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UniProtKB/Swiss-Prot entry P31105


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CHER_BACSU
Primary accession number P31105
Secondary accession number O32009
Integrated into Swiss-Prot on July 1, 1993
Sequence was last modified on August 15, 2003 (Sequence version 4)
Annotations were last modified on    November 4, 2008 (Entry version 64)
Name and origin of the protein
Protein name Chemotaxis protein methyltransferase
Synonym EC 2.1.1.80
Gene name
Name: cheR
OrderedLocusNames: BSU22720
From
Bacillus subtilis [TaxID: 1423] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
Protein existence 4: Predicted;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168 / OI1085;
PubMed=8244966 [NCBI, ExPASy, EBI, Israel, Japan]
Kirsch M.L., Zuberi A.R., Henner D.J., Peters P.D., Yazdi M.A., Ordal G.W.;
"Chemotactic methyltransferase promotes adaptation to repellents in Bacillus subtilis.";
J. Biol. Chem. 268:25350-25356(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Henner D.J.;
"Sequence of Bacillus subtilis dbpA, mtr(A,B), gerC(1-3), ndk, cheR, aro(B,E,F,H), trp(A-F), hisH, and tyrA genes.";
Submitted (JAN-1992) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
DOI=10.1038/36786; PubMed=9384377 [NCBI, ExPASy, EBI, Israel, Japan]
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.;
"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis.";
Nature 390:249-256(1997).
[4]
SEQUENCE REVISION.
DOI=10.1101/gr.9.11.1116; PubMed=10568751 [NCBI, ExPASy, EBI, Israel, Japan]
Medigue C., Rose M., Viari A., Danchin A.;
"Detecting and analyzing DNA sequencing errors: toward a higher quality of the Bacillus subtilis genome sequence.";
Genome Res. 9:1116-1127(1999).
Comments
  • FUNCTION: Methylation of the membrane-bound methyl-accepting chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP. CheR is responsible for the chemotactic adaptation to repellents.
  • CATALYTIC ACTIVITY: S-adenosyl-L-methionine + protein L-glutamate = S-adenosyl-L-homocysteine + protein L-glutamate methyl ester.
  • SUBUNIT: Monomer.
  • SIMILARITY: Contains 1 cheR-type methyltransferase domain.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X73681; CAA52033.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M80245; AAA20858.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z99115; CAB14188.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A69599; A69599.
RefSeq NP_390153.2; -.
3D structure databases
ModBase P31105.
Enzyme and pathway databases
BioCyc BSUB224308:BSU2271-MON; -.
Organism-specific databases
SubtiList BG10283; cheR. [Micado]
Ontologies
GO
GO:0008983; Molecular function: protein-glutamate O-methyltransferase activity (inferred from electronic annotation from EC).
GO:0006935; Biological process: chemotaxis (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR000780; CheR_MeTrfase.
Graphical view of domain structure.
Pfam PF01739; CheR; 1.
PF03705; CheR_N; 1.
Pfam graphical view of domain structure.
PRINTS PR00996; CHERMTFRASE.
SMART SM00138; MeTrc; 1.
SMART graphical view of domain structure.
PROSITE PS50123; CHER; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P31105.
ProtoNet P31105.
Genome annotation databases
GeneID 939003; -.
GenomeReviews AL009126_GR; BSU22720.
KEGG bsu:BSU22720; -.
Phylogenomic databases
HOGENOM P31105; -.
Genome annotation databases
CMR P31105; BSU22720.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Chemotaxis; Complete proteome; Methyltransferase; S-adenosyl-L-methionine; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   256  256     Chemotaxis protein methyltransferase. PRO_0000176030
DOMAIN   1   256  256     CheR-type methyltransferase. 
REGION   185   186  2     S-adenosyl-L-methionine binding (By similarity). 
REGION   201   202  2     S-adenosyl-L-methionine binding (By similarity). 
BINDING   67    67        S-adenosyl-L-methionine (By similarity). 
BINDING   69    69        S-adenosyl-L-methionine (By similarity). 
BINDING   73    73        S-adenosyl-L-methionine (By similarity). 
BINDING   107   107        S-adenosyl-L-methionine (By similarity). 
BINDING   130   130        S-adenosyl-L-methionine (By similarity). 
CONFLICT   154   155        LS -> VC (in Ref. 1; CAA52033). 
CONFLICT   156   156        V -> M (in Ref. 2; AAA20858). 
CONFLICT   256   256        R -> KID (in Ref. 2; AAA20858). 
Sequence information
Length: 256 AA [This is the length of the unprocessed precursor] Molecular weight: 29952 Da [This is the MW of the unprocessed precursor] CRC64: A89786FF70A9F40D [This is a checksum on the sequence]
        10         20         30         40         50         60 
MDTYSVFTTK WKQLTGVDLT LYKEAQMKRR LTSLYEKKGF QSFKDFAAAL EKDQALLNET 

        70         80         90        100        110        120 
LDRMTINVSE FYRNYKRWEV LETAILPLIK TSRPLKIWSA ACSTGEEPYT LAMLLDQQKG 

       130        140        150        160        170        180 
LPGYQILATD IDEKALEKAK KGVYQERSLQ EVPLSVKDRY FTQNANRSYE VKTEIKKNIT 

       190        200        210        220        230        240 
FKKHNLLADR YEQDFDLIVC RNVFIYFTES AKEELYLKMA HSLKKNGVLF VGSTEQIFNP 

       250 
EKFGLVPADT FFYQKR 

P31105 in FASTA format

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