(data stored in SCRATCH zone)

SWISSPROT: C3MG03_SINFN

ID   C3MG03_SINFN            Unreviewed;       302 AA.
AC   C3MG03;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   07-JUN-2017, entry version 43.
DE   RecName: Full=Chemotaxis protein methyltransferase {ECO:0000256|PIRNR:PIRNR000410};
DE            EC=2.1.1.80 {ECO:0000256|PIRNR:PIRNR000410};
GN   Name=cheR {ECO:0000313|EMBL:ACP24054.1};
GN   OrderedLocusNames=NGR_c02560 {ECO:0000313|EMBL:ACP24054.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP24054.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP24054.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
CC   -!- FUNCTION: Methylation of the membrane-bound methyl-accepting
CC       chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester
CC       residues in MCP. {ECO:0000256|PIRNR:PIRNR000410}.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + protein L-glutamate
CC       = S-adenosyl-L-homocysteine + protein L-glutamate methyl ester.
CC       {ECO:0000256|PIRNR:PIRNR000410}.
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DR   EMBL; CP001389; ACP24054.1; -; Genomic_DNA.
DR   RefSeq; WP_012706839.1; NC_012587.1.
DR   RefSeq; YP_002824807.1; NC_012587.1.
DR   STRING; 394.NGR_c02560; -.
DR   EnsemblBacteria; ACP24054; ACP24054; NGR_c02560.
DR   GeneID; 7790834; -.
DR   KEGG; rhi:NGR_c02560; -.
DR   PATRIC; fig|394.7.peg.3057; -.
DR   eggNOG; ENOG4105BZU; Bacteria.
DR   eggNOG; ENOG410XNMH; LUCA.
DR   HOGENOM; HOG000254353; -.
DR   KO; K00575; -.
DR   OMA; FREEHHF; -.
DR   OrthoDB; POG091H03XG; -.
DR   Proteomes; UP000001054; Chromosome.
DR   GO; GO:0008983; F:protein-glutamate O-methyltransferase activity; IEA:UniProtKB-EC.
DR   Gene3D; 1.10.155.10; -; 1.
DR   InterPro; IPR026024; Chemotaxis_MeTrfase_CheR.
DR   InterPro; IPR022642; CheR_C.
DR   InterPro; IPR000780; CheR_MeTrfase.
DR   InterPro; IPR022641; CheR_N.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   Pfam; PF01739; CheR; 1.
DR   Pfam; PF03705; CheR_N; 1.
DR   PIRSF; PIRSF000410; CheR; 1.
DR   PRINTS; PR00996; CHERMTFRASE.
DR   SMART; SM00138; MeTrc; 1.
DR   SUPFAM; SSF47757; SSF47757; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS50123; CHER; 1.
PE   4: Predicted;
DR   PRODOM; C3MG03.
DR   SWISS-2DPAGE; C3MG03.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001054};
KW   Methyltransferase {ECO:0000256|PIRNR:PIRNR000410,
KW   ECO:0000313|EMBL:ACP24054.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001054};
KW   S-adenosyl-L-methionine {ECO:0000256|PIRNR:PIRNR000410,
KW   ECO:0000256|PIRSR:PIRSR000410-1};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000410,
KW   ECO:0000313|EMBL:ACP24054.1}.
FT   DOMAIN       17    296       CheR-type methyltransferase.
FT                                {ECO:0000259|PROSITE:PS50123}.
FT   REGION      222    223       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|PIRSR:PIRSR000410-1}.
FT   REGION      239    240       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|PIRSR:PIRSR000410-1}.
FT   BINDING      94     94       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PIRSR:PIRSR000410-1}.
FT   BINDING      96     96       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PIRSR:PIRSR000410-1}.
FT   BINDING     100    100       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PIRSR:PIRSR000410-1}.
FT   BINDING     138    138       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PIRSR:PIRSR000410-1}.
FT   BINDING     164    164       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PIRSR:PIRSR000410-1}.
SQ   SEQUENCE   302 AA;  33858 MW;  19E9B335220B9D4B CRC64;
     MRAQATFEQK LSPDECLAAG EYPLTRRDLG EIAAMIYADA GIYLNESKAS LVYSRLSKHI
     RNLGLKGFRD YCQLVASPAG AAARRDMLSH LTTNFTRFFR ENHHFEHLKT DVLPGLIARA
     KNGGRVRIWS AACSDGQEPY SIALTVLSLL PNAADYDFRI LATDIDPKIL ALARAGAYDA
     TALETVSPAM RKQWFREVDV NGRGKWQVDD RVKRLITFNE LNLMAQWPLK GPFDVIFCRN
     VVIYFDEPTQ MKIWSRFAGV LDTGGHLYIG HSERVSGDAK AIFDNIGVTT YRHTGKFHGG
     RA
//

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