ID W0E653_MARPU Unreviewed; 977 AA.
AC W0E653;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=protein-glutamate O-methyltransferase {ECO:0000256|ARBA:ARBA00012534};
DE EC=2.1.1.80 {ECO:0000256|ARBA:ARBA00012534};
GN ORFNames=MARPU_15205 {ECO:0000313|EMBL:AHF05038.1};
OS Marichromatium purpuratum 984.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Marichromatium.
OX NCBI_TaxID=765910 {ECO:0000313|EMBL:AHF05038.1, ECO:0000313|Proteomes:UP000005275};
RN [1] {ECO:0000313|EMBL:AHF05038.1, ECO:0000313|Proteomes:UP000005275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=984 {ECO:0000313|EMBL:AHF05038.1,
RC ECO:0000313|Proteomes:UP000005275};
RG DOE Joint Genome Institute;
RA Bryant D.A., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
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};
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DR EMBL; CP007031; AHF05038.1; -; Genomic_DNA.
DR RefSeq; WP_005225064.1; NZ_CP007031.1.
DR AlphaFoldDB; W0E653; -.
DR STRING; 765910.MARPU_15205; -.
DR KEGG; mpur:MARPU_15205; -.
DR eggNOG; COG1352; Bacteria.
DR eggNOG; COG2201; Bacteria.
DR HOGENOM; CLU_000892_0_1_6; -.
DR OrthoDB; 9816309at2; -.
DR Proteomes; UP000005275; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro.
DR GO; GO:0008984; F:protein-glutamate methylesterase activity; IEA:InterPro.
DR GO; GO:0008983; F:protein-glutamate O-methyltransferase activity; IEA:RHEA.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-UniRule.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd16434; CheB-CheR_fusion; 1.
DR Gene3D; 1.10.155.10; Chemotaxis receptor methyltransferase CheR, N-terminal domain; 1.
DR Gene3D; 3.40.50.180; Methylesterase CheB, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR035909; CheB_C.
DR InterPro; IPR022642; CheR_C.
DR InterPro; IPR000780; CheR_MeTrfase.
DR InterPro; IPR022641; CheR_N.
DR InterPro; IPR036804; CheR_N_sf.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR000673; Sig_transdc_resp-reg_Me-estase.
DR PANTHER; PTHR24422; CHEMOTAXIS PROTEIN METHYLTRANSFERASE; 1.
DR PANTHER; PTHR24422:SF25; CHEMOTAXIS PROTEIN METHYLTRANSFERASE; 1.
DR Pfam; PF01339; CheB_methylest; 1.
DR Pfam; PF01739; CheR; 1.
DR Pfam; PF03705; CheR_N; 1.
DR Pfam; PF13596; PAS_10; 1.
DR Pfam; PF08448; PAS_4; 1.
DR PRINTS; PR00996; CHERMTFRASE.
DR SMART; SM00138; MeTrc; 1.
DR SUPFAM; SSF47757; Chemotaxis receptor methyltransferase CheR, N-terminal domain; 1.
DR SUPFAM; SSF52738; Methylesterase CheB, C-terminal domain; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS50122; CHEB; 1.
DR PROSITE; PS50123; CHER; 1.
PE 4: Predicted;
KW Chemotaxis {ECO:0000256|PROSITE-ProRule:PRU00050};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00050};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000005275};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 19..206
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT DOMAIN 232..488
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT REGION 494..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 653..722
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 30
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 57
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 148
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 977 AA; 108115 MW; F011BD0BD098B3CF CRC64;
MSSVSETTQD TTGPRGADGY DGYVVAIGAS AGGLDALERF FQCLPSDSGA AYVVIQHLSP
DHKSMMGNLL ARHTEMPVVT VTDAMRLEPN RVHLIPPANM MTVRGDALRL SPKNPRGLTL
PIDLFFTSLA KEFGKHAIGV VLSGTGSDGT RGAVAINDAG GMLLAQDPES AKFDGMPRSV
IATGLVDATL SPDDLGPRLI EFITQAPQIK TENPPQDPTF DKEDALEEAM HLLKHQGGIN
FRDYKPATVM RRIERRMQVR HTPDLHSYVR LLDSDRGELA VLRRELLIPV TSFFRDPDTF
EILDQTVIRS IVSERGENQP IRVWVPGVST GEEAYTLAIL FAEAFERERH WPSFKLFATD
VEQQNVEIGG AGVFSEAIAA EISPERLERF FYKRGNHFVV KNEIRQNIVF ARHNLLEDPP
FTRMDLVTCR NLLIYFRTQA QERALRRIQY ALSPGGYLLL GPSETLADLH TDFTAVNSRH
KIYRVLRHVS LPLDTATPSR PPASAAESRH YSQRSRHQST DAAAIDAGQS ILLRDYAPTT
LLLNAHGELL HVFGEAARYL RIGEGSATLD IAKLLPQPLV PVAQALLYKC ARSGTAMRSD
QLGIELPSGE HERLRMAVRP YDAPQSERHL LLSFESEPQE VIPRQGMETL DLDDETAQRV
ENLERELAAT RESLQATIEE LETANEELQA TNEELMASNE ELQSSNEELQ SVNEELYTVN
AENQEKIEIL NRLNADLDGM AKAAAIATVF VDAELRLTRF TPEATTLFKI RNGDLGRPID
DFTNLLQYPD FIDELRRTIA SGEMLQREIA AANSRIYLAR VLPYAVRAGE ARGAVATFVD
ITSLHDIERL QAVLDSLPEQ IAVLDPQGIV TQINRSWREA ARHAGDPSLS DTGPGAGYER
ALQLLGPDGE HPCGRELRAG IRAVLEGHSP AVVVDFATTD EPPTRLAIHV SPIQHHDGGA
VLARLDASEW HPHEAED
//
