ID L0H0E3_9GAMM Unreviewed; 980 AA.
AC L0H0E3;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=protein-glutamate O-methyltransferase {ECO:0000256|ARBA:ARBA00012534};
DE EC=2.1.1.80 {ECO:0000256|ARBA:ARBA00012534};
GN ORFNames=Thimo_2816 {ECO:0000313|EMBL:AGA91522.1};
OS Thioflavicoccus mobilis 8321.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thioflavicoccus.
OX NCBI_TaxID=765912 {ECO:0000313|EMBL:AGA91522.1, ECO:0000313|Proteomes:UP000010816};
RN [1] {ECO:0000313|EMBL:AGA91522.1, ECO:0000313|Proteomes:UP000010816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8321 {ECO:0000313|EMBL:AGA91522.1,
RC ECO:0000313|Proteomes:UP000010816};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Lu M., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Vogl K., Liu Z., Imhoff J.,
RA Thiel V., Frigaard N.-U., Bryant D., Woyke T.;
RT "Complete sequence of chromosome of Thioflavicoccus mobilis 8321.";
RL Submitted (SEP-2011) 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; CP003051; AGA91522.1; -; Genomic_DNA.
DR RefSeq; WP_015281654.1; NC_019940.1.
DR AlphaFoldDB; L0H0E3; -.
DR STRING; 765912.Thimo_2816; -.
DR KEGG; tmb:Thimo_2816; -.
DR PATRIC; fig|765912.4.peg.2760; -.
DR eggNOG; COG1196; Bacteria.
DR eggNOG; COG1352; Bacteria.
DR eggNOG; COG2201; Bacteria.
DR HOGENOM; CLU_000892_0_1_6; -.
DR OrthoDB; 9816309at2; -.
DR Proteomes; UP000010816; 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 CDD; cd00130; PAS; 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; IPR000014; PAS.
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 SMART; SM00091; PAS; 2.
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 ECO:0000313|EMBL:AGA91522.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010816};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 17..210
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT DOMAIN 230..470
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 666..749
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 34
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 61
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 152
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 980 AA; 106450 MW; F1F8EBB07B02F948 CRC64;
MPKVTQGSAP APAGQPPGET TGEFDGYLVA VGASAGGLDA LERFFEGLPP HTDVAYVVIQ
HLSPDHKSMM GNLLGRHTRM PVVTVEDGMA IAAGRVHLIP PACIMRAAGG RLWLTPKDPR
VLTLPIDLFF TSLAKELGNR AVGVILSGTG SDGTRGAVAI NEAGGLLLAQ DPETAKFDGM
PRSVIATGLV DAILAPEELG LRVLDHTREA PRTPIRHERL VADRDKGSAL EEIQHLLRHV
AGIDFRDYKP GTVLRRIERR LQVRHIPDHE SYAQLLDGDR AELATLHREL LIPVTSFFRD
PESFEVLAEA AIEVLVKERQ ANQPLRIWVP GVSTGEEAYS LAILFTEACE RVRRWPGFKV
FATDVAQQSL DTASAGVFSE AITSEIAPER LERFFVPRGN HFVIRPEVRQ NIIFARHNLL
EDPPFTRMDL VSCRNVLIYF EPEAQERVLR RLQYALAPGG FLFLGSSESL GALQGDFTPV
STKHKIHRVL RHVALPLDQA SAGHSRLPAI GRRLRAGPSA TRDGDAAVID AGLTTLLRSY
APASLLLNRR HELLHVFGDV SRFLRIGEGS ATLDLAKLLP QRLAPVALAL LHRAAKGAAP
LRSDVLGLPC AEGPPLRLRL VARPVEVPQG EPHLILSFEP EPPIAEPALP AGIETLDLDR
ENAARLQTLE QELAATRESL QATIEELETA NEELQATNEE LMASNEELQS SNEELQSVNE
ELYTVNAENQ EKIEILNQLN ADLDSLARAV SIATVFVDGG LRITRFTPEA TTLFNIRDGD
IGRPIGDITN RLDHPELVAE LRHTIEDGHL FEREIHASNG ATYLARILPY AVRARGPRGA
VATFVDVTSL HDRDRLQATL DALPAGVALL DAAGRIQMVN ARWRALAREG GDPDLHRSGP
GIGIEDACAI LPGGESLAAA RDGIARVLGG ETAAFRREYI HDGPREAGRW RLLYAAPLGG
RGGGAVVSHC DLTAQVAADA
//
