ID   CHER_CAMJE              Reviewed;         262 AA.
AC   Q0P9X6; P45676; Q9PP10;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 25.
DE   RecName: Full=Chemotaxis protein methyltransferase;
DE            EC=2.1.1.80;
GN   Name=cheR; OrderedLocusNames=Cj0923c;
OS   Campylobacter jejuni.
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=197;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 11168 / Serotype O:2;
RX   MEDLINE=20150912; PubMed=10688204; DOI=10.1038/35001088;
RA   Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA   Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA   Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W.,
RA   Quail M.A., Rajandream M.A., Rutherford K.M., van Vliet A.H.M.,
RA   Whitehead S., Barrell B.G.;
RT   "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT   reveals hypervariable sequences.";
RL   Nature 403:665-668(2000).
CC   -!- FUNCTION: Methylation of the membrane-bound methyl-accepting
CC       chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester
CC       residues in MCP (By similarity).
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + protein L-glutamate
CC       = S-adenosyl-L-homocysteine + protein L-glutamate methyl ester.
CC   -!- SIMILARITY: Contains 1 cheR-type methyltransferase domain.
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DR   EMBL; AL111168; CAL35043.1; -; Genomic_DNA.
DR   PIR; B48518; B48518.
DR   PIR; B81366; B81366.
DR   RefSeq; YP_002344321.1; -.
DR   IntAct; Q0P9X6; 2.
DR   GeneID; 905222; -.
DR   GenomeReviews; AL111168_GR; Cj0923c.
DR   KEGG; cje:Cj0923c; -.
DR   HOGENOM; Q0P9X6; -.
DR   OMA; Q0P9X6; KVLNQMA.
DR   BRENDA; 2.1.1.80; 255835.
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   3: Inferred from homology;
KW   Chemotaxis; Complete proteome; Methyltransferase;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN         1    262       Chemotaxis protein methyltransferase.
FT                                /FTId=PRO_0000176032.
FT   DOMAIN        1    262       CheR-type methyltransferase.
FT   REGION      188    189       S-adenosyl-L-methionine binding (By
FT                                similarity).
FT   REGION      206    207       S-adenosyl-L-methionine binding (By
FT                                similarity).
FT   BINDING      76     76       S-adenosyl-L-methionine (By similarity).
FT   BINDING      80     80       S-adenosyl-L-methionine (By similarity).
FT   BINDING     111    111       S-adenosyl-L-methionine (By similarity).
FT   BINDING     133    133       S-adenosyl-L-methionine (By similarity).
SQ   SEQUENCE   262 AA;  30655 MW;  57B545B90AA04328 CRC64;
     MEKKITPSEL ELNEFIKIIN EMSGIDLTDK KNILALKLNK FLEGTNTKNF SEFLGKLKSN
     RQLKQETLDF VTIGETYFLR ELAQLKEIIY YAKSLEKRVN ILSAPCSSGE EVYSLALLAA
     QNFIKDMYIL GVDINSSVIE KAKLGKYQGR TLQRLSESEK RRFFLESEDK FYTINKNELC
     TCKFELCNVF EEKFSRLGKF DIIASRNMII YFDHESKLKL MERFHRILND KGRLYVGNAD
     LIPETIYFKK IFSPRGVYYE KV
//