ID   CHER_BACSU              Reviewed;         256 AA.
AC   P31105; O32009;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   15-AUG-2003, sequence version 4.
DT   04-NOV-2026, entry version 149.
DE   RecName: Full=Chemotaxis protein methyltransferase;
DE            EC=2.1.1.80;
GN   Name=cheR; OrderedLocusNames=BSU22720;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae;
OC   Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / OI1085;
RX   PubMed=8244966; DOI=10.1016/s0021-9258(19)74398-1;
RA   Kirsch M.L., Zuberi A.R., Henner D.J., Peters P.D., Yazdi M.A., Ordal G.W.;
RT   "Chemotactic methyltransferase promotes adaptation to repellents in
RT   Bacillus subtilis.";
RL   J. Biol. Chem. 268:25350-25356(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Henner D.J.;
RT   "Sequence of Bacillus subtilis dbpA, mtr(A,B), gerC(1-3), ndk, cheR,
RT   aro(B,E,F,H), trp(A-F), hisH, and tyrA genes.";
RL   Submitted (JAN-1992) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
RP   SEQUENCE REVISION.
RX   PubMed=10568751; DOI=10.1101/gr.9.11.1116;
RA   Medigue C., Rose M., Viari A., Danchin A.;
RT   "Detecting and analyzing DNA sequencing errors: toward a higher quality of
RT   the Bacillus subtilis genome sequence.";
RL   Genome Res. 9:1116-1127(1999).
CC   -!- FUNCTION: Methylation of the membrane-bound methyl-accepting chemotaxis
CC       proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP.
CC       CheR is responsible for the chemotactic adaptation to repellents.
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   -!- SUBUNIT: Monomer.
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DR   EMBL; X73681; CAA52033.1; -; Genomic_DNA.
DR   EMBL; M80245; AAA20858.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14188.2; -; Genomic_DNA.
DR   PIR; A69599; A69599.
DR   RefSeq; NP_390153.2; NC_000964.3.
DR   RefSeq; WP_003230589.1; NC_000964.3.
DR   PDB; 5FTW; X-ray; 1.80 A; A=1-256.
DR   AlphaFoldDB; P31105; -.
DR   MDRepo; P31105; -.
DR   SMR; P31105; -.
DR   FunCoup; P31105; 257.
DR   STRING; 224308.BSU22720; -.
DR   PaxDb; 224308-BSU22720; -.
DR   EnsemblBacteria; CAB14188; CAB14188; BSU_22720.
DR   GeneID; 939003; -.
DR   KEGG; bsu:BSU22720; -.
DR   eggNOG; COG1352; Bacteria.
DR   InParanoid; P31105; -.
DR   OMA; AATFFYQ; -.
DR   OrthoDB; 9816309at2; -.
DR   PhylomeDB; P31105; -.
DR   BioCyc; BSUB:BSU22720-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0008276; F:protein methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0008983; F:protein-glutamate O-methyltransferase activity; IEA:UniProtKB-EC.
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; IPR050903; Bact_Chemotaxis_MeTrfase.
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   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   1: Evidence at protein level;
KW   3D-structure; Chemotaxis; Methyltransferase; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..256
FT                   /note="Chemotaxis protein methyltransferase"
FT                   /id="PRO_0000176030"
FT   DOMAIN          1..256
FT                   /note="CheR-type methyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00051"
FT   BINDING         67
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         69
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         73
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         107
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         130
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         185..186
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         201..202
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        154..155
FT                   /note="LS -> VC (in Ref. 1; CAA52033)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        156
FT                   /note="V -> M (in Ref. 2; AAA20858)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        256
FT                   /note="R -> KID (in Ref. 2; AAA20858)"
FT                   /evidence="ECO:0000305"
FT   HELIX           3..15
FT                   /evidence="ECO:0007829|PDB:5FTW"
FT   HELIX           19..21
FT                   /evidence="ECO:0007829|PDB:5FTW"
FT   HELIX           24..37
FT                   /evidence="ECO:0007829|PDB:5FTW"
FT   HELIX           43..52
FT                   /evidence="ECO:0007829|PDB:5FTW"
FT   HELIX           54..62
FT                   /evidence="ECO:0007829|PDB:5FTW"
FT   HELIX           75..80
FT                   /evidence="ECO:0007829|PDB:5FTW"
FT   HELIX           81..85
FT                   /evidence="ECO:0007829|PDB:5FTW"
FT   HELIX           86..89
FT                   /evidence="ECO:0007829|PDB:5FTW"
FT   STRAND          95..101
FT                   /evidence="ECO:0007829|PDB:5FTW"
FT   TURN            103..105
FT                   /evidence="ECO:0007829|PDB:5FTW"
FT   HELIX           106..116
FT                   /evidence="ECO:0007829|PDB:5FTW"
FT   STRAND          124..131
FT                   /evidence="ECO:0007829|PDB:5FTW"
FT   HELIX           133..141
FT                   /evidence="ECO:0007829|PDB:5FTW"
FT   STRAND          143..145
FT                   /evidence="ECO:0007829|PDB:5FTW"
FT   HELIX           146..148
FT                   /evidence="ECO:0007829|PDB:5FTW"
FT   HELIX           154..160
FT                   /evidence="ECO:0007829|PDB:5FTW"
FT   STRAND          161..165
FT                   /evidence="ECO:0007829|PDB:5FTW"
FT   STRAND          168..171
FT                   /evidence="ECO:0007829|PDB:5FTW"
FT   HELIX           173..176
FT                   /evidence="ECO:0007829|PDB:5FTW"
FT   STRAND          179..183
FT                   /evidence="ECO:0007829|PDB:5FTW"
FT   TURN            186..188
FT                   /evidence="ECO:0007829|PDB:5FTW"
FT   STRAND          195..200
FT                   /evidence="ECO:0007829|PDB:5FTW"
FT   HELIX           204..206
FT                   /evidence="ECO:0007829|PDB:5FTW"
FT   HELIX           209..222
FT                   /evidence="ECO:0007829|PDB:5FTW"
FT   STRAND          223..231
FT                   /evidence="ECO:0007829|PDB:5FTW"
FT   HELIX           240..243
FT                   /evidence="ECO:0007829|PDB:5FTW"
FT   STRAND          245..249
FT                   /evidence="ECO:0007829|PDB:5FTW"
FT   STRAND          252..255
FT                   /evidence="ECO:0007829|PDB:5FTW"
SQ   SEQUENCE   256 AA;  29952 MW;  A89786FF70A9F40D CRC64;
     MDTYSVFTTK WKQLTGVDLT LYKEAQMKRR LTSLYEKKGF QSFKDFAAAL EKDQALLNET
     LDRMTINVSE FYRNYKRWEV LETAILPLIK TSRPLKIWSA ACSTGEEPYT LAMLLDQQKG
     LPGYQILATD IDEKALEKAK KGVYQERSLQ EVPLSVKDRY FTQNANRSYE VKTEIKKNIT
     FKKHNLLADR YEQDFDLIVC RNVFIYFTES AKEELYLKMA HSLKKNGVLF VGSTEQIFNP
     EKFGLVPADT FFYQKR
//