ID Q2RX17_RHORT Unreviewed; 280 AA.
AC Q2RX17;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=protein-glutamate O-methyltransferase {ECO:0000256|ARBA:ARBA00012534};
DE EC=2.1.1.80 {ECO:0000256|ARBA:ARBA00012534};
GN OrderedLocusNames=Rru_A0524 {ECO:0000313|EMBL:ABC21328.1};
OS Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 /
OS NCIMB 8255 / S1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Rhodospirillum.
OX NCBI_TaxID=269796 {ECO:0000313|EMBL:ABC21328.1, ECO:0000313|Proteomes:UP000001929};
RN [1] {ECO:0000313|EMBL:ABC21328.1, ECO:0000313|Proteomes:UP000001929}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1
RC {ECO:0000313|Proteomes:UP000001929};
RX PubMed=21886856; DOI=10.4056/sigs.1804360;
RA Munk A.C., Copeland A., Lucas S., Lapidus A., Del Rio T.G., Barry K.,
RA Detter J.C., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N.C.,
RA Mavromatis K., Richardson P., Rohde M., Goker M., Klenk H.P., Zhang Y.,
RA Roberts G.P., Reslewic S., Schwartz D.C.;
RT "Complete genome sequence of Rhodospirillum rubrum type strain (S1).";
RL Stand. Genomic Sci. 4:293-302(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamyl-[protein] + S-adenosyl-L-methionine = [protein]-L-
CC glutamate 5-O-methyl ester + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:24452, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:10311,
CC ChEBI:CHEBI:29973, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:82795; EC=2.1.1.80;
CC Evidence={ECO:0000256|ARBA:ARBA00001541};
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DR EMBL; CP000230; ABC21328.1; -; Genomic_DNA.
DR RefSeq; WP_011388282.1; NC_007643.1.
DR RefSeq; YP_425615.1; NC_007643.1.
DR AlphaFoldDB; Q2RX17; -.
DR STRING; 269796.Rru_A0524; -.
DR EnsemblBacteria; ABC21328; ABC21328; Rru_A0524.
DR KEGG; rru:Rru_A0524; -.
DR PATRIC; fig|269796.9.peg.578; -.
DR eggNOG; COG1352; Bacteria.
DR HOGENOM; CLU_025854_0_2_5; -.
DR PhylomeDB; Q2RX17; -.
DR Proteomes; UP000001929; Chromosome.
DR GO; GO:0008983; F:protein-glutamate O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.155.10; Chemotaxis receptor methyltransferase CheR, N-terminal domain; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR022642; CheR_C.
DR InterPro; IPR000780; CheR_MeTrfase.
DR InterPro; IPR022641; CheR_N.
DR InterPro; IPR036804; CheR_N_sf.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR24422; CHEMOTAXIS PROTEIN METHYLTRANSFERASE; 1.
DR PANTHER; PTHR24422:SF25; CHEMOTAXIS PROTEIN METHYLTRANSFERASE; 1.
DR Pfam; PF01739; CheR; 1.
DR Pfam; PF03705; CheR_N; 1.
DR PRINTS; PR00996; CHERMTFRASE.
DR SMART; SM00138; MeTrc; 1.
DR SUPFAM; SSF47757; Chemotaxis receptor methyltransferase CheR, N-terminal domain; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS50123; CHER; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:ABC21328.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001929};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..256
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
SQ SEQUENCE 280 AA; 31748 MW; DF418EB484BDFC50 CRC64;
MKPEDFDFIS KLLKDKSGLV LTKDKSYLIE SRLMPLARKR GFKGLDELIG QLRRRDLALE
REITEAMTTN ESFFFRDSKP FDQFRQVVLP NILKARASKK SFRIWCAAAS SGQEPYSLAM
ILKEEAARLA GWRVEIVGTD LSTDILKKAR SGLYSQFEVQ RGMPMNLLVK YFKKKDEMWE
IDAGIRAMVQ YKEWNLLEDL RPLGQFDVVY CRNVLIYFDQ PTKTKVLDAA AALMPEDGVL
YLGGAETVLG ITNAFRPIPG QRGVYAVAKG ENVKSLGAEA
//
