CHER1_VIBCH
ID CHER1_VIBCH Reviewed; 275 AA.
AC Q9KQ06; Q9XCL5;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Chemotaxis protein methyltransferase 1;
DE EC=2.1.1.80;
GN Name=cheR1; Synonyms=cheR; OrderedLocusNames=VC_2201;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 10-266.
RC STRAIN=CVD110;
RX PubMed=10400589; DOI=10.1128/jb.181.14.4308-4317.1999;
RA O'Toole R., Lundberg S., Fredriksson S.A., Jansson A., Nilsson B.,
RA Wolf-Watz H.;
RT "The chemotactic response of Vibrio anguillarum to fish intestinal mucus is
RT mediated by a combination of multiple mucus components.";
RL J. Bacteriol. 181:4308-4317(1999).
CC -!- FUNCTION: Methylation of the membrane-bound methyl-accepting chemotaxis
CC proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP.
CC {ECO:0000250}.
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; AE003852; AAF95346.1; -; Genomic_DNA.
DR EMBL; AF139167; AAD45254.1; -; Genomic_DNA.
DR PIR; H82106; H82106.
DR RefSeq; NP_231832.1; NC_002505.1.
DR RefSeq; WP_000125387.1; NZ_LT906614.1.
DR AlphaFoldDB; Q9KQ06; -.
DR SMR; Q9KQ06; -.
DR STRING; 243277.VC_2201; -.
DR DNASU; 2613241; -.
DR EnsemblBacteria; AAF95346; AAF95346; VC_2201.
DR GeneID; 57740827; -.
DR KEGG; vch:VC_2201; -.
DR PATRIC; fig|243277.26.peg.2098; -.
DR eggNOG; COG1352; Bacteria.
DR HOGENOM; CLU_025854_0_2_6; -.
DR OMA; MWQLNAD; -.
DR BioCyc; VCHO:VC2201-MON; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0008983; F:protein-glutamate O-methyltransferase activity; IEA:UniProtKB-EC.
DR Gene3D; 1.10.155.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
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 PRINTS; PR00996; CHERMTFRASE.
DR SMART; SM00138; MeTrc; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS50123; CHER; 1.
PE 3: Inferred from homology;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..275
FT /note="Chemotaxis protein methyltransferase 1"
FT /id="PRO_0000176042"
FT DOMAIN 1..275
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00051"
FT BINDING 76
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 117
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 201..202
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 218..219
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
SQ SEQUENCE 275 AA; 30871 MW; F008ADCBFA46A921 CRC64;
MTAITISDQE YRDFCRFLES QCGIVLGDSK QYLVRSRLSP LVTKFKLSSL SDLLRDVVTG
RNRDLRVAAV DAMTTNETLW FRDSYPFTVL ADKLLPEMAA NKRPIKIWSA ASSSGQEPYS
MAMTILEVQQ KRPGLLPSVS ITATDISASM LDMCRAGIYD NLALGRGLSP ERRRVFFEDA
GDGRMKVKDN VKRLVNFRPQ NLMESYSLLG KFDIIFCRNV LIYFSPDMKS KVLNQMAASL
NPGGYLLLGA SESLTGLTDK FEMVRCNPGI IYKLK
