Escherichia coli.";
RL J. Bacteriol. 172:3842-3848(1990).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 140-293.
RX PubMed=1459953; DOI=10.1128/jb.174.24.8043-8056.1992;
RA Ball C.A., Osuna R., Ferguson K.C., Johnson R.C.;
RT "Dramatic changes in Fis levels upon nutrient upshift in Escherichia
RT coli.";
RL J. Bacteriol. 174:8043-8056(1992).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 279-293, FUNCTION, CATALYTIC ACTIVITY,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF TRP-285.
RX PubMed=7715456; DOI=10.1111/j.1365-2958.1994.tb01330.x;
RA Vanet A., Plumbridge J.A., Guerin M.F., Alix J.-H.;
RT "Ribosomal protein methylation in Escherichia coli: the gene prmA, encoding
RT the ribosomal protein L11 methyltransferase, is dispensable.";
RL Mol. Microbiol. 14:947-958(1994).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=331082; DOI=10.1007/bf00330832;
RA Colson C.;
RT "Genetics of ribosomal protein methylation in Escherichia coli. I. A mutant
RT deficient in methylation of protein L11.";
RL Mol. Gen. Genet. 154:167-173(1977).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=372746; DOI=10.1007/bf00382270;
RA Colson C., Lhoest J., Urlings C.;
RT "Genetics of ribosomal protein methylation in Escherichia coli. III. Map
RT position of two genes, prmA and prmB, governing methylation of proteins L11
RT and L3.";
RL Mol. Gen. Genet. 169:245-250(1979).
CC -!- FUNCTION: Methylates ribosomal protein L11. {ECO:0000255|HAMAP-
CC Rule:MF_00735, ECO:0000269|PubMed:372746, ECO:0000269|PubMed:7715456}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) +
CC N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:54192, Rhea:RHEA-COMP:9752, Rhea:RHEA-
CC COMP:13826, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00735, ECO:0000305|PubMed:372746,
CC ECO:0000305|PubMed:7715456};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-terminal L-alpha-aminoacyl-[protein] + 3 S-adenosyl-L-
CC methionine = an N-terminal trimethyl-L-alpha-aminoacyl-[protein] + 3
CC H(+) + 3 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:62916, Rhea:RHEA-
CC COMP:10636, Rhea:RHEA-COMP:16230, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:78597,
CC ChEBI:CHEBI:146135; Evidence={ECO:0000305|PubMed:372746,
CC ECO:0000305|PubMed:7715456};
CC -!- INTERACTION:
CC P0A8T1; P0A7J7: rplK; NbExp=4; IntAct=EBI-556300, EBI-547288;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00735,
CC ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Mutant lacks several methyl groups in protein L11
CC (PubMed:331082, PubMed:372746). Null mutant is perfectly viable
CC (PubMed:7715456, PubMed:331082). {ECO:0000269|PubMed:331082,
CC ECO:0000269|PubMed:372746, ECO:0000269|PubMed:7715456}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. PrmA family.
CC {ECO:0000255|HAMAP-Rule:MF_00735, ECO:0000305}.
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DR EMBL; S67010; AAB28769.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58062.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U18997; AAA58063.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U00096; AAC76291.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77300.1; -; Genomic_DNA.
DR EMBL; M30953; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M95784; AAA23781.1; -; Genomic_DNA.
DR PIR; E65118; E65118.
DR RefSeq; NP_417725.1; NC_000913.3.
DR RefSeq; WP_001145827.1; NZ_SSZK01000034.1.
DR AlphaFoldDB; P0A8T1; -.
DR SMR; P0A8T1; -.
DR BioGRID; 4261866; 39.
DR BioGRID; 852021; 1.
DR DIP; DIP-47862N; -.
DR IntAct; P0A8T1; 14.
DR STRING; 511145.b3259; -.
DR jPOST; P0A8T1; -.
DR PaxDb; P0A8T1; -.
DR PRIDE; P0A8T1; -.
DR EnsemblBacteria; AAC76291; AAC76291; b3259.
DR EnsemblBacteria; BAE77300; BAE77300; BAE77300.
DR GeneID; 66672847; -.
DR GeneID; 947708; -.
DR KEGG; ecj:JW3227; -.
DR KEGG; eco:b3259; -.
DR PATRIC; fig|1411691.4.peg.3469; -.
DR EchoBASE; EB1460; -.
DR eggNOG; COG2264; Bacteria.
DR HOGENOM; CLU_049382_4_1_6; -.
DR InParanoid; P0A8T1; -.
DR OMA; EFFFIFP; -.
DR PhylomeDB; P0A8T1; -.
DR BioCyc; EcoCyc:EG11497-MON; -.
DR BioCyc; MetaCyc:EG11497-MON; -.
DR BRENDA; 2.1.1.244; 2026.
DR PRO; PR:P0A8T1; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0071885; F:N-terminal protein N-methyltransferase activity; IMP:EcoCyc.
DR GO; GO:0008276; F:protein methyltransferase activity; IBA:GO_Central.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IDA:EcoCyc.
DR GO; GO:0018012; P:N-terminal peptidyl-alanine trimethylation; IMP:EcoCyc.
DR GO; GO:0018023; P:peptidyl-lysine trimethylation; IDA:EcoCyc.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_00735; Methyltr_PrmA; 1.
DR InterPro; IPR004498; Ribosomal_PrmA_MeTrfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PIRSF; PIRSF000401; RPL11_MTase; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00406; prmA; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..293
FT /note="Ribosomal protein L11 methyltransferase"
FT /id="PRO_0000192257"
FT BINDING 145
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00735"
FT BINDING 166
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00735"
FT BINDING 188
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00735"
FT BINDING 230
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00735"
FT MUTAGEN 285
FT /note="W->R: Great decrease in activity."
FT /evidence="ECO:0000269|PubMed:7715456"
FT CONFLICT 78
FT /note="L -> S (in Ref. 1; AAB28769)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 293 AA; 31877 MW; CF0EDE130245B8FC CRC64;
MPWIQLKLNT TGANAEDLSD ALMEAGAVSI TFQDTHDTPV FEPLPGETRL WGDTDVIGLF
DAETDMNDVV AILENHPLLG AGFAHKIEQL EDKDWEREWM DNFHPMRFGE RLWICPSWRD
VPDENAVNVM LDPGLAFGTG THPTTSLCLQ WLDSLDLTGK TVIDFGCGSG ILAIAALKLG
AAKAIGIDID PQAIQASRDN AERNGVSDRL ELYLPKDQPE EMKADVVVAN ILAGPLRELA
PLISVLPVSG GLLGLSGILA SQAESVCEAY ADSFALDPVV EKEEWCRITG RKN
