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Database: UniProt
Entry: A0A1C6LG43_9NEIS
LinkDB: A0A1C6LG43_9NEIS
Original site: A0A1C6LG43_9NEIS 
ID   A0A1C6LG43_9NEIS        Unreviewed;       286 AA.
AC   A0A1C6LG43;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Chemotaxis protein methyltransferase {ECO:0000256|PIRNR:PIRNR000410};
DE            EC=2.1.1.80 {ECO:0000256|PIRNR:PIRNR000410};
GN   ORFNames=PSELUDRAFT_0131 {ECO:0000313|EMBL:SCK05557.1};
OS   Vogesella sp. LIG4.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC   Chromobacteriaceae; Vogesella.
OX   NCBI_TaxID=1192162 {ECO:0000313|EMBL:SCK05557.1, ECO:0000313|Proteomes:UP000198213};
RN   [1] {ECO:0000313|EMBL:SCK05557.1, ECO:0000313|Proteomes:UP000198213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LIG4 {ECO:0000313|Proteomes:UP000198213};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Methylation of the membrane-bound methyl-accepting chemotaxis
CC       proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP.
CC       {ECO:0000256|PIRNR:PIRNR000410}.
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         ECO:0000256|PIRNR:PIRNR000410};
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DR   EMBL; LT607802; SCK05557.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C6LG43; -.
DR   Proteomes; UP000198213; Chromosome i.
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:SF19; 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:0000256|PIRNR:PIRNR000410};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198213};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PIRNR:PIRNR000410};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000410}.
FT   DOMAIN          14..286
FT                   /note="CheR-type methyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50123"
FT   BINDING         91
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
FT   BINDING         93
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
FT   BINDING         97
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
FT   BINDING         131
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
FT   BINDING         154
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
FT   BINDING         212..213
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
FT   BINDING         230..231
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
SQ   SEQUENCE   286 AA;  31697 MW;  003FE8D117341163 CRC64;
     MGGVLKPASD DGAIFPRDLH FSEADFHAVR SLLYDRTGIA LSDAKNHMAY ARLAKRVRHQ
     GFRSFADYLA LLHSPQGERE WEHFINALTT NLTAFFREGH HFDILRQHAR QHAGDEGGYR
     VWSSAASTGE EPYSILFTLA QSLAGGSYDI VASDIDTNVL AKAAAGVYGA DRVASLAPEL
     LRQFFVRGVG GNAGKVKVKA SYAQQIRFCR INLVDDSWPQ LGLFDVIFCR NVLIYFDKPT
     QAGIIEHFAR YLKPHGLLFL GHSENIQHIS QTFVPCGKTA YRLAGG
//
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