ID A0A0A7LQ38_9BACT Unreviewed; 972 AA.
AC A0A0A7LQ38;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, 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=PK28_15870 {ECO:0000313|EMBL:AIZ65304.1};
OS Hymenobacter sp. DG25B.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=1385664 {ECO:0000313|EMBL:AIZ65304.1, ECO:0000313|Proteomes:UP000030789};
RN [1] {ECO:0000313|EMBL:AIZ65304.1, ECO:0000313|Proteomes:UP000030789}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG25B {ECO:0000313|EMBL:AIZ65304.1,
RC ECO:0000313|Proteomes:UP000030789};
RA Jung H.-Y., Kim M.K., Srinivasan S., Lim S.;
RT "Hymenobacter radioresistens genome sequence.";
RL Submitted (NOV-2014) 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};
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DR EMBL; CP010054; AIZ65304.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A7LQ38; -.
DR STRING; 1385664.PK28_15870; -.
DR KEGG; hyd:PK28_15870; -.
DR HOGENOM; CLU_000892_0_2_10; -.
DR Proteomes; UP000030789; 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 CDD; cd00130; PAS; 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; IPR000014; PAS.
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 SMART; SM00091; PAS; 3.
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); 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000030789};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 10..196
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT DOMAIN 216..477
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT COILED 654..730
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 19
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 46
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 138
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 972 AA; 110115 MW; 51337623018C94E1 CRC64;
MQAQEDSRET FPIVGMGGSA GSLGAFEQFF RHMPPHSGIA FVVVMHLAPN PNGELAQVMQ
RFTDMPVLEA ADGMKVLPNH VYVIPPDRDM SILHGTLLLF PPTQPRGKRL PIDLFYQSLA
KDARERAVCI IFSGMGADGT LGLKMVMENF GMVMVQTPET AEYDSMPRSA IATEFVDYIL
PADQLPNKLL EYLHKPIMER PRRERPESVS RPAHALQKIF LLIRTQTGHD FSYYKRNTVF
RRIERRMNSH QIKEFTQYVR YLQENPSEVD ALFKELLIGV TKFFRDQEAY DSLKTQLIPM
LRQKPINSVF RVWAPGCSTG EEAYSLAMLL QECLEQIEPG HYLKIQIFAT DINPQGIDFA
RAGLYQDNIV ADVSPERLER FFIKQEIGYQ IRKEVRDAVI FALHDINKDA PFTRLDLLCC
RNLLIYLSAE LQRNLLPVFH YALNPGGLLF LGPSENMTGF HELFKPLDIK WKIFRRNDAS
SSVTRLANFP FALTRQQTSV PVAASSMNTS SPRKDGTFAS LVQRVMLRAF TPPAVLINAK
GEILYVNGRT GRYLEPAPGL GGLNIFEMAR EDLNYEISAV VHKASTARES VVAENVKVKT
DAGYQLLRIS VTYLTEPDAL AGLMLVAFED QPTPRRVRTG KASPGSDLSR DTVVAALEKE
LQYTKHRLQT TIEEMESSVE ELKSTNEELQ SANEELQSTN EEAMTNKEEM QSLNEELMTL
NMQYLSKTEE LSQAANDMKN LLDATEIATV FLDNDMIIRR FTPSVGRIMH LQPADVGRPI
THFASNLRYA SLIQDINQVL ERLVSTESII QTTTNEWYAM RILPYRTLDN YISGAVITFT
DISGLKHLEE ELQSSRRYAE SIVETVREPM LVLDHELRVL TVSQAFTEAF GQEPAKGQPL
AELNNGVWRQ PILRDNLMDL LNGVSVGFDD LPLALSSLNR DEPPRHVLVY GRRIHSEGHP
TDRILMGVRF VY
//
