ID A0A5Q0BJA9_9GAMM Unreviewed; 960 AA.
AC A0A5Q0BJA9;
DT 22-APR-2020, integrated into UniProtKB/TrEMBL.
DT 22-APR-2020, sequence version 1.
DT 02-APR-2025, entry version 16.
DE RecName: Full=protein-glutamate O-methyltransferase {ECO:0000256|ARBA:ARBA00012534};
DE EC=2.1.1.80 {ECO:0000256|ARBA:ARBA00012534};
GN ORFNames=F6R98_06080 {ECO:0000313|EMBL:QFY42247.1};
OS Candidatus Methylospira mobilis.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Methylococcales; Methylococcaceae; Candidatus Methylospira.
OX NCBI_TaxID=1808979 {ECO:0000313|EMBL:QFY42247.1, ECO:0000313|Proteomes:UP000325755};
RN [1] {ECO:0000313|EMBL:QFY42247.1, ECO:0000313|Proteomes:UP000325755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Shm1 {ECO:0000313|EMBL:QFY42247.1,
RC ECO:0000313|Proteomes:UP000325755};
RA Oshkin I.Y., Dedysh S.N., Miroshnikov K., Danilova O.V., Hakobyan A.,
RA Liesack W.;
RT "Ecophysiology of the spiral-shaped methanotroph Methylospira mobilis as
RT revealed by the complete genome sequence.";
RL Submitted (SEP-2019) 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; CP044205; QFY42247.1; -; Genomic_DNA.
DR RefSeq; WP_153248228.1; NZ_CP044205.1.
DR AlphaFoldDB; A0A5Q0BJA9; -.
DR KEGG; mmob:F6R98_06080; -.
DR InParanoid; A0A5Q0BJA9; -.
DR OrthoDB; 9816309at2; -.
DR Proteomes; UP000325755; 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:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-UniRule.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
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; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR050903; Bact_Chemotaxis_MeTrfase.
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; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR000673; Sig_transdc_resp-reg_Me-estase.
DR PANTHER; PTHR24422; CHEMOTAXIS PROTEIN METHYLTRANSFERASE; 1.
DR PANTHER; PTHR24422:SF27; PROTEIN-GLUTAMATE O-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 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 ECO:0000313|EMBL:QFY42247.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000325755};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:QFY42247.1}.
FT DOMAIN 9..198
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT DOMAIN 225..470
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT REGION 489..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 654..733
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 21
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 48
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 140
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 960 AA; 107146 MW; 118F82A7AAAE58E0 CRC64;
MPIKKTDDAA TVFHIVGIGA SAGGLEAFKQ FFLHTAADTG MAFVLVSHLD PDRDSLLADI
LQRSTIMPVA EALDQMPVEP NRVYVIPPNR EMVIAQGRLQ LSVPLEPRGQ RMAVDKFLGS
LAEDRKKSAI GIVLSGSGTD GTLGLQAIQD QGGVTFAQQP DTAEFDGMPS SAIQAGCATH
ILPVDKMPEA VLACAGTLAS QTETPAFSTM KSGIRAILKQ LLDFTGHDFS LYKKSTIVRR
IERRMHQLHI EDIEVYAHYI EENPDESRNL FKELLINVTG FFRDAEAFAV LRNDILPKMC
RDKADDYVFR VWVAGCATGE EAYTIAILLR ELMEKTHQPF KTQIYSTDLD DSAIAVARQG
IYPPSIAQDV AQERLQRFFT REDARYRVKK DIREMVVFAT QNVIKDPPFT RIDLISCRNL
LIYLTAELQN RLIPKFHYAL NPGGVLFLSP SESIGNHTEL FSSIHRKWKF YRVSHSNLSS
RAAMARGMHR PAESGGKPPE QAMKKASRTK PLQHANYWTP VQCFAQASVT ANLQGDIICS
HGETGRYLHP ASEHTKLNVI EMAREGLELE LRSAFHAAAG EGIATLNREV RIESYGGSTS
LSLSVKPLPC PVGAQRLLLV SFHDVTDTAV KLGRERSAKP GRIEELERDL AYLKECHQTT
VEELQVSNEE LKSTNEELQS TNEELQSTNE ELETSTDELH LANEELITVN SELHSKIEQL
ERMQNDMKNL LDNISVGIIF LDRRLMIRSF TQEAVRIYPL IATDVGRPLN DFKPVVEEGG
ELLPAARSVL ESLMPYEREL KINGNAWVLA RIQPYRMLDN VIDGIVLTFT DITARINAVA
AQEALNLAEG IVNTVREPLV VLDSTMKVVT ASRSFYQEFQ VTAEETAGSL IFDLGCRQWD
HPALHELLEK ILPDDRGFEG FVLEQDFPVI GHRRIVLNAR QFIGKAGEPQ LILLSMEVDA
//
