CHER_BACSU
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 03-AUG-2022, entry version 133.
DE RecName: Full=Chemotaxis protein methyltransferase;
DE EC=2.1.1.80;
GN Name=cheR; OrderedLocusNames=BSU22720;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; 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; NZ_JNCM01000036.1.
DR PDB; 5FTW; X-ray; 1.80 A; A=1-256.
DR PDBsum; 5FTW; -.
DR AlphaFoldDB; P31105; -.
DR SMR; P31105; -.
DR STRING; 224308.BSU22720; -.
DR PaxDb; P31105; -.
DR PRIDE; P31105; -.
DR EnsemblBacteria; CAB14188; CAB14188; BSU_22720.
DR GeneID; 939003; -.
DR KEGG; bsu:BSU22720; -.
DR eggNOG; COG1352; Bacteria.
DR InParanoid; P31105; -.
DR OMA; EWQEFVN; -.
DR PhylomeDB; P31105; -.
DR BioCyc; BSUB:BSU22720-MON; -.
DR Proteomes; UP000001570; 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; 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 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..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..84
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
