ID A0A0Q7ASC3_9BURK Unreviewed; 889 AA.
AC A0A0Q7ASC3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=protein-glutamate O-methyltransferase {ECO:0000256|ARBA:ARBA00012534};
DE EC=2.1.1.80 {ECO:0000256|ARBA:ARBA00012534};
GN ORFNames=ASC76_08015 {ECO:0000313|EMBL:KQW38007.1};
OS Rhizobacter sp. Root404.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Rhizobacter.
OX NCBI_TaxID=1736528 {ECO:0000313|EMBL:KQW38007.1, ECO:0000313|Proteomes:UP000051611};
RN [1] {ECO:0000313|EMBL:KQW38007.1, ECO:0000313|Proteomes:UP000051611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root404 {ECO:0000313|EMBL:KQW38007.1,
RC ECO:0000313|Proteomes:UP000051611};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQW38007.1, ECO:0000313|Proteomes:UP000051611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root404 {ECO:0000313|EMBL:KQW38007.1,
RC ECO:0000313|Proteomes:UP000051611};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KQW38007.1}.
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DR EMBL; LMDS01000004; KQW38007.1; -; Genomic_DNA.
DR RefSeq; WP_056464663.1; NZ_LMDS01000004.1.
DR AlphaFoldDB; A0A0Q7ASC3; -.
DR STRING; 1736528.ASC76_08015; -.
DR Proteomes; UP000051611; 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 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; 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 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; 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:UP000051611};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 23..207
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT DOMAIN 230..508
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 646..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 861..889
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..680
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..717
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 35
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 62
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 154
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 889 AA; 97098 MW; C163C3F13B6A3591 CRC64;
MSSKVNRVPR RAAAPTTKRA TTAGSSLQVI GIGASAGGLE AIEAFLSEAG CLRDSTFVVI
QHLGAGTPSL LPELLKRATR LPVKSIEPDA PVQPDVVYVV PPGCDLTIDT DRFVLTPQQA
SAGHKLPIDA FFRSLAAAYG DRAVGVVLSG MGSDGTKGLA ALKARGGAAF VQAPDSAQFD
SMPRSALQAG LADAAAAPAD LPALIAAHLL KWRHEHGEPV SLVADDPQAL EAIVQTLRAQ
TGHEFADYKK STLQRRIERR MGVHQCRALD DYSRLLRENK AEAELLFKEL LIGVTSFFRD
PRVWDHLRDV VLPEFLRGRS DTKPLRLWVP GCSTGEEAYT LAMVLTEALQ ALDAPAPRAF
RIFATDIDSD AIDRARQARY PLGIAGSMSA ERLARFFVRD DTGYQIRKDL RETVIFALQN
VAMDPPFTKL DMLVCRNLMI YFEPALQRRL LRLFHYSLEP GGLLLLGRAE TTGQAGDHFA
PVPGEIKLFR RLETFRSSGF VAFPATFDRP VALAPQDSRA SLADDGDLGL QGLADHLLLQ
RYSPAAVLVN REGDVLYVSG KTGRYLEPAA GKANWNVFAM AREGLSRPLG AAFKDAVRAQ
RGVSVDGSVF DPDLGARKMR VTVDPITSPT LLAGMLMIVF REVEPDRTER PAKDAARPKR
GDAGDLQLTE LRDALRAARD EARSAAAQSR ASNEELQSTN EELQSTNEEL TTSKEELQSM
NEELQTVNQE LQAKVDELSQ ASDDMRNLLN STEIATVFLD ELLHIRRFTA QAVSVFKLIP
TDIGRPITDI TNALEGWDVA RDAQEVLHNL VPKEREVPAS GERFFRVRMM PYRTSTNRID
GVVITLSDVS AAKRLEQRLT GALSASEQRA GDGAAAPAVR KRAPTSKRP
//
