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Database: UniProt
Entry: U5N4P2_9BURK
LinkDB: U5N4P2_9BURK
Original site: U5N4P2_9BURK 
ID   U5N4P2_9BURK            Unreviewed;       244 AA.
AC   U5N4P2;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=protein-glutamate O-methyltransferase {ECO:0000256|ARBA:ARBA00012534};
DE            EC=2.1.1.80 {ECO:0000256|ARBA:ARBA00012534};
GN   Name=cheR-1 {ECO:0000313|EMBL:AGX86451.1};
GN   ORFNames=Cenrod_0327 {ECO:0000313|EMBL:AGX86451.1};
OS   Candidatus Symbiobacter mobilis CR.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae.
OX   NCBI_TaxID=946483 {ECO:0000313|EMBL:AGX86451.1, ECO:0000313|Proteomes:UP000017184};
RN   [1] {ECO:0000313|EMBL:AGX86451.1, ECO:0000313|Proteomes:UP000017184}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CR {ECO:0000313|EMBL:AGX86451.1};
RX   PubMed=24267588; DOI=10.1186/gb-2013-14-11-r127;
RA   Liu Z., Muller J., Li T., Alvey R.M., Vogl K., Frigaard N.U.,
RA   Rockwell N.C., Boyd E.S., Tomsho L.P., Schuster S.C., Henke P., Rohde M.,
RA   Overmann J., Bryant D.A.;
RT   "Genomic analysis reveals key aspects of prokaryotic symbiosis in the
RT   phototrophic consortium "Chlorochromatium aggregatum".";
RL   Genome Biol. 14:R127-R127(2013).
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; CP004885; AGX86451.1; -; Genomic_DNA.
DR   AlphaFoldDB; U5N4P2; -.
DR   STRING; 946483.Cenrod_0327; -.
DR   KEGG; cbx:Cenrod_0327; -.
DR   PATRIC; fig|946483.4.peg.328; -.
DR   eggNOG; COG1352; Bacteria.
DR   HOGENOM; CLU_025854_0_0_4; -.
DR   Proteomes; UP000017184; 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; IPR026024; Chemotaxis_MeTrfase_CheR.
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:SF26; CHEMOTAXIS PROTEIN METHYLTRANSFERASE; 1.
DR   Pfam; PF01739; CheR; 1.
DR   Pfam; PF03705; CheR_N; 1.
DR   PIRSF; PIRSF000410; CheR; 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:AGX86451.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017184};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PIRSR:PIRSR000410-1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AGX86451.1}.
FT   DOMAIN          1..244
FT                   /note="CheR-type methyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50123"
FT   BINDING         51
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
FT   BINDING         53
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
FT   BINDING         57
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
FT   BINDING         91
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
FT   BINDING         114
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
FT   BINDING         172..173
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
FT   BINDING         189..190
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
SQ   SEQUENCE   244 AA;  28100 MW;  81CB1D65531ABAB1 CRC64;
     MADAKKPLVT GRLHKRLAHY GLDSFGQYFQ LLSSGQYPDE VQMAVDLLTT NETYFFREIK
     HFEFLRKLAL QERDRSAMFR VWSAASSSGE EAYSIAMVLA DCMQSTQWEV MGTDISTRVL
     EGARRALYTL ERARHVPDNY RKKFCRKGTG QYEGYLLIDR SLRTHVSFRQ VNLNNTLPEL
     GQFDVVFLRN VMIYFNNETK RQVVARVIAN IKPKGYFMIG HSESLNDISQ AVQMVAPSVY
     RKGA
//
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