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Database: UniProt
Entry: E4SFZ1_CALK2
LinkDB: E4SFZ1_CALK2
Original site: E4SFZ1_CALK2 
ID   E4SFZ1_CALK2            Unreviewed;       260 AA.
AC   E4SFZ1;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=protein-glutamate O-methyltransferase {ECO:0000256|ARBA:ARBA00012534};
DE            EC=2.1.1.80 {ECO:0000256|ARBA:ARBA00012534};
GN   OrderedLocusNames=Calkro_1820 {ECO:0000313|EMBL:ADQ46666.1};
OS   Caldicellulosiruptor kronotskyensis (strain DSM 18902 / VKM B-2412 / 2002).
OC   Bacteria; Bacillota; Clostridia; Caldicellulosiruptorales;
OC   Caldicellulosiruptoraceae; Caldicellulosiruptor.
OX   NCBI_TaxID=632348 {ECO:0000313|EMBL:ADQ46666.1, ECO:0000313|Proteomes:UP000006835};
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=2002;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA   Blumer-Schuette S.E., Kelly R.M., Woyke T.;
RT   "Complete sequence of Caldicellulosiruptor kronotskyensis 2002.";
RL   Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADQ46666.1, ECO:0000313|Proteomes:UP000006835}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18902 / VKM B-2412 / 2002
RC   {ECO:0000313|Proteomes:UP000006835};
RX   PubMed=21216991; DOI=10.1128/JB.01515-10;
RA   Blumer-Schuette S.E., Ozdemir I., Mistry D., Lucas S., Lapidus A.,
RA   Cheng J.F., Goodwin L.A., Pitluck S., Land M.L., Hauser L.J., Woyke T.,
RA   Mikhailova N., Pati A., Kyrpides N.C., Ivanova N., Detter J.C.,
RA   Walston-Davenport K., Han S., Adams M.W., Kelly R.M.;
RT   "Complete genome sequences for the anaerobic, extremely thermophilic plant
RT   biomass-degrading bacteria Caldicellulosiruptor hydrothermalis,
RT   Caldicellulosiruptor kristjanssonii, Caldicellulosiruptor kronotskyensis,
RT   Caldicellulosiruptor owensenis, and Caldicellulosiruptor lactoaceticus.";
RL   J. Bacteriol. 193:1483-1484(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; CP002330; ADQ46666.1; -; Genomic_DNA.
DR   RefSeq; WP_013430753.1; NC_014720.1.
DR   AlphaFoldDB; E4SFZ1; -.
DR   KEGG; ckn:Calkro_1820; -.
DR   PATRIC; fig|632348.3.peg.1918; -.
DR   HOGENOM; CLU_025854_1_1_9; -.
DR   OrthoDB; 9816309at2; -.
DR   Proteomes; UP000006835; 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; 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:ADQ46666.1};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ADQ46666.1}.
FT   DOMAIN          1..259
FT                   /note="CheR-type methyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50123"
SQ   SEQUENCE   260 AA;  31329 MW;  568B723CF5F4BB3F CRC64;
     MQLDYEWFKK KIWEYVGINL SYYKEKQMKR RIESLMKKNG YETFADYYNA LTKDQKLFNE
     FINYLTINVS EFYRNPQQWE ILEKEIMPYI LKRTKKPKIW SAACSTGEEP YSIVMLLTRF
     FPLSEIKILA TDIDDDAIRK AKEGVYMKKS LEGLPQEFVR RFFKENGELY YISDEIKRCV
     EFKHHDLLKD PYPKDIDLIV CRNVLIYFTE EAKDMVYRNF NMSLVMNGIL FVGSTEQIIM
     PQKYGLKPIK TFFYEKVMNI
//
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