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Database: UniProt
Entry: A0A0S2K5B8_9GAMM
LinkDB: A0A0S2K5B8_9GAMM
Original site: A0A0S2K5B8_9GAMM 
ID   A0A0S2K5B8_9GAMM        Unreviewed;       270 AA.
AC   A0A0S2K5B8;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Chemotaxis protein methyltransferase {ECO:0000256|PIRNR:PIRNR000410};
DE            EC=2.1.1.80 {ECO:0000256|PIRNR:PIRNR000410};
GN   ORFNames=PP2015_3040 {ECO:0000313|EMBL:ALO43521.1};
OS   Pseudoalteromonas phenolica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=161398 {ECO:0000313|EMBL:ALO43521.1, ECO:0000313|Proteomes:UP000061457};
RN   [1] {ECO:0000313|EMBL:ALO43521.1, ECO:0000313|Proteomes:UP000061457}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 12086 {ECO:0000313|EMBL:ALO43521.1,
RC   ECO:0000313|Proteomes:UP000061457};
RA   Zhang Y., Guo Z.;
RL   Submitted (NOV-2015) 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; CP013187; ALO43521.1; -; Genomic_DNA.
DR   RefSeq; WP_058031176.1; NZ_PNBV01000012.1.
DR   AlphaFoldDB; A0A0S2K5B8; -.
DR   STRING; 161398.PP2015_3040; -.
DR   KEGG; pphe:PP2015_3040; -.
DR   PATRIC; fig|161398.10.peg.3098; -.
DR   OrthoDB; 9761808at2; -.
DR   Proteomes; UP000061457; Chromosome I.
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:SF19; 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   4: Predicted;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000256|PIRNR:PIRNR000410};
KW   Reference proteome {ECO:0000313|Proteomes:UP000061457};
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          1..270
FT                   /note="CheR-type methyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50123"
FT   BINDING         75
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
FT   BINDING         77
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
FT   BINDING         81
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
FT   BINDING         119
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
FT   BINDING         143
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
FT   BINDING         199..200
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
FT   BINDING         216..217
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
SQ   SEQUENCE   270 AA;  31475 MW;  B41774E4170EC2F0 CRC64;
     MREFALSEQD FQTIAQKVYR SCGIVLGPHK REMVYSRLAR RIRANQLDSF SAYLNFLEEN
     EEHEFSQFIN AITTNLTSFF RENHHFEFLS NTLIPRLIER NKASKRIRIW SAGCSTGEEP
     YSIAMTIANR FPSDWDVKIL ATDLDSNVLA KAQSGVYDAG NVTGLDDDIL KKWFLKSPDN
     HAYKVKQNLQ SLIFFKRLNL LEKWPMKGPF DVIFCRNVLI YFDKETKDKL FKGYHQMLGA
     DGHLFIGHSE TMGKEHHEFK NLGRTMYQKV
//
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