ID A0A0Q8QEV1_9BURK Unreviewed; 827 AA.
AC A0A0Q8QEV1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=protein-glutamate O-methyltransferase {ECO:0000256|ARBA:ARBA00012534};
DE EC=2.1.1.80 {ECO:0000256|ARBA:ARBA00012534};
GN ORFNames=ASE26_14935 {ECO:0000313|EMBL:KRB81818.1};
OS Duganella sp. Root198D2.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Duganella.
OX NCBI_TaxID=1736489 {ECO:0000313|EMBL:KRB81818.1, ECO:0000313|Proteomes:UP000051728};
RN [1] {ECO:0000313|EMBL:KRB81818.1, ECO:0000313|Proteomes:UP000051728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root198D2 {ECO:0000313|EMBL:KRB81818.1,
RC ECO:0000313|Proteomes:UP000051728};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB81818.1, ECO:0000313|Proteomes:UP000051728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root198D2 {ECO:0000313|EMBL:KRB81818.1,
RC ECO:0000313|Proteomes:UP000051728};
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:KRB81818.1}.
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DR EMBL; LMIC01000051; KRB81818.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q8QEV1; -.
DR Proteomes; UP000051728; 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:UniProtKB-EC.
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; 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: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; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF57997; Tropomyosin; 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 Reference proteome {ECO:0000313|Proteomes:UP000051728};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..165
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT DOMAIN 195..436
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT COILED 628..694
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 4
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 31
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 122
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 827 AA; 91951 MW; 5CEC3F7F19CEABE3 CRC64;
MGASAGGLDA ISEFLASMPS RTGMAFVVLQ HQDPSRRGLL PELLRRITSM EVYEIAESTE
VRPDHVYVAP PNFDLAFSGG KLMAVETSDT HARYPIDSFF RTLAAEKGQA AAGVVFSGMG
TDGTAGLRAI QEAGGVTLAQ EPNSAKFDSM PRSAITAGVA DFVAPPGAMP MWLCQVRSVP
HGGAHGAARA RRQALRELMS LLQRHTGNNF TEYKMSTVLR RIERRMKLHQ LDSMESYVAY
LRENTGEVQL LFREMLIGVT SFFRDPTVWE HLCNETIPAL LAANPDGAAF KAWVPACSTG
EEAYTLAMVF DEAVTRASGL GKFSLQIFAT DLHGDAIDKA RQGMFGRAVE DALSHERLLR
YFIVDGAGYR IRKELRNMII FAQQNIISDP PFTKLDILSC RNLLIYFNPK LQEQLIPLFH
YALKPEGLLV LGSADTPGSY NELFTPVPGC GRIYRRLDAS TQRVANYFPT KIAKAAQPSS
IEVTTMTMNG NIQTQVEHLL LKAHTPAAVM INSDDDILYI HGRTGTFLEP AAGRANWNIH
AMARDGLRYE LADLIERANR SESTETVREL LFKDGAASLL VDMTAEVLRE DAHSGHNLLV
TFNASPMPAR KRGSRGADPR PQELEQQLTM ARLELQAVRE EMQTSREELK AANEELQSTN
EELQSTNEEL TTSKEEMQSL NEELYTVNAE LQSKVDDLSL VNSDMKNLLN STDIAVIFLD
SQMNIRRYTN QATQLYKLIA TDLNRPLSDI ANDLVYPTME DDAAEVLRSL VFCERQIPTR
DGRWFMVRIM PYRTVNNVID GLVLTFVNVT ELKLLEARLT PEGGSLK
//
