ID A0A0F3GX65_9BACT Unreviewed; 496 AA.
AC A0A0F3GX65;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=protein-glutamate O-methyltransferase {ECO:0000256|ARBA:ARBA00012534};
DE EC=2.1.1.80 {ECO:0000256|ARBA:ARBA00012534};
DE Flags: Fragment;
GN ORFNames=MBAV_001237 {ECO:0000313|EMBL:KJU86569.1};
OS Candidatus Magnetobacterium bavaricum.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Magnetobacterium.
OX NCBI_TaxID=29290 {ECO:0000313|EMBL:KJU86569.1, ECO:0000313|Proteomes:UP000033423};
RN [1] {ECO:0000313|EMBL:KJU86569.1, ECO:0000313|Proteomes:UP000033423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TM-1 {ECO:0000313|EMBL:KJU86569.1};
RA Kolinko S., Richter M., Glockner F.O., Brachmann A., Schuler D.;
RT "Single-cell genomics of uncultivated deep-branching MTB reveals a
RT conserved set of magnetosome genes.";
RL Submitted (FEB-2015) 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};
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:KJU86569.1}.
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DR EMBL; LACI01000546; KJU86569.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F3GX65; -.
DR PATRIC; fig|29290.4.peg.1647; -.
DR Proteomes; UP000033423; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
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 GO; GO:0016310; P:phosphorylation; 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 Kinase {ECO:0000313|EMBL:KJU86569.1};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000033423};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 47..236
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT DOMAIN 239..470
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 59
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 86
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 178
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT NON_TER 496
FT /evidence="ECO:0000313|EMBL:KJU86569.1"
SQ SEQUENCE 496 AA; 56269 MW; 4148D0E37A46AF31 CRC64;
MPKNQKNGHQ GKHKKIRRIV AADNDHSSRE SQNGVPAPEG SEVVCSPEVD FPIVAIGASA
GGLEALEVFF SNMPSDANMA FVVIQHLSPK HKSIMGLLLE KHTDMKIQVA EDGVKLKPNH
VYLNPPEKNL AIMHKVICLM EPPHIHSLNL PIDYFFQSLS DDQGERSICI ILSGTGTDGT
KGLRAIKGVG GVAMVQDEKQ ARYNGMPSSA IGTGLVDYVL PVEDMPKTLI RYVRHPYVEG
QRKSTISQDK LNRIFMATRH VTGHDFSHYK KNTICRRLQR RMAVHQIEDI DDYIRYFQQT
PIEVRLFFKD MLIGVTNFFR DKNAFEFLKE TVLWEMLKDR PYGSNLRIWV AGCATGEEAY
SIGIVVAEVM KALKISLNVQ IFATDIDSEA IAFARAGIYP QNISADVSDD RLTNYFSKDN
DTYMVKKEIR QMVVFSEQNI IKDPPFSKLD LISCRNVLIY MESTLQKKLI PILHYTGDSR
NYEARWYHRM LNMLAI
//
