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Database: UniProt
Entry: A0A142XMB1_9BACT
LinkDB: A0A142XMB1_9BACT
Original site: A0A142XMB1_9BACT 
ID   A0A142XMB1_9BACT        Unreviewed;       347 AA.
AC   A0A142XMB1;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=protein-glutamate O-methyltransferase {ECO:0000256|ARBA:ARBA00012534};
DE            EC=2.1.1.80 {ECO:0000256|ARBA:ARBA00012534};
GN   Name=cheR {ECO:0000313|EMBL:AMV28035.1};
GN   ORFNames=VT84_26760 {ECO:0000313|EMBL:AMV28035.1};
OS   Gemmata sp. SH-PL17.
OC   Bacteria; Planctomycetota; Planctomycetia; Gemmatales; Gemmataceae;
OC   Gemmata.
OX   NCBI_TaxID=1630693 {ECO:0000313|EMBL:AMV28035.1, ECO:0000313|Proteomes:UP000076098};
RN   [1] {ECO:0000313|EMBL:AMV28035.1, ECO:0000313|Proteomes:UP000076098}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SH-PL17 {ECO:0000313|EMBL:AMV28035.1,
RC   ECO:0000313|Proteomes:UP000076098};
RA   van der Voort M., Raaijmakers J.M.;
RT   "Genome minning of novel planctomycete species.";
RL   Submitted (APR-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};
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DR   EMBL; CP011271; AMV28035.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A142XMB1; -.
DR   STRING; 1630693.VT84_26760; -.
DR   KEGG; ges:VT84_26760; -.
DR   PATRIC; fig|1630693.3.peg.5697; -.
DR   OrthoDB; 288469at2; -.
DR   Proteomes; UP000076098; Chromosome.
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:SF19; 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:AMV28035.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076098};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AMV28035.1}.
FT   DOMAIN          1..271
FT                   /note="CheR-type methyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50123"
FT   REGION          268..347
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        305..320
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   347 AA;  39463 MW;  6E162AC2BFA27CE0 CRC64;
     MREEEFAAIR QYLYDETGIS LSAGKRDMAC SRLAKRLRHF GLNSYSAYLR KVQDGDPPTE
     RQEFINCLTT NKTDFFREPH HFDFLRDTVI PQLRASGRKR LRLWCAASST GEEPYTLAMT
     LREHCPASEG WDARILASDI DTSVLAHAER GVYDLDRAGD IPPAMLHKYF LRGTGAKAGK
     ISARPELREL LTFRQINLIE EPWPIRAQFD VIFCRNVVIY FDRDTQHKLL TRFAAQLDPN
     GFLFLGHSEN IHWLADTFAP LGSTVYKMRG GTDTPPPART LPRSAARPEA APRPARRPRL
     RSRGLRKTST TSFSATSRRR AARPSSRRCS ARAWPRASTT RKRASVG
//
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