ID A0A1B6BBA4_9FIRM Unreviewed; 256 AA.
AC A0A1B6BBA4;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, 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=F3D3_1594 {ECO:0000313|EMBL:GAU76995.1};
OS Fusibacter sp. 3D3.
OC Bacteria; Bacillota; Clostridia; Eubacteriales;
OC Eubacteriales Family XII. Incertae Sedis; Fusibacter.
OX NCBI_TaxID=1048380 {ECO:0000313|EMBL:GAU76995.1, ECO:0000313|Proteomes:UP000095197};
RN [1] {ECO:0000313|EMBL:GAU76995.1, ECO:0000313|Proteomes:UP000095197}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D3 {ECO:0000313|EMBL:GAU76995.1,
RC ECO:0000313|Proteomes:UP000095197};
RA Serrano A.E., Escudero L.V., Encalada O., Tebes C.J., Fernandez S.,
RA Demergasso C.S.;
RT "Draft genome sequence of Fusibacter ascotence 3D3 isolated from the high
RT arsenic level Ascotan salt flat in northern Chile.";
RL Submitted (SEP-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:GAU76995.1}.
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DR EMBL; BDHH01000005; GAU76995.1; -; Genomic_DNA.
DR RefSeq; WP_069872732.1; NZ_BDHH01000005.1.
DR AlphaFoldDB; A0A1B6BBA4; -.
DR STRING; 1048380.F3D3_1594; -.
DR OrthoDB; 9816309at2; -.
DR Proteomes; UP000095197; 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 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:GAU76995.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000095197};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:GAU76995.1}.
FT DOMAIN 1..256
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
SQ SEQUENCE 256 AA; 30718 MW; 164EA8308A55D90F CRC64;
MEGYEKFKER VFNKTKLDLT LYKERQMKRR IESLITRHGL GDFDSYFKLI DTDKDSFDEF
ITYLTINVSE FYRNPSQWET LREDVFPAIL KRNKRPKIWS AACSTGEEPY SLVMCLSEFM
PLKDIKIYAV DFDDEALSKA QMGIYSEKSI KNVPKQYVDK YFEIVGKSYR IKDEIKRCVE
FKKMNLLSDP YPKGFDMIIC RNVMIYFTEE AKDEMYKKFY DALVNDGYFF VGSTEQIIQP
QRYNFESSKT FFYYKR
//