ID   CHER_SALTY              Reviewed;         288 AA.
AC   P07801;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=Chemotaxis protein methyltransferase;
DE            EC=2.1.1.80;
GN   Name=cheR; OrderedLocusNames=STM1918;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3298235; DOI=10.1016/s0021-9258(18)47447-9;
RA   Simms S.A., Stock A.M., Stock J.B.;
RT   "Purification and characterization of the S-adenosylmethionine:glutamyl
RT   methyltransferase that modifies membrane chemoreceptor proteins in
RT   bacteria.";
RL   J. Biol. Chem. 262:8537-8543(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 11-284 IN COMPLEX WITH
RP   S-ADENOSYL-L-HOMOCYSTEINE.
RX   PubMed=9115443; DOI=10.1016/s0969-2126(97)00210-4;
RA   Djordjevic S., Stock A.M.;
RT   "Crystal structure of the chemotaxis receptor methyltransferase CheR
RT   suggests a conserved structural motif for binding S-adenosylmethionine.";
RL   Structure 5:545-558(1997).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 16-284 IN COMPLEX WITH
RP   S-ADENOSYL-L-HOMOCYSTEINE AND TAR.
RX   PubMed=9628482; DOI=10.1038/nsb0698-446;
RA   Djordjevic S., Stock A.M.;
RT   "Chemotaxis receptor recognition by protein methyltransferase CheR.";
RL   Nat. Struct. Biol. 5:446-450(1998).
CC   -!- FUNCTION: Methylation of the membrane-bound methyl-accepting chemotaxis
CC       proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP.
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;
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DR   EMBL; J02757; AAA27035.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL20834.1; -; Genomic_DNA.
DR   PIR; A29303; XYEBGM.
DR   RefSeq; NP_460875.1; NC_003197.2.
DR   RefSeq; WP_000204362.1; NC_003197.2.
DR   PDB; 1AF7; X-ray; 2.00 A; A=11-284.
DR   PDB; 1BC5; X-ray; 2.20 A; A=16-284.
DR   PDBsum; 1AF7; -.
DR   PDBsum; 1BC5; -.
DR   AlphaFoldDB; P07801; -.
DR   SMR; P07801; -.
DR   STRING; 99287.STM1918; -.
DR   DrugBank; DB01752; S-adenosyl-L-homocysteine.
DR   PaxDb; P07801; -.
DR   EnsemblBacteria; AAL20834; AAL20834; STM1918.
DR   GeneID; 1253439; -.
DR   KEGG; stm:STM1918; -.
DR   PATRIC; fig|99287.12.peg.2034; -.
DR   HOGENOM; CLU_025854_0_0_6; -.
DR   OMA; EWQEFVN; -.
DR   PhylomeDB; P07801; -.
DR   BioCyc; SENT99287:STM1918-MON; -.
DR   EvolutionaryTrace; P07801; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0008983; F:protein-glutamate O-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.155.10; -; 1.
DR   Gene3D; 3.40.50.150; -; 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   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; SSF53335; SSF53335; 1.
DR   PROSITE; PS50123; CHER; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Chemotaxis; Methyltransferase; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..288
FT                   /note="Chemotaxis protein methyltransferase"
FT                   /id="PRO_0000176039"
FT   DOMAIN          15..286
FT                   /note="CheR-type methyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00051"
FT   BINDING         92
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT   BINDING         94
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT   BINDING         98
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT   BINDING         129
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT   BINDING         154
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT   BINDING         212..213
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT   BINDING         230..231
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT   HELIX           24..38
FT                   /evidence="ECO:0007829|PDB:1AF7"
FT   HELIX           44..46
FT                   /evidence="ECO:0007829|PDB:1AF7"
FT   HELIX           47..61
FT                   /evidence="ECO:0007829|PDB:1AF7"
FT   HELIX           66..75
FT                   /evidence="ECO:0007829|PDB:1AF7"
FT   HELIX           81..89
FT                   /evidence="ECO:0007829|PDB:1AF7"
FT   TURN            96..101
FT                   /evidence="ECO:0007829|PDB:1AF7"
FT   HELIX           102..112
FT                   /evidence="ECO:0007829|PDB:1AF7"
FT   STRAND          117..122
FT                   /evidence="ECO:0007829|PDB:1AF7"
FT   TURN            125..127
FT                   /evidence="ECO:0007829|PDB:1AF7"
FT   HELIX           128..141
FT                   /evidence="ECO:0007829|PDB:1AF7"
FT   STRAND          147..155
FT                   /evidence="ECO:0007829|PDB:1AF7"
FT   HELIX           157..165
FT                   /evidence="ECO:0007829|PDB:1AF7"
FT   STRAND          167..169
FT                   /evidence="ECO:0007829|PDB:1AF7"
FT   HELIX           170..173
FT                   /evidence="ECO:0007829|PDB:1AF7"
FT   HELIX           178..184
FT                   /evidence="ECO:0007829|PDB:1AF7"
FT   STRAND          185..187
FT                   /evidence="ECO:0007829|PDB:1AF7"
FT   HELIX           190..192
FT                   /evidence="ECO:0007829|PDB:1BC5"
FT   STRAND          194..198
FT                   /evidence="ECO:0007829|PDB:1AF7"
FT   HELIX           200..203
FT                   /evidence="ECO:0007829|PDB:1AF7"
FT   STRAND          206..210
FT                   /evidence="ECO:0007829|PDB:1AF7"
FT   STRAND          224..229
FT                   /evidence="ECO:0007829|PDB:1AF7"
FT   HELIX           233..235
FT                   /evidence="ECO:0007829|PDB:1AF7"
FT   HELIX           238..248
FT                   /evidence="ECO:0007829|PDB:1AF7"
FT   HELIX           249..251
FT                   /evidence="ECO:0007829|PDB:1AF7"
FT   STRAND          252..260
FT                   /evidence="ECO:0007829|PDB:1AF7"
FT   TURN            267..269
FT                   /evidence="ECO:0007829|PDB:1AF7"
FT   STRAND          273..277
FT                   /evidence="ECO:0007829|PDB:1AF7"
FT   STRAND          280..283
FT                   /evidence="ECO:0007829|PDB:1AF7"
SQ   SEQUENCE   288 AA;  32924 MW;  4D344E6F326DD482 CRC64;
     MTSSLPSGQT SVLLQMTQRL ALSDAHFRRI CQLIYQRAGI VLADHKRDMV YNRLVRRLRA
     LGLDDFGRYL SMLEANQNSA EWQAFINALT TNLTAFFREA HHFPILAEHA RRRHGEYRVW
     SAAASTGEEP YSIAITLADA LGMAPGRWKV FASDIDTEVL EKARSGIYRL SELKTLSPQQ
     LQRYFMRGTG PHEGLVRVRQ ELANYVEFSS VNLLEKQYNV PGPFDAIFCR NVMIYFDKTT
     QEDILRRFVP LLKPDGLLFA GHSENFSNLV REFSLRGQTV YALSKDKA