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Database: UniProt
Entry: A0A0K9GVF1_9BACI
LinkDB: A0A0K9GVF1_9BACI
Original site: A0A0K9GVF1_9BACI 
ID   A0A0K9GVF1_9BACI        Unreviewed;       258 AA.
AC   A0A0K9GVF1;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=protein-glutamate O-methyltransferase {ECO:0000256|ARBA:ARBA00012534};
DE            EC=2.1.1.80 {ECO:0000256|ARBA:ARBA00012534};
GN   ORFNames=AC625_14725 {ECO:0000313|EMBL:KMY50606.1};
OS   Peribacillus loiseleuriae.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Peribacillus.
OX   NCBI_TaxID=1679170 {ECO:0000313|EMBL:KMY50606.1, ECO:0000313|Proteomes:UP000037146};
RN   [1] {ECO:0000313|Proteomes:UP000037146}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FJAT-27997 {ECO:0000313|Proteomes:UP000037146};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA   Shi H., Pan Z., Liu X.;
RT   "Genome sequencing project for genomic taxonomy and phylogenomics of
RT   Bacillus-like bacteria.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:KMY50606.1}.
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DR   EMBL; LFZW01000001; KMY50606.1; -; Genomic_DNA.
DR   RefSeq; WP_049681959.1; NZ_LFZW01000001.1.
DR   AlphaFoldDB; A0A0K9GVF1; -.
DR   STRING; 1679170.AC625_14725; -.
DR   PATRIC; fig|1679170.3.peg.3359; -.
DR   OrthoDB; 9816309at2; -.
DR   Proteomes; UP000037146; Unassembled WGS sequence.
DR   GO; GO:0008983; F:protein-glutamate O-methyltransferase activity; IEA:UniProtKB-EC.
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; 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   Reference proteome {ECO:0000313|Proteomes:UP000037146};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..258
FT                   /note="CheR-type methyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50123"
SQ   SEQUENCE   258 AA;  30380 MW;  31392F074763BF4C CRC64;
     MVQEYEQFIL KIKKLTGIDL SLYKEAQMKR RLTSLYEKKG YQSFDAYFQA IQQDTKQREE
     FLDRMTINVS EFFRNAKRWE VLAEKILPRL LLSKRKLKIW SAACSTGEEP YTIAMVLSAF
     LPLQQIEVYA TDIDENVIAR AKLGVYPERS LNEVPAEVKK KFFIKEGNFY HVADEIKKTV
     TFKKQNLLSE KFDTNYDLIV CRNVLIYFTE EAKHSLYTKF SQALKTDGVF FVGSTEQIFN
     PNQYGFETED TFFYKKLP
//
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