ID F7XT66_TREPU Unreviewed; 303 AA.
AC F7XT66;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
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:AEH40563.1};
GN OrderedLocusNames=TPCCA_0630 {ECO:0000313|EMBL:AEH40563.1};
OS Treponema paraluiscuniculi (strain Cuniculi A).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC Treponema.
OX NCBI_TaxID=545776 {ECO:0000313|EMBL:AEH40563.1, ECO:0000313|Proteomes:UP000008317};
RN [1] {ECO:0000313|EMBL:AEH40563.1, ECO:0000313|Proteomes:UP000008317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cuniculi A {ECO:0000313|EMBL:AEH40563.1,
RC ECO:0000313|Proteomes:UP000008317};
RX PubMed=21655244; DOI=10.1371/journal.pone.0020415;
RA Smajs D., Zobanikova M., Strouhal M., Cejkova D., Dugan-Rocha S.,
RA Pospisilova P., Norris S.J., Albert T., Qin X., Hallsworth-Pepin K.,
RA Buhay C., Muzny D.M., Chen L., Gibbs R.A., Weinstock G.M.;
RT "Complete genome sequence of Treponema paraluiscuniculi, strain Cuniculi A:
RT the loss of infectivity to humans is associated with genome decay.";
RL PLoS ONE 6:E20415-E20415(2011).
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; CP002103; AEH40563.1; -; Genomic_DNA.
DR AlphaFoldDB; F7XT66; -.
DR KEGG; tpl:TPCCA_0630; -.
DR PATRIC; fig|545776.3.peg.633; -.
DR HOGENOM; CLU_025854_1_1_12; -.
DR Proteomes; UP000008317; Chromosome.
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; 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:SF25; 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:AEH40563.1};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AEH40563.1}.
FT DOMAIN 26..294
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
SQ SEQUENCE 303 AA; 34501 MW; 406A7F29E487D772 CRC64;
MTAATEKSDI TRSYLTLGKG VRPMSTLSDA EFAAFKTLIY EHSGITFSAL NRSVLESRIR
SRLRELALPS ACAYYQQVLA SSAELSALLD SVTTNLTRFF RNKAHFDSFS HYVIPELVKA
KRSVGEHSIT VWSAGCSTGE EPYTIAMLLK RYAPAAFSCQ VIASDLSLKS LLVARQGYYP
RARVSGVPDE YLRAYFRETQ EGYQINADIR KMVRFDYHNL KHRSMHRNID VLFCRNVLIY
FDETAQKAVI ERFWDAMSAH SFLFIGHSES LFGMNTKFSF LKTPWGCLYQ KNDEGSAHEC
HTR
//
