ID B7GHQ1_ANOFW Unreviewed; 293 AA.
AC B7GHQ1;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 60.
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:ACJ33473.1};
GN OrderedLocusNames=Aflv_1097 {ECO:0000313|EMBL:ACJ33473.1};
OS Anoxybacillus flavithermus (strain DSM 21510 / WK1).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX NCBI_TaxID=491915 {ECO:0000313|EMBL:ACJ33473.1, ECO:0000313|Proteomes:UP000000742};
RN [1] {ECO:0000313|EMBL:ACJ33473.1, ECO:0000313|Proteomes:UP000000742}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21510 / WK1 {ECO:0000313|Proteomes:UP000000742};
RX PubMed=19014707; DOI=10.1186/gb-2008-9-11-r161;
RA Saw J.H., Mountain B.W., Feng L., Omelchenko M.V., Hou S., Saito J.A.,
RA Stott M.B., Li D., Zhao G., Wu J., Galperin M.Y., Koonin E.V.,
RA Makarova K.S., Wolf Y.I., Rigden D.J., Dunfield P.F., Wang L., Alam M.;
RT "Encapsulated in silica: genome, proteome and physiology of the
RT thermophilic bacterium Anoxybacillus flavithermus WK1.";
RL Genome Biol. 9:R161.1-R161.16(2008).
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; CP000922; ACJ33473.1; -; Genomic_DNA.
DR AlphaFoldDB; B7GHQ1; -.
DR STRING; 491915.Aflv_1097; -.
DR KEGG; afl:Aflv_1097; -.
DR eggNOG; COG1352; Bacteria.
DR HOGENOM; CLU_025854_1_1_9; -.
DR Proteomes; UP000000742; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:ACJ33473.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000742};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ACJ33473.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 40..293
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
SQ SEQUENCE 293 AA; 34561 MW; 1027AA7652B36B67 CRC64;
MGILKKVGTC LSLFFYFCFF TFSLYCMYER KGRGVFCMSD YQQFIANVKR KTGIDLALYK
EAQMKRRLTS LYEKKGFKNF DEFFRAMNHD QALFHEFLDR MTINVSEFFR NAKRWEVLEK
KIIPKLLEKN KRLKVWSAAC STGEEPYTLA IILSKFMPLS QVSVLATDID DNAMARAKLG
IYTERSLQEV PEDVKKKFFV KEGSHYKIID DIKRTVTFKK HNLLADPFDT NFDLIVCRNV
LIYFTEEAKH ELYLKFNRAL RPGGIFFVGS TEQIFNPTAY GFEVEDTFFY RKM
//
