ID A0A117KE15_9FLAO Unreviewed; 1107 AA.
AC A0A117KE15;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=protein-glutamate O-methyltransferase {ECO:0000256|ARBA:ARBA00012534};
DE EC=2.1.1.80 {ECO:0000256|ARBA:ARBA00012534};
GN ORFNames=AR687_20630 {ECO:0000313|EMBL:KUJ59893.1};
OS Flavobacteriaceae bacterium CRH.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=1742859 {ECO:0000313|EMBL:KUJ59893.1, ECO:0000313|Proteomes:UP000053826};
RN [1] {ECO:0000313|EMBL:KUJ59893.1, ECO:0000313|Proteomes:UP000053826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRH {ECO:0000313|EMBL:KUJ59893.1,
RC ECO:0000313|Proteomes:UP000053826};
RA Newman J.D., Miller J.R., Jacobs K.T.;
RT "Genome Sequence of Flavobacterium sp. CHR.";
RL Submitted (OCT-2015) 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};
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00050}.
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:KUJ59893.1}.
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DR EMBL; LMAJ01000026; KUJ59893.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A117KE15; -.
DR STRING; 1742859.AR687_20630; -.
DR OrthoDB; 9816309at2; -.
DR Proteomes; UP000053826; 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:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0008984; F:protein-glutamate methylesterase activity; IEA:InterPro.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 1.10.155.10; Chemotaxis receptor methyltransferase CheR, N-terminal domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-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; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_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; PF02518; HATPase_c; 1.
DR PRINTS; PR00996; CHERMTFRASE.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00138; MeTrc; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47757; Chemotaxis receptor methyltransferase CheR, N-terminal domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 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.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 12..160
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT DOMAIN 213..479
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT DOMAIN 855..1081
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 631..707
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1107 AA; 126034 MW; DD8A5CE4DFC39113 CRC64;
MEIAEFNTNQ LKNPSFPVVG IATDTSQIDV VKQILSTIPA HSGMAYVIME NLEIHQHTNL
PQQLAPYASI PVIEIVNTIE LQPNHVYIVP EKNFLILENG TLKLKPAIRG SRTNNCLDIF
YNALAQKYES YAIGLLAYWS PIDGAAGLKN IREQGGATVS AVTKTGFELN KANAEFIDYF
TIPAETVSKL IEIQESYLVN RAYEDIEATV DQDEFFHAII DLIYLKTGTN LHLYKPQTLR
RRIAKRMVIT RQENTERYLN LLQNKSGEKT LLFNDILIPV TYFFRDPLFF DSLPKLVFPS
LLESVKGKEI RIWSAGCSTG EEAYSLAICI DEYLQLTNNS DISVKIFASD LSEKCIEKAR
LGLYTQQDLK NISEERLSKY FTKKESGYHI SKLIRDRCVF AIHDLTKDFP FSNIDLITCR
NVLIYFDTEL QNKVLSSFHY SLRDQGFLFL GKSESAVRLK ELFTTVERQA KIYIRKNADV
RLAMDITGFS GSKSKQFEEL ANTVTNYKKI AADTLLEQYS PAAVVVNEDF EIVHFHGDTS
SFLQPSAGKP SFNIINMVPH EIRFSLRNAI LKARNEKKTV LGDFISIKNQ SFLTSFEAVY
LPSNTELLLV IFGRKPIPAT NSLRSGTILG EKETEKELFQ LQNDFRHLTE EQQIYFEELH
ATNEELSKRT DELQFINEEL ETSIEELLSK NEELSFTNDE LQNHRRQIAS MRNFYELIVN
TIREPLLIID KNFIVHSTNP AFYSYFNTQE ERTEGISIFE IGNSTWNTPE FKENVLKKIS
RNELVENLKI QFKGAGGVNK VMLINVAPII ESIPEGLILI ALEDITDLEN TNEVLKSKND
ELINRSRQLE SFTAVAAQEL LEPVRKMYMF GKKIIDNEPG LSESAQYNAK RLLNAATNMN
KLIEDLVTYS KINFSEKRFK KTDLNLLLKK VINDLKKIIN DHNAVITVDA LPHLNIVASQ
FHMLFIHLIS NAIKFAQQNS VPQIKISVHE PDVKEFSSLG ADTDTEYIVL SVSDNGIGFK
KDFEYQIFDP FYKLQSNEQH YGSGLGLTLV QTIVSNHKGF IKASSEVGKG TTLYIYLPLQ
KSITENTATA ALTFDEILNI KQSQIPY
//
