CHER2_PSEAE
ID CHER2_PSEAE Reviewed; 280 AA.
AC Q9I6V7;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Chemotaxis protein methyltransferase 2;
DE EC=2.1.1.80 {ECO:0000269|PubMed:24714571};
GN Name=cheR2 {ECO:0000303|PubMed:24714571}; OrderedLocusNames=PA0175;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
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).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH MCPB, AND MUTAGENESIS OF
RP 186-GLY--ASN-188.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=24714571; DOI=10.1126/scisignal.2004849;
RA Garcia-Fontana C., Corral Lugo A., Krell T.;
RT "Specificity of the CheR2 methyltransferase in Pseudomonas aeruginosa is
RT directed by a C-terminal pentapeptide in the McpB chemoreceptor.";
RL Sci. Signal. 7:ra34-ra34(2014).
CC -!- FUNCTION: Methylation of the methyl-accepting chemotaxis proteins (MCP)
CC to form gamma-glutamyl methyl ester residues in MCP (PubMed:24714571).
CC It specifically targets the McpB chemoreceptor (PubMed:24714571).
CC {ECO:0000269|PubMed:24714571}.
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;
CC Evidence={ECO:0000269|PubMed:24714571};
CC -!- SUBUNIT: Interacts with the C-terminal pentapeptide GWEEF of the
CC methyl-accepting chemotaxis protein McpB.
CC {ECO:0000269|PubMed:24714571}.
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DR EMBL; AE004091; AAG03565.1; -; Genomic_DNA.
DR PIR; H83623; H83623.
DR RefSeq; NP_248865.1; NC_002516.2.
DR RefSeq; WP_003102222.1; NZ_QZGE01000015.1.
DR AlphaFoldDB; Q9I6V7; -.
DR SMR; Q9I6V7; -.
DR STRING; 287.DR97_3131; -.
DR PaxDb; Q9I6V7; -.
DR DNASU; 882282; -.
DR EnsemblBacteria; AAG03565; AAG03565; PA0175.
DR GeneID; 882282; -.
DR KEGG; pae:PA0175; -.
DR PATRIC; fig|208964.12.peg.181; -.
DR PseudoCAP; PA0175; -.
DR HOGENOM; CLU_025854_0_0_6; -.
DR InParanoid; Q9I6V7; -.
DR OMA; EWQEFVN; -.
DR PhylomeDB; Q9I6V7; -.
DR BioCyc; PAER208964:G1FZ6-176-MON; -.
DR BRENDA; 2.1.1.80; 5087.
DR Proteomes; UP000002438; Chromosome.
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; 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 1: Evidence at protein level;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..280
FT /note="Chemotaxis protein methyltransferase 2"
FT /id="PRO_0000176038"
FT DOMAIN 10..280
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00051"
FT BINDING 85
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 208..209
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 226..227
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT MUTAGEN 186..188
FT /note="Missing: Abolishes interaction with McpB and its
FT methylation."
FT /evidence="ECO:0000269|PubMed:24714571"
SQ SEQUENCE 280 AA; 32029 MW; FD2AF1491DDC57FB CRC64;
MPTSTPSPVF GNQEFHYTRE DFQQVRERLY RLTGISLAES KAQLVYSRLS RRLRLLRLGS
FAEYFTHLDR EPGEQQLFVN ALTTNLTAFF RERHHFPLLA DLARRQLQRH RPLRIWSAAA
STGEEPYSIA ITLVEALGSF DPPVKIVASD IDTGVLDCAR QGVYPLERLE QMPAPLKKRF
FLRGTGPNAG KARVVEELRQ LVEFRQINLL EADWSIAGEL DAIFCRNVMI YFDKPTQTRL
LERMVALLRP EGLFFAGHSE NFVHASHLVR SVGQTVYSPA
