ID   C5AJF7_BURGB            Unreviewed;       511 AA.
AC   C5AJF7;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=MCP methyltransferase {ECO:0000313|EMBL:ACR32037.1};
GN   OrderedLocusNames=bglu_2g16970 {ECO:0000313|EMBL:ACR32037.1};
OS   Burkholderia glumae (strain BGR1).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=626418 {ECO:0000313|EMBL:ACR32037.1, ECO:0000313|Proteomes:UP000002187};
RN   [1] {ECO:0000313|EMBL:ACR32037.1, ECO:0000313|Proteomes:UP000002187}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGR1 {ECO:0000313|EMBL:ACR32037.1,
RC   ECO:0000313|Proteomes:UP000002187};
RX   PubMed=19329631; DOI=10.1128/JB.00349-09;
RA   Lim J., Lee T.H., Nahm B.H., Choi Y.D., Kim M., Hwang I.;
RT   "Complete genome sequence of Burkholderia glumae BGR1.";
RL   J. Bacteriol. 191:3758-3759(2009).
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DR   EMBL; CP001504; ACR32037.1; -; Genomic_DNA.
DR   RefSeq; WP_015877720.1; NC_012721.2.
DR   AlphaFoldDB; C5AJF7; -.
DR   STRING; 626418.bglu_2g16970; -.
DR   KEGG; bgl:bglu_2g16970; -.
DR   PATRIC; fig|626418.3.peg.1998; -.
DR   eggNOG; COG0457; Bacteria.
DR   eggNOG; COG1352; Bacteria.
DR   HOGENOM; CLU_025854_4_0_4; -.
DR   Proteomes; UP000002187; Chromosome 2.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR022642; CheR_C.
DR   InterPro; IPR000780; CheR_MeTrfase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR24422; CHEMOTAXIS PROTEIN METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR24422:SF19; CHEMOTAXIS PROTEIN METHYLTRANSFERASE; 1.
DR   Pfam; PF01739; CheR; 1.
DR   PRINTS; PR00996; CHERMTFRASE.
DR   SMART; SM00138; MeTrc; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS50123; CHER; 1.
PE   4: Predicted;
KW   Methyltransferase {ECO:0000313|EMBL:ACR32037.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002187};
KW   Transferase {ECO:0000313|EMBL:ACR32037.1}.
FT   DOMAIN          64..266
FT                   /note="CheR-type methyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50123"
FT   REGION          309..371
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          488..511
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        488..503
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   511 AA;  54295 MW;  DEE2C9AF6F1140E8 CRC64;
     MKAAGGFEAR FHAWLSRETG IDPASLGADF VARALAERIG ATFGGDAARE LAAVARAWQP
     SPAELDAYWQ LLNASAAERH ALIELFVVPE TWFFREREAF AALAALAVER LRTRPSQPVQ
     VLSAPCSTGE EPYTAAMALI DAGLDAAQLR IDALDISARA IEHARRGEYG RNSFRGHALE
     FRARHFEPTA HGWRLHERIR DCVQFRHANL LDLDLDLDTD DASRYDFIFC RNVLIYFDRG
     AQERVLRTLD ARLADDGLLF VGPAETGVVM RYGMSSARIP LAFGFRRQAR RAAAVPAAPV
     AAGRAGFGTA PPPPVGARPT LVAPPEPAAR AGSGELARPL PGAAPRPAGA PEGGAGFAGA
     GRSGAPGRPP RAPAVLGAVA STRCSLAVPA SPAPARAGSL EAARALADAG QFEAAERAVR
     AVLDEAGPSA DAYYLLGLIA DAQGQPGAVA HYRKALYLAP THREALTHLA TLLDIAGDHE
     GARWLKERAR RADAQAGKHG EPGGRSHARR R
//