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Database: UniProt
Entry: A0A3M8HFC4_9BACI
LinkDB: A0A3M8HFC4_9BACI
Original site: A0A3M8HFC4_9BACI 
ID   A0A3M8HFC4_9BACI        Unreviewed;       256 AA.
AC   A0A3M8HFC4;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   18-JUN-2025, entry version 24.
DE   RecName: Full=protein-glutamate O-methyltransferase {ECO:0000256|ARBA:ARBA00012534};
DE            EC=2.1.1.80 {ECO:0000256|ARBA:ARBA00012534};
GN   ORFNames=EC501_03485 {ECO:0000313|EMBL:RND00751.1};
OS   Lysinibacillus halotolerans.
OC   Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC   Lysinibacillus.
OX   NCBI_TaxID=1368476 {ECO:0000313|EMBL:RND00751.1, ECO:0000313|Proteomes:UP000279909};
RN   [1] {ECO:0000313|EMBL:RND00751.1, ECO:0000313|Proteomes:UP000279909}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCCC 1A12703 {ECO:0000313|EMBL:RND00751.1,
RC   ECO:0000313|Proteomes:UP000279909};
RX   PubMed=24814335; DOI=10.1099/ijs.0.061465-0;
RA   Kong D., Wang Y., Zhao B., Li Y., Song J., Zhai Y., Zhang C., Wang H.,
RA   Chen X., Zhao B., Ruan Z.;
RT   "Lysinibacillus halotolerans sp. nov., isolated from saline-alkaline
RT   soil.";
RL   Int. J. Syst. Evol. Microbiol. 64:2593-2598(2014).
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};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RND00751.1}.
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DR   EMBL; RHLQ01000005; RND00751.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M8HFC4; -.
DR   OrthoDB; 9816309at2; -.
DR   Proteomes; UP000279909; Unassembled WGS sequence.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd02440; AdoMet_MTases; 1.
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; IPR050903; Bact_Chemotaxis_MeTrfase.
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:SF19; 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:RND00751.1};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RND00751.1}.
FT   DOMAIN          1..256
FT                   /note="CheR-type methyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50123"
SQ   SEQUENCE   256 AA;  30166 MW;  20DC75F9C71F9357 CRC64;
     MSDYEQFIAG IKNKTGIDLA LYKEAQMKRR LTSLYEKKGY QNFVEFLHAL EKDRDLMNEF
     LDRMTINVSE FYRNGKRWDV LQNKIFPLLL NHNKRLKIWS AACSTGEEPY TISMVLSHHI
     PLSQIQVLAT DIDENVIQKA KLGLYPERSL DEVPNDVKHK YFIQEGPFFK VKDEIKRTVT
     FKKHNLLKDT YDSNLDLIVC RNVMIYFTEE AKDQIYQKFS QSLRPGGVLF VGSTEQIFNP
     SRYGFEVVDT FFYRKI
//
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