ID A0A1M4WFT2_9BACT Unreviewed; 973 AA.
AC A0A1M4WFT2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=protein-glutamate O-methyltransferase {ECO:0000256|ARBA:ARBA00012534};
DE EC=2.1.1.80 {ECO:0000256|ARBA:ARBA00012534};
GN ORFNames=SAMN05444008_10317 {ECO:0000313|EMBL:SHE80161.1};
OS Cnuella takakiae.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Cnuella.
OX NCBI_TaxID=1302690 {ECO:0000313|EMBL:SHE80161.1, ECO:0000313|Proteomes:UP000184368};
RN [1] {ECO:0000313|EMBL:SHE80161.1, ECO:0000313|Proteomes:UP000184368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26897 {ECO:0000313|EMBL:SHE80161.1,
RC ECO:0000313|Proteomes:UP000184368};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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; FQUO01000003; SHE80161.1; -; Genomic_DNA.
DR RefSeq; WP_073040401.1; NZ_MTFE01000010.1.
DR AlphaFoldDB; A0A1M4WFT2; -.
DR STRING; 1302690.BUE76_07305; -.
DR OrthoDB; 9816309at2; -.
DR Proteomes; UP000184368; 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 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; IPR013656; PAS_4.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR000673; Sig_transdc_resp-reg_Me-estase.
DR NCBIfam; TIGR00229; sensory_box; 1.
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; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 1.
DR PRINTS; PR00996; CHERMTFRASE.
DR SMART; SM00138; MeTrc; 1.
DR SMART; SM00091; PAS; 2.
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.
DR PROSITE; PS50112; PAS; 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:UP000184368};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 11..189
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT DOMAIN 206..478
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT DOMAIN 854..924
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT COILED 646..726
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 20
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 47
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 139
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 973 AA; 110326 MW; 9B3D9C54AC49398E CRC64;
MTNNNIQQDK PLLVAGIGGS AGAFEAVREL VSHLTSQNGI AYVYLQHQPA DFDSQMVPLL
AKKTKVPVLV AEEGMEVQPD VFYIVPPGKE LTLKEGLFRL AKRASEGYDH MPINRLFSSV
ADAYKELAIG VVLSGADGDG AQGLKAIKAA GGLSFAQDAS AQFQSMPQTA IAIDAVDLVL
SPKEIAEELN SLGRQKDFYF SALQDPSGEL LSNKDKDLII ILQMVQKATS VDFGQYKMST
IKRRIIRRIL LHKLNTLQDY VQYMRAHPAE TQQLFNDLLI NVTHFFRDKE TTEYLKNKLF
PEIIAAKQHN EPIRIWVPAC SSGQEVYSIA IILIEVLGEH HGTHPIQIFA SDLSETAIHK
ARLGMYSTDE ITGISPKRLQ RFFTKVDGQF RINKSIRDLC VFATQNITLD PPFSRLDLVS
CCNFLIYIDN NLQQKIMSTF HYALNNNGYL VLGKSETVGS SAYLFSQVDK KVKVFAKKKD
TPAKALFPMS YLLPVGHRVQ AITKQKTVAA SRNDDQDLEK AVDTLLLKKF TPASVVINHD
MDIVQFRGST GIFLEPTPGK ASLNLLKMAR PGLAFELRNT VHKAIKSGEA VKKSDLELTY
NDKVMRINVE VVPIKSELEE SYFLVAFSES GLPPEVELSA LKDHRVKQLE TELSALREDM
RSIVEEQEAS VEELQSANEE IVSANEELQS INEELETSKE EVESSNEELI TINQELQLRN
EQLTESQDYA QAVFSTIREA LLILDRNLRV KLANFQFYRM FQLREEHTEG RMLYELNSRQ
WDIPELRQLL EEKLPGNAYI HGLEITHNFA GIGEKTLVIN ARRIVQRIHS DQLTLLALED
ITEHRRAQQI IADRELWFRN LADNAPVMIW VTDKDKKATF FNKAWLEFRS DTMEEALVKG
WMDDVHPEDR PRLKKLFDDC FQEKLPFELK YRVLYHDTEY KLLHNKAKPN FSPEGQFLGY
IGSCVVIQEI NAA
//
