CHER_KLEAK
ID CHER_KLEAK Reviewed; 290 AA.
AC P21824; G0DZQ8;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Chemotaxis protein methyltransferase;
DE EC=2.1.1.80;
GN Name=cheR; OrderedLocusNames=EAE_15545;
OS Klebsiella aerogenes (strain ATCC 13048 / DSM 30053 / CCUG 1429 / JCM 1235
OS / KCTC 2190 / NBRC 13534 / NCIMB 10102 / NCTC 10006 / CDC 819-56)
OS (Enterobacter aerogenes).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=1028307;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13048 / DSM 30053 / CCUG 1429 / JCM 1235 / KCTC 2190 / NBRC
RC 13534 / NCIMB 10102 / NCTC 10006 / CDC 819-56;
RX PubMed=22493190; DOI=10.1128/jb.00028-12;
RA Shin S.H., Kim S., Kim J.Y., Lee S., Um Y., Oh M.K., Kim Y.R., Lee J.,
RA Yang K.S.;
RT "Complete genome sequence of Enterobacter aerogenes KCTC 2190.";
RL J. Bacteriol. 194:2373-2374(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-100.
RC STRAIN=ATCC 13048 / DSM 30053 / CCUG 1429 / JCM 1235 / KCTC 2190 / NBRC
RC 13534 / NCIMB 10102 / NCTC 10006 / CDC 819-56;
RX PubMed=2496104; DOI=10.1128/jb.171.5.2361-2371.1989;
RA Dahl M.K., Boos W., Manson M.D.;
RT "Evolution of chemotactic-signal transducers in enteric bacteria.";
RL J. Bacteriol. 171:2361-2371(1989).
CC -!- FUNCTION: Methylation of the membrane-bound methyl-accepting chemotaxis
CC proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamyl-[protein] + S-adenosyl-L-methionine = [protein]-L-
CC glutamate 5-O-methyl ester + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:24452, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:10311,
CC ChEBI:CHEBI:29973, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:82795; EC=2.1.1.80;
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DR EMBL; CP002824; AEG98020.1; -; Genomic_DNA.
DR EMBL; M26411; AAA24799.1; -; Genomic_DNA.
DR PIR; E32302; E32302.
DR RefSeq; WP_015367340.1; NC_015663.1.
DR RefSeq; YP_004593299.1; NC_015663.1.
DR AlphaFoldDB; P21824; -.
DR SMR; P21824; -.
DR STRING; 1028307.EAE_15545; -.
DR EnsemblBacteria; AEG98020; AEG98020; EAE_15545.
DR GeneID; 66604599; -.
DR KEGG; eae:EAE_15545; -.
DR PATRIC; fig|1028307.3.peg.3109; -.
DR eggNOG; COG1352; Bacteria.
DR HOGENOM; CLU_025854_0_0_6; -.
DR OMA; EWQEFVN; -.
DR Proteomes; UP000008881; Chromosome.
DR GO; GO:0008983; F:protein-glutamate O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.155.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR026024; Chemotaxis_MeTrfase_CheR.
DR InterPro; IPR022642; CheR_C.
DR InterPro; IPR000780; CheR_MeTrfase.
DR InterPro; IPR022641; CheR_N.
DR InterPro; IPR036804; CheR_N_sf.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
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; SSF53335; SSF53335; 1.
DR PROSITE; PS50123; CHER; 1.
PE 4: Predicted;
KW Chemotaxis; Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..290
FT /note="Chemotaxis protein methyltransferase"
FT /id="PRO_0000176034"
FT DOMAIN 18..289
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00051"
FT BINDING 95
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 215..216
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 233..234
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT CONFLICT 4..7
FT /note="TTST -> DDIN (in Ref. 2; AAA24799)"
FT /evidence="ECO:0000305"
FT CONFLICT 16
FT /note="L -> V (in Ref. 2; AAA24799)"
FT /evidence="ECO:0000305"
FT CONFLICT 47
FT /note="A -> P (in Ref. 2; AAA24799)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 290 AA; 32828 MW; E98A1462BFC74CD5 CRC64;
MKQTTSTAAR ESGSALAQMA QRLPLSDAHF RRISQLIYQR AGIVLAAHKR EMVYNRLVRR
LRLLGIHDFG DYLALLESDP HSAEWQAFIN ALTTNLTAFF REAHHFPILA EHARSRPGNY
SVWSTAASTG EEPYSIAITL GDALGERAGS CQVWASDIDT QVLEKAEAGI YRHEDLRTLT
PIQMQRYFLR GTGPHQGLVR VRQELAARVN FQPLNLLAAE WALPGPFDAI FCRNVMIYFD
KPTQERILRR FVPLLKPGGL LFAGHSENFS QISRDFYLRG QTVYGLTKEK
