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Database: UniProt
Entry: A0A192D834_9SPHN
LinkDB: A0A192D834_9SPHN
Original site: A0A192D834_9SPHN 
ID   A0A192D834_9SPHN        Unreviewed;       286 AA.
AC   A0A192D834;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Chemotaxis protein methyltransferase {ECO:0000256|PIRNR:PIRNR000410};
DE            EC=2.1.1.80 {ECO:0000256|PIRNR:PIRNR000410};
GN   ORFNames=A9D12_10050 {ECO:0000313|EMBL:ANK14275.1};
OS   Erythrobacter neustonensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX   NCBI_TaxID=1112 {ECO:0000313|EMBL:ANK14275.1, ECO:0000313|Proteomes:UP000078263};
RN   [1] {ECO:0000313|EMBL:ANK14275.1, ECO:0000313|Proteomes:UP000078263}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9434 {ECO:0000313|EMBL:ANK14275.1,
RC   ECO:0000313|Proteomes:UP000078263};
RA   Shi X.-L., Wu Y.-H., Cheng H., Xu L., Zhang X.-Q., Wang C.-S., Xu X.-W.;
RT   "Compelete Genome Sequence of Bacteriochlorophyll-Synthesizing Bacterium
RT   Porphyrobacter neustonensis DSM 9434.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Methylation of the membrane-bound methyl-accepting chemotaxis
CC       proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP.
CC       {ECO:0000256|PIRNR:PIRNR000410}.
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:0000256|ARBA:ARBA00001541,
CC         ECO:0000256|PIRNR:PIRNR000410};
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DR   EMBL; CP016033; ANK14275.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A192D834; -.
DR   STRING; 1112.A9D12_10050; -.
DR   KEGG; pns:A9D12_10050; -.
DR   Proteomes; UP000078263; Chromosome.
DR   GO; GO:0008983; F:protein-glutamate O-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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; CONSERVED HYPOTHETICAL CHEMOTAXIS PROTEIN; 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   4: Predicted;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000256|PIRNR:PIRNR000410};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078263};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PIRNR:PIRNR000410};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000410}.
FT   DOMAIN          11..285
FT                   /note="CheR-type methyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50123"
FT   BINDING         78
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
FT   BINDING         80
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
FT   BINDING         84
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
FT   BINDING         122
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
FT   BINDING         152
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
FT   BINDING         211..212
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
FT   BINDING         228..229
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
SQ   SEQUENCE   286 AA;  31484 MW;  FFEE3EF56F0A1F4E CRC64;
     MVPGVSPAIY SEADFRRISG LIHAETGIVL SDRKRMLAYS RLAPLVRRSG LTSFGAFLDT
     LDGDARLLTE VVAALTTNHT YFHREPHHFD HFETTVRPDL VRRATAGEEV RIWSAGCSTG
     EEIWTLLMVL LGADRGAGMR LAQSRLIALA SDISINALAG ARAATYPASA LEAVPEPLRR
     AWSIAAPGSG SEPRLGIDPV LQAMVRFREL NLMGEWPMRR PFDVIFCRNV MIYFDGPTKD
     RLLTRFANAL LPGGYLYIGH SERVSGPAAE LLDPVGPTIY RRREAA
//
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