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Database: UniProt
Entry: A0A2K8U2U1_9GAMM
LinkDB: A0A2K8U2U1_9GAMM
Original site: A0A2K8U2U1_9GAMM 
ID   A0A2K8U2U1_9GAMM        Unreviewed;       644 AA.
AC   A0A2K8U2U1;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=protein-glutamate O-methyltransferase {ECO:0000256|ARBA:ARBA00012534};
DE            EC=2.1.1.80 {ECO:0000256|ARBA:ARBA00012534};
GN   ORFNames=THSYN_01965 {ECO:0000313|EMBL:AUB79845.1};
OS   Candidatus Thiodictyon syntrophicum.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Thiodictyon.
OX   NCBI_TaxID=1166950 {ECO:0000313|EMBL:AUB79845.1, ECO:0000313|Proteomes:UP000232638};
RN   [1] {ECO:0000313|EMBL:AUB79845.1, ECO:0000313|Proteomes:UP000232638}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cad16T {ECO:0000313|EMBL:AUB79845.1,
RC   ECO:0000313|Proteomes:UP000232638};
RA   Luedin S.M., Pothier J.F., Danza F., Storelli N., Wittwer M., Tonolla M.;
RT   "Complete genome sequence of Candidatus 'Thiodictyon syntrophicum' sp. nov.
RT   strain Cad16T, a photolithoautotroph purple sulfur bacterium isolated from
RT   an alpine meromictic lake.";
RL   Submitted (MAR-2017) 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; CP020370; AUB79845.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K8U2U1; -.
DR   KEGG; tsy:THSYN_01965; -.
DR   OrthoDB; 9816309at2; -.
DR   Proteomes; UP000232638; 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; 3.40.50.150; 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; 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   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; 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   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00050};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Reference proteome {ECO:0000313|Proteomes:UP000232638};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          41..230
FT                   /note="CheB-type methylesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50122"
FT   DOMAIN          249..511
FT                   /note="CheR-type methyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50123"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..34
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        53
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT   ACT_SITE        80
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT   ACT_SITE        172
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ   SEQUENCE   644 AA;  69641 MW;  D84CD3B41255DAC8 CRC64;
     MKKVAAPAKG QSTAASPSSA QPPPGAPAAS PLVAPDDAPP LDQGFPIVGI GASAGGLEAL
     ELFLGAVPPA CGLAFIVVQH LDPTYQGNMA ALLQRVTAMP VAQITDRLKV APGHVYVIPP
     NRDLSILHGV LHLLEPVAPR GLRLPIDFFL RALAEDQHEH GLGVILSGMG SDGSLGLRAI
     KERGGAVFVQ DPASARFDSM PRSAIAAGLA DVIAPAEELA GRILAYLKHL SPLVLPSDLT
     LADPNQSGLE KVVVLLRTRA GHDFSAYKKS TLYRRIERRM GLHQLDRIAD YVHYLRENPQ
     ELDLLFKELL IGVTSFFRDP AVWEQLKTTV IPGLLAAHPD GATLRLWSAG CSTGEEAYSL
     AIILHEALEQ VQLPVRFAFQ VFATDLDRDA IDKARVGSYP ANISADCSAE RLERFFVQDD
     HGYRVKKDIR EMLIFATQNL VMDPPFTRLD LLVCRNLLIY IDASLQKKLI PLFHYSLNPG
     GILVLGNSET IGQHQDLFTP LPGKTRIYQR RAVARGNTVE FPSVFAPAPA AVRPPTAPVP
     LSALSLQSLI EPLLLRHYGP AAVLTTEQGD LVYISGKTGR YLEPAVGKVD LNLFAMARDG
     LKTALSEVFH KAVRQQAGIS VKAVKVTGTD GDRLVDLTQG NRIR
//
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