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Database: UniProt
Entry: A0A139CHF5_9FIRM
LinkDB: A0A139CHF5_9FIRM
Original site: A0A139CHF5_9FIRM 
ID   A0A139CHF5_9FIRM        Unreviewed;       281 AA.
AC   A0A139CHF5;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=protein-glutamate O-methyltransferase {ECO:0000256|ARBA:ARBA00012534};
DE            EC=2.1.1.80 {ECO:0000256|ARBA:ARBA00012534};
GN   ORFNames=AWU54_1926 {ECO:0000313|EMBL:KXS40569.1};
OS   Candidatus Frackibacter sp. T328-2.
OC   Bacteria; Bacillota; Clostridia; Halanaerobiales; Halobacteroidaceae;
OC   Frackibacter.
OX   NCBI_TaxID=1785949 {ECO:0000313|EMBL:KXS40569.1, ECO:0000313|Proteomes:UP000070439};
RN   [1] {ECO:0000313|EMBL:KXS40569.1, ECO:0000313|Proteomes:UP000070439}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T328-2 {ECO:0000313|EMBL:KXS40569.1};
RA   Wolfe R., Daly R., Wrighton K.;
RT   "Candidatus Frackibacter-2 T328 Annotated.";
RL   Submitted (JAN-2016) 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:KXS40569.1}.
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DR   EMBL; LSBO01000129; KXS40569.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A139CHF5; -.
DR   PATRIC; fig|1785949.3.peg.2259; -.
DR   Proteomes; UP000070439; 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; 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:KXS40569.1};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KXS40569.1}.
FT   DOMAIN          1..279
FT                   /note="CheR-type methyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50123"
SQ   SEQUENCE   281 AA;  33427 MW;  0DED83B70065F290 CRC64;
     MDFRKQISDE AFDQISQLVQ QKIGLNLTKK KKAMVHSRLA KRIRKLGLDS FDEYYEFLNG
     NDSELIHLYN MLTTNVTKFF REKYHFDFLQ EEVFPQIKAD KSKKKVRIWS AGCSSGEEVY
     SLAISLKEFF NLDEWDIKIL ATDINTEVLE LAKRGIYHQR QIQPIPYKLL TKYFKLGQGQ
     NEGLFKVKNE LRNLIIFKKL NLNQNESYPI KSRLDFIFCR NVFIYFKKET RNSILDRFHR
     HLKRGGYLFL GHSESINTAG KLGRKWRLIR QTTYQKIIKD C
//
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