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-2008, entry version 64. DE RecName: Full=Chemotaxis protein methyltransferase; DE EC=2.1.1.80; GN Name=cheR; OrderedLocusNames=BSU22720; OS Bacillus subtilis. OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1423; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=168 / OI1085; RX MEDLINE=94064595; PubMed=8244966; RA Kirsch M.L., Zuberi A.R., Henner D.J., Peters P.D., Yazdi M.A., RA 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 MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786; RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., RA Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., RA Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., RA Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M., RA Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., RA Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., RA Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., RA Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., RA Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., RA Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., RA Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., RA Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., RA Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., RA 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., RA Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., RA Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., RA Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., RA Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., RA Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., RA Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., RA Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., RA 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 MEDLINE=20036940; 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 RT quality of the Bacillus subtilis genome sequence."; RL Genome Res. 9:1116-1127(1999). CC -!- FUNCTION: Methylation of the membrane-bound methyl-accepting CC chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester CC residues in MCP. CheR is responsible for the chemotactic CC adaptation to repellents. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + protein L-glutamate CC = S-adenosyl-L-homocysteine + protein L-glutamate methyl ester. CC -!- SUBUNIT: Monomer. CC -!- SIMILARITY: Contains 1 cheR-type methyltransferase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X73681; CAA52033.1; -; Genomic_DNA. DR EMBL; M80245; AAA20858.1; -; Genomic_DNA. DR EMBL; Z99115; CAB14188.2; -; Genomic_DNA. DR PIR; A69599; A69599. DR RefSeq; NP_390153.2; -. DR GeneID; 939003; -. DR GenomeReviews; AL009126_GR; BSU22720. DR KEGG; bsu:BSU22720; -. DR SubtiList; BG10283; cheR. DR HOGENOM; P31105; -. DR BioCyc; BSUB224308:BSU2271-MON; -. DR GO; GO:0008983; F:protein-glutamate O-methyltransferase activity; IEA:EC. DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW. DR InterPro; IPR000780; CheR_MeTrfase. DR Pfam; PF01739; CheR; 1. DR Pfam; PF03705; CheR_N; 1. DR PRINTS; PR00996; CHERMTFRASE. DR SMART; SM00138; MeTrc; 1. DR PROSITE; PS50123; CHER; 1. PE 4: Predicted; KW Chemotaxis; Complete proteome; Methyltransferase; KW S-adenosyl-L-methionine; Transferase. FT CHAIN 1 256 Chemotaxis protein methyltransferase. FT /FTId=PRO_0000176030. FT DOMAIN 1 256 CheR-type methyltransferase. FT REGION 185 186 S-adenosyl-L-methionine binding (By FT similarity). FT REGION 201 202 S-adenosyl-L-methionine binding (By FT similarity). FT BINDING 67 67 S-adenosyl-L-methionine (By similarity). FT BINDING 69 69 S-adenosyl-L-methionine (By similarity). FT BINDING 73 73 S-adenosyl-L-methionine (By similarity). FT BINDING 107 107 S-adenosyl-L-methionine (By similarity). FT BINDING 130 130 S-adenosyl-L-methionine (By similarity). FT CONFLICT 154 155 LS -> VC (in Ref. 1; CAA52033). FT CONFLICT 156 156 V -> M (in Ref. 2; AAA20858). FT CONFLICT 256 256 R -> KID (in Ref. 2; AAA20858). 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 //