ID A0A126T4N4_9GAMM Unreviewed; 842 AA.
AC A0A126T4N4;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=protein-glutamate O-methyltransferase {ECO:0000256|ARBA:ARBA00012534};
DE EC=2.1.1.80 {ECO:0000256|ARBA:ARBA00012534};
GN ORFNames=JT25_011095 {ECO:0000313|EMBL:AMK77028.1};
OS Methylomonas denitrificans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylomonas.
OX NCBI_TaxID=1538553 {ECO:0000313|EMBL:AMK77028.1, ECO:0000313|Proteomes:UP000030512};
RN [1] {ECO:0000313|EMBL:AMK77028.1, ECO:0000313|Proteomes:UP000030512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJG1 {ECO:0000313|EMBL:AMK77028.1,
RC ECO:0000313|Proteomes:UP000030512};
RX PubMed=25580993; DOI=10.1111/1462-2920.12772;
RA Kits K.D., Klotz M.G., Stein L.Y.;
RT "Methane oxidation coupled to nitrate reduction under hypoxia by the
RT Gammaproteobacterium Methylomonas denitrificans, sp. nov. type strain
RT FJG1.";
RL Environ. Microbiol. 17:3219-3232(2015).
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; CP014476; AMK77028.1; -; Genomic_DNA.
DR RefSeq; WP_062328598.1; NZ_CP014476.1.
DR AlphaFoldDB; A0A126T4N4; -.
DR STRING; 1538553.JT25_011095; -.
DR KEGG; mdn:JT25_011095; -.
DR OrthoDB; 9816309at2; -.
DR Proteomes; UP000030512; 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: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; 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 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:UP000030512};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 9..192
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT DOMAIN 208..477
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT REGION 649..698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..666
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..698
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 15
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 42
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 134
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 842 AA; 94192 MW; 10E21F6AADBB71F3 CRC64;
MKVDITPPVV GIGASAGGLE ALEQFFTHIP TGCGAAFIVV QHLDPTHQGL LPELLQRVTP
MKVTQADEGM KVQTNCIYVI PPNKDLSILQ GKLQLLDPIA PRGLRLPIDF FFRALAGDQH
ERAIGVILSG MGSDSTLGLR AIKENAGLAL AQLPDSAKFD AMPRSAIDAG LADIVATPET
LWEKIASSLQ QSRRGGHVIS EPMQELKSQS ALEQIVMLLR SLTGNDFSLY RKNTLYRRIE
RRMGLHQIDT IADYVRYLQE NTQELELLFK ELLIGVTHFF RDTVAWEQLK SHGIPALLAE
YPKGKEMRAW VSACSTGEEA YSLAMVFKEV LAQCQLTHNF KLQIFATDLD ADAIEKARQG
FYPKTIAGDV SPERLSRFFV AEDNGYRINK DIREMVIFAQ QNIIMDPPFT KLHLLLCRNL
LIYLDPACQQ KLIPLFHYAL IPNGMLLLGN AETIGNFNDL FTAIDSRSRL YRRIDQALSF
AEIEFPTKYF PVAAMIKSDN STSQPVLNLQ SQVEQLLLQK YSPSTVLINA EGDILYIHGR
TGKYLEPAAG KANLNIHAMA REGLRHELAA AITLAQQQSE AVVVSGLTVG TNGGSQMINL
TVQAIDKPEA LKGALMIIFT DVAMPKPRKR SQRSPNAELL QVSDELQKAR EENQSLREEA
QSSQEELKSS NEELQSTNEE LQSTNEELTT SKEEMQSLNE ELQTVNAELQ TKVNDLSWVN
NDMKNLLNSM EIATIFLDNA LNIRRFTNHA THLFKLIGGD VGRPLSDIVT DLDYPQLHQD
ALSVLRTLIF AEKQVKTDDD RWFKVRIMPY RTQENVIDGV VITFIDISET KKLEARVRGN
NE
//
