ID CHER1_PSEAE Reviewed; 274 AA.
AC O87131;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 27-MAR-2024, entry version 123.
DE RecName: Full=Chemotaxis protein methyltransferase 1;
DE EC=2.1.1.80;
GN Name=cheR1; OrderedLocusNames=PA3348;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RA Kato J., Nakamura T., Kuroda A., Ohtake H.;
RT "Cloning, sequence and characterization of chemotaxis genes in Pseudomonas
RT aeruginosa.";
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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; AB012768; BAA33556.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG06736.1; -; Genomic_DNA.
DR PIR; A83227; A83227.
DR RefSeq; NP_252038.1; NC_002516.2.
DR RefSeq; WP_003091728.1; NZ_QZGE01000017.1.
DR PDB; 5XLX; X-ray; 1.97 A; A/B/C/D=1-274.
DR PDB; 5XLY; X-ray; 1.76 A; A=1-274.
DR PDB; 5Y4R; X-ray; 2.30 A; A/B=2-274.
DR PDB; 5Y4S; X-ray; 3.40 A; A/B/C/D/E/F/G/H/I/J=2-274.
DR PDBsum; 5XLX; -.
DR PDBsum; 5XLY; -.
DR PDBsum; 5Y4R; -.
DR PDBsum; 5Y4S; -.
DR AlphaFoldDB; O87131; -.
DR SMR; O87131; -.
DR STRING; 208964.PA3348; -.
DR PaxDb; 208964-PA3348; -.
DR DNASU; 882515; -.
DR GeneID; 882515; -.
DR KEGG; pae:PA3348; -.
DR PATRIC; fig|208964.12.peg.3507; -.
DR PseudoCAP; PA3348; -.
DR HOGENOM; CLU_025854_0_2_6; -.
DR InParanoid; O87131; -.
DR OrthoDB; 9816309at2; -.
DR PhylomeDB; O87131; -.
DR BioCyc; PAER208964:G1FZ6-3412-MONOMER; -.
DR PHI-base; PHI:9031; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0008983; F:protein-glutamate O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 1.10.155.10; Chemotaxis receptor methyltransferase CheR, N-terminal domain; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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 PANTHER; PTHR24422; CHEMOTAXIS PROTEIN METHYLTRANSFERASE; 1.
DR PANTHER; PTHR24422:SF25; CHEMOTAXIS PROTEIN METHYLTRANSFERASE; 1.
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; Chemotaxis receptor methyltransferase CheR, N-terminal domain; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS50123; CHER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..274
FT /note="Chemotaxis protein methyltransferase 1"
FT /id="PRO_0000176037"
FT DOMAIN 1..274
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00051"
FT BINDING 72
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 74
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 115
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 200..201
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 217..218
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT HELIX 6..19
FT /evidence="ECO:0007829|PDB:5XLY"
FT HELIX 28..42
FT /evidence="ECO:0007829|PDB:5XLY"
FT HELIX 47..53
FT /evidence="ECO:0007829|PDB:5XLY"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:5XLY"
FT HELIX 61..69
FT /evidence="ECO:0007829|PDB:5XLY"
FT TURN 76..79
FT /evidence="ECO:0007829|PDB:5XLY"
FT HELIX 81..88
FT /evidence="ECO:0007829|PDB:5XLY"
FT HELIX 90..95
FT /evidence="ECO:0007829|PDB:5XLY"
FT STRAND 103..108
FT /evidence="ECO:0007829|PDB:5XLY"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:5XLX"
FT HELIX 114..129
FT /evidence="ECO:0007829|PDB:5XLY"
FT STRAND 138..144
FT /evidence="ECO:0007829|PDB:5XLY"
FT HELIX 148..155
FT /evidence="ECO:0007829|PDB:5XLY"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:5XLY"
FT HELIX 160..163
FT /evidence="ECO:0007829|PDB:5XLY"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:5XLY"
FT HELIX 169..175
FT /evidence="ECO:0007829|PDB:5XLY"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:5XLY"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:5XLY"
FT HELIX 188..192
FT /evidence="ECO:0007829|PDB:5XLY"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:5XLY"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:5XLY"
FT STRAND 211..215
FT /evidence="ECO:0007829|PDB:5XLY"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:5XLY"
FT HELIX 225..238
FT /evidence="ECO:0007829|PDB:5XLY"
FT STRAND 239..246
FT /evidence="ECO:0007829|PDB:5XLY"
FT TURN 257..259
FT /evidence="ECO:0007829|PDB:5XLY"
FT STRAND 260..264
FT /evidence="ECO:0007829|PDB:5XLY"
FT STRAND 266..273
FT /evidence="ECO:0007829|PDB:5XLY"
SQ SEQUENCE 274 AA; 30647 MW; 9B5DD76DFD2012BF CRC64;
MSAANADFEL FRVFLEKTCG IVLGSNKQYL VSSRLNKLME QQGIKSLGEL VQRIQTQRGG
LREMVVDAMT TNETLWFRDT YPFEVLKQRV LPELIKANGG QRLRIWSAAC SSGQEPYSLS
MAIDEFEKTN LGQLKAGVQI VATDLSGSML TAAKAGEYDT LAMGRGLSPE RLQRYFDAKG
PGRWAVKPAI RSRVEFRALN LLDSYASLGK FDMVFCRNVL IYFSAEVKRD ILLRIHGTLK
PGGYLFLGAS EALNNLPDHY QMVQCSPGII YRAK
//
