ID A0A1S1Y474_9GAMM Unreviewed; 825 AA.
AC A0A1S1Y474;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=protein-glutamate O-methyltransferase {ECO:0000256|ARBA:ARBA00012534};
DE EC=2.1.1.80 {ECO:0000256|ARBA:ARBA00012534};
GN ORFNames=BJL95_15890 {ECO:0000313|EMBL:OHX35819.1};
OS Methylomonas sp. LWB.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylomonas.
OX NCBI_TaxID=1905845 {ECO:0000313|EMBL:OHX35819.1, ECO:0000313|Proteomes:UP000180009};
RN [1] {ECO:0000313|EMBL:OHX35819.1, ECO:0000313|Proteomes:UP000180009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LWB {ECO:0000313|EMBL:OHX35819.1,
RC ECO:0000313|Proteomes:UP000180009};
RA Stephenson J., Kumaresan D., Hillebrand-Voiculescu A.M., Murrell J.C.;
RT "Draft genome sequence of the methane oxidising bacterium Candidatus
RT Methylomonas sp. LWB isolated from Movile Cave.";
RL Submitted (OCT-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};
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:OHX35819.1}.
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DR EMBL; MKMC01000034; OHX35819.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S1Y474; -.
DR Proteomes; UP000180009; 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:InterPro.
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; 1.10.287.620; Helix Hairpins; 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; IPR000700; PAS-assoc_C.
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 SUPFAM; SSF57997; Tropomyosin; 1.
DR PROSITE; PS50122; CHEB; 1.
DR PROSITE; PS50123; CHER; 1.
DR PROSITE; PS50113; PAC; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000180009};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..174
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT DOMAIN 190..458
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT DOMAIN 766..819
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT REGION 638..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..666
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 825 AA; 92083 MW; A82663D3A5172C4C CRC64;
MEALEQFFAE VPAACGVAFV VVQHLDPHHQ GMLPALLQRT SQLTVIQAGD HMPVKPDWVY
VIPPNKDLSI QRGKLRLLEP RVLRGLRLPI DAFFKALADD QHERAIGVIL SGMGSDGTLG
LRAIKENAGL AVAQSPESAQ FDSMPRSAID AGLADIVAPP RVLWEKILAY LKHSPRGLHA
TPETAPASKS RSSLEQILIL LRDRTGNDFS LYKKNTMYRR IERRMGLRQI DAIAGYADYL
RENPQELDLL FKELLIGVTS FFRDPEVWAS LKTEVIPALL AEYPAGKALR AWVPACSTGE
EAYSLAMIFK EVLAESQSPR PFKLQIFATD LDQDAIDKAR QGFFPATIAG EVSEDRLSRF
FNVDGGGYRI KKDIREMVIF APHNVIMDPP FTKLDLLCCR NLLIYLSQEL QQKLILLFHY
TLASHGILTL GNAETIGNAS HLFSATDHKL RLYRRIDTPF PLNVDFPTKY FPVASMIEDT
EKHPPIANLQ TLADQLLLQH FAPAAVLVNA DGDILYISGR TGKYLEPAAG KANWNIHAMA
RDGLRHELIG ALKKARTETD VVQVAGLTVA NDSGGQTVNL SVQAIHKPDA LKGMLMVVFT
DVAAAPAGKV SRKSPNAAQT LLQAELQHTQ EDLQTLREEM QTSQEELKSA NEELQSTNEE
LQSTNEELTT SKEEMQSLNE ELQTVNAELQ IKVDDLSRAS NDMNNLLNSM EIATVFLDGT
LNIRRFTSHI GHLFKLIAAD VGRPLSDIVT DLDYPDLQQD AREVLRTLVF VEKQIRASDE
RWFKVRIMPY RTQDNLIDGV VITFIDISET KKLEAELRNS HEKSE
//
