ID K2H7J2_9BACI Unreviewed; 949 AA.
AC K2H7J2;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=protein-glutamate O-methyltransferase {ECO:0000256|ARBA:ARBA00012534};
DE EC=2.1.1.80 {ECO:0000256|ARBA:ARBA00012534};
GN ORFNames=MJ3_07538 {ECO:0000313|EMBL:EKE31615.1};
OS Salimicrobium jeotgali.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Salimicrobium.
OX NCBI_TaxID=1230341 {ECO:0000313|EMBL:EKE31615.1, ECO:0000313|Proteomes:UP000011746};
RN [1] {ECO:0000313|EMBL:EKE31615.1, ECO:0000313|Proteomes:UP000011746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MJ3 {ECO:0000313|EMBL:EKE31615.1,
RC ECO:0000313|Proteomes:UP000011746};
RX PubMed=23144427; DOI=10.1128/JB.01808-12;
RA Lee S.H., Jung J.Y., Jeon C.O.;
RT "Draft Genome Sequence of Salimicrobium sp. Strain MJ3, Isolated from
RT Myulchi-Jeot, Korean Fermented Seafood.";
RL J. Bacteriol. 194:6695-6695(2012).
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:EKE31615.1}.
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DR EMBL; AMPQ01000008; EKE31615.1; -; Genomic_DNA.
DR RefSeq; WP_008590026.1; NZ_JAFBFF010000007.1.
DR AlphaFoldDB; K2H7J2; -.
DR STRING; 1230341.AAV35_009080; -.
DR KEGG; sje:AAV35_009080; -.
DR PATRIC; fig|1230341.3.peg.1562; -.
DR eggNOG; COG1352; Bacteria.
DR eggNOG; COG2201; Bacteria.
DR OrthoDB; 9816309at2; -.
DR Proteomes; UP000011746; 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; 2.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00050};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:EKE31615.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000011746};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EKE31615.1}.
FT DOMAIN 3..192
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT DOMAIN 209..462
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT COILED 637..720
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 134
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 949 AA; 108867 MW; 4C2C5A307591EC05 CRC64;
MSHTEEKYYI GIGASAGGLE SLERFFKTMP NDTGLTFIII QHLSPDFESH MDDLLRRYTS
MNIHVAEDMM ATEPNSVYLI PPRKNLSIYH GTLHLSEQTE RKHLNLPIDL FFKSLAEDQG
RNSIGVILSG TGSDGTLGVR ALKDADGMVI AEDETTAKFD GMPRSAISTG LIDYILPPDD
MAEEIINYVT HPADPVNRSL QTSDGKSMLS RINRIMRSHS KIDFDNYKET TMIRRINRRV
KLNRLQTLEE YAEHLSNSEK ERNILQQELF IGVTGFFRDK EAFDSLTENV LPKLDYNKEA
LRIWSAGCST GEEVYSLAIL LCEYMEKNNL QTGLKIFATD IDDKALETAG NGVYPESLMS
DVPPELVAKY FIKEEEGYRI ANSIRKMVVF AKHNLVNDPP FSRLDLLVCR NLFIYLKSET
QQYILNKFYY SLLKNGYLFL GTSETLGDLT KAYRSIDNKW KFYKPREDYR PDHPSGISLY
SDKGPEIEKN TQPAKSVAQN VNLENVLQKA VSSISPPSII IDGNDQIIHV INDMSDYLRP
QPGKFSNNFN TNMSRELSLF VNNILRRLKA ERTHVRLNNI MNGAGEETSL SLSGHIIEMK
YQFFYFISFI EATEVKVKNS EEVDVSDQMK ERVRYLESEL QLAREGLQAT VEELETSNEE
LQTSNEELTA SNEELQSTNE ELQSVNEEIY TVNNEYQEKI EELKKANNDL NNLLNNTEIG
ALYLDEMLCI RRITPLMKEV SNVRDEDIGR PISHISVMSE YPEVVDDVYE VLDSLIKKEK
EIEDNKGRHW FVRIRPYRTE YNSVNGIIVT LVEITNLKKE RSKVMETKEK FEQVLEISNM
GWWEFNGRAD HFDVSPSFLQ NCGYGKEDFP TTLNEVSRYF KTNDIKVAFE KMLSGKKKSI
NLFASYQCED GSFIPVHFLG RVLEKDHDED PLRIGGTIID ISNYMKQGD
//
