ID Q1GJH3_RUEST Unreviewed; 837 AA.
AC Q1GJH3;
DT 27-JUN-2006, integrated into UniProtKB/TrEMBL.
DT 27-JUN-2006, sequence version 1.
DT 27-MAR-2024, entry version 122.
DE RecName: Full=protein-glutamate O-methyltransferase {ECO:0000256|ARBA:ARBA00012534};
DE EC=2.1.1.80 {ECO:0000256|ARBA:ARBA00012534};
GN Name=cheR3 {ECO:0000313|EMBL:ABF63193.1};
GN OrderedLocusNames=TM1040_0460 {ECO:0000313|EMBL:ABF63193.1};
OS Ruegeria sp. (strain TM1040) (Silicibacter sp.).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria.
OX NCBI_TaxID=292414 {ECO:0000313|EMBL:ABF63193.1, ECO:0000313|Proteomes:UP000000636};
RN [1] {ECO:0000313|Proteomes:UP000000636}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TM1040 {ECO:0000313|Proteomes:UP000000636};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Brettin T., Bruce D., Han C., Tapia R., Goodwin L., Thompson L.S.,
RA Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Belas R., Moran M.A., Buchan A., Gonzalez J.M., Schell M.A., Sun F.,
RA Richardson P.;
RT "Complete sequence of chromosome of Silicibacter sp. TM1040.";
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABF63193.1, ECO:0000313|Proteomes:UP000000636}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TM1040 {ECO:0000313|EMBL:ABF63193.1,
RC ECO:0000313|Proteomes:UP000000636};
RX PubMed=17526795; DOI=10.1128/AEM.02580-06;
RA Moran M.A., Belas R., Schell M.A., Gonzalez J.M., Sun F., Sun S.,
RA Binder B.J., Edmonds J., Ye W., Orcutt B., Howard E.C., Meile C.,
RA Palefsky W., Goesmann A., Ren Q., Paulsen I., Ulrich L.E., Thompson L.S.,
RA Saunders E., Buchan A.;
RT "Ecological genomics of marine Roseobacters.";
RL Appl. Environ. Microbiol. 73:4559-4569(2007).
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; CP000377; ABF63193.1; -; Genomic_DNA.
DR RefSeq; WP_011537808.1; NC_008044.1.
DR AlphaFoldDB; Q1GJH3; -.
DR STRING; 292414.TM1040_0460; -.
DR KEGG; sit:TM1040_0460; -.
DR eggNOG; COG1352; Bacteria.
DR eggNOG; COG2201; Bacteria.
DR eggNOG; COG2433; Bacteria.
DR HOGENOM; CLU_000892_0_2_5; -.
DR OrthoDB; 9816309at2; -.
DR Proteomes; UP000000636; 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: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; 3.40.50.150; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00050};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:ABF63193.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000636};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABF63193.1}.
FT DOMAIN 9..196
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT DOMAIN 200..476
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT COILED 650..723
FT /evidence="ECO:0000256|SAM:Coils"
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 138
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 837 AA; 92792 MW; EBA671FC10C379FB CRC64;
MSDRSIPFLV GIAASAGGLE ALSELVQELG EQNEAAYVIA QHMSPNHKSM LSALISRETR
LPVRELTPDA DIWPEANTIY VVMPGHDVIV TEGGQLGLRA PSGLRGQPKP LADLLLKTMA
EECGENCAAI ILSGTGSDGS YGVRAIREVG GITIAQDPES SKYSGMPTSA LQTGCVDLTL
RPREIGEHLG KILSRPRDFT ELQELHQKPN HLSDLFQILT ARTGVDFREY KASTINRRIA
RRMLALGFSE YNAYVDFCRS DLAEVDALYK DLMISVTRFF RDPQQFDALK ADIQKLVAKL
ESSSDQRTVR VWVSGCATGE EAYSVAILFL EAMGGLEKVS QRRLQVFATD IDQHALDVAR
RGEYPISAIN DIPQELVDRY FVERTDTIEV KKALRAFVLF SRHNVIQDPP FTNLDCVSLR
NLLIYFNGPL QDKVLARIGY ALVPDGLLFL GAAETVGGME TIFEPTSTSD RIYRKRLVTR
KPALQPFIED ATARRPLEQS ALPYLADKNK HHSATRQFDN LIRVLAPNGF LASATGAILR
VIGDISFVTA LTENTGLQVD LKILLPELRS EASSLINVTL RSRGVRSGQW HPLPRSKHEQ
VRLTCYPIVS APDGEMDGNS IVLIGVESRI KEEQAAPPES RNPEEQDRYI RQIEDEVIST
REALQQTIEE LQTANEELQS VNEEMQAANE ELQSTNEELE TSNEELQSTN EELITVNEEI
QVNSSEIQHL SAELSAVLRA NPFVMIVVDQ ALQVRHASRQ AMTMFELDAL PKSGIHISQC
APVEGMPDLT SRISHVFRTS APLVENAEFG GASHEMTFTP FREREGRDLI GVAVTIV
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