ID S7V8C8_DESML Unreviewed; 1095 AA.
AC S7V8C8;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=protein-glutamate O-methyltransferase {ECO:0000256|ARBA:ARBA00012534};
DE EC=2.1.1.80 {ECO:0000256|ARBA:ARBA00012534};
GN ORFNames=dsmv_2296 {ECO:0000313|EMBL:EPR40793.1};
OS Desulfococcus multivorans DSM 2059.
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfococcaceae; Desulfococcus.
OX NCBI_TaxID=1121405 {ECO:0000313|EMBL:EPR40793.1, ECO:0000313|Proteomes:UP000014977};
RN [1] {ECO:0000313|EMBL:EPR40793.1, ECO:0000313|Proteomes:UP000014977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2059 {ECO:0000313|EMBL:EPR40793.1,
RC ECO:0000313|Proteomes:UP000014977};
RX PubMed=23950126;
RA Brown S.D., Hurt R.A.Jr., Gilmour C.C., Elias D.A.;
RT "Draft genome sequences for three mercury-methylating, sulfate-reducing
RT bacteria.";
RL Genome Announc. 1:e00618-e00613(2013).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EPR40793.1}.
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DR EMBL; ATHJ01000080; EPR40793.1; -; Genomic_DNA.
DR AlphaFoldDB; S7V8C8; -.
DR STRING; 897.B2D07_00880; -.
DR PATRIC; fig|1121405.3.peg.1863; -.
DR eggNOG; COG1352; Bacteria.
DR eggNOG; COG2201; Bacteria.
DR Proteomes; UP000014977; Unassembled WGS sequence.
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; IPR001345; PG/BPGM_mutase_AS.
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.
DR PROSITE; PS00175; PG_MUTASE; 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:EPR40793.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000014977};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EPR40793.1}.
FT DOMAIN 112..297
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT DOMAIN 313..558
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT REGION 592..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 768..855
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 118
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 147
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 239
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 1095 AA; 120708 MW; 79B8FBF12BE02709 CRC64;
MMTLVLLRHG ERIWNKKTGS RAGRMQACQK KESRKPGRGK AWRCVRRRCC LKKQERCSGE
GWGADTITNR KKDRSEAAIT PGDTGAIETQ ECVAASAESQ ETVESTSAYF PIVGIGASAG
GLAAFEAFFS GMPADTDPGM AFILVQHLAP DHKSILTNLV QRYTRMQVFE VEDGMTVRPN
CTYIIPPGRD MAFLGGALQL LEPSAPRGRR MPIDFFFRSL AQDQRERAIG IVLSGTGSDG
MLGVRAIKGE GGMVMAQNPA STAYDGMPRS ALATGLVDYE LPPAEMPAQL IAYAAHAFGI
PRSPAIALPP KVENALKKIF ILLRAHTGHD FSQYKPSTVN RRIERRMSIH QIETMDGYVK
FLQQTPNEVE ALFRDMLIGV TSFFRDPAAF KAVQEQIIPK LFSGKSSNCA IRVWSAGCST
GEEAYSLAIL LAELQEKLKQ SFKVQIFATD IDSHSIVTAR AGLYPASIDA DISPERLARF
FSVEHDGNFY RIRKNIRDML VFSEQNVIRD PPFSKIDLIS CRNLMIYMGA ELQKKIIPLF
HYALNPCGFL FLGTSETVGE FGHLFTTLDR ISKLYQRRED FHPTGPYRFL PPMTEAATPL
PPATPKSAYP GKPSLRELTE KALLRHVAPV AALVNGDGDI LYLHGRTGLY LEPAPGETGV
NNILKMAREG LRRELVTAIR KVVAGEEVVR CPNLRVKTNG DVTATNLTVR TVPLGMPAVH
AGASEAPLML VILEQGLPLE RGEDALTVLS ATEAVAGIEA GDEAHALIDS LRQELQAKEE
YLQTASEELK TTNEELKSSN EEMQSVNEEL QSTNEELETS KEELVSMNEE LSTVNAELQT
KVADLSRANN DMNNLLSGTG IATVFVDQSL RILRFTPTAT RIINLIHSDI GRPVGHIVSN
LTGYDALPAD TQEVLDTLVP KEVEVQTRAG VWHTMRILPY RTLDNVIEGA VITFVDISSA
KQAQEALHEA HIRVTEAIVA TVHEPLLMLD ADLRIIAASR SFHSIFRAAP DSATGRFLYD
FGNHLWDIPV LRNLLETILA RGSVFNNYIL SHEFEAIGLR TIRINARMVS EAGRPRFILL
AMADITEPKN EGNAP
//
