ID A0A221KHS4_VITFI Unreviewed; 985 AA.
AC A0A221KHS4;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=protein-glutamate O-methyltransferase {ECO:0000256|ARBA:ARBA00012534};
DE EC=2.1.1.80 {ECO:0000256|ARBA:ARBA00012534};
GN ORFNames=VITFI_CDS2606 {ECO:0000313|EMBL:ASM78383.1};
OS Vitreoscilla filiformis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Vitreoscilla.
OX NCBI_TaxID=63 {ECO:0000313|EMBL:ASM78383.1, ECO:0000313|Proteomes:UP000199729};
RN [1] {ECO:0000313|EMBL:ASM78383.1, ECO:0000313|Proteomes:UP000199729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15551 {ECO:0000313|EMBL:ASM78383.1,
RC ECO:0000313|Proteomes:UP000199729};
RA Contreras S., Sagory-Zalkind P., Blanquart H., Iltis A., Morand S.C.;
RT "Complete Genome Sequence of the cosmetic ferment Vitreoscilla filiformis
RT (ATCC15551).";
RL Submitted (JUL-2017) 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; CP022423; ASM78383.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A221KHS4; -.
DR KEGG; vff:VITFI_CDS2606; -.
DR OrthoDB; 9816309at2; -.
DR Proteomes; UP000199729; 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: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; 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; 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.
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:ASM78383.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199729};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ASM78383.1}.
FT DOMAIN 23..210
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT DOMAIN 233..503
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT COILED 661..734
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 34
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 61
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 152
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 985 AA; 108493 MW; 363AA65C042F5711 CRC64;
MTDDHLTLGT PSEPSTLATP VSVFTGHVVC IGASAGGLDA LERFFRHCPN HTGAAFVVIQ
HLSPDHKSMM CNLLARHTRM PVVLVQDGMD IQPDRLHLIP PGSVMHVREG HLHLTPKNPH
GLTLPIDIFF NALARACGPR AVGVILSGTG TDGTRGATAL NEAGGFLMAQ EPESASFDGM
PRSVIATGLV DAVLPPEKLP LRLLSHLNKN AAPAEGGFVP IQRYATLNPQ EVFSAILQLL
HQIGGIDFSD YKSSTLMRRI DRRQQVRHTP ELHQYLELLE NDRAEVITLR RELLISVTSF
FRDPETFNLL AEKVIAPMVA AKSAGETIRV WIAGVATGEE AYSVGILFLE AFENARLWPH
LKIFATDVDQ QCVATAGMGQ YPESAAAEIH PERLERFFVR KDRVFYVKND LRQCVVFARH
NLLADPPFTK MDLVVCRNTL IYFNLFAQER ALRSLQYALN DGGVLLLGAS ESFAAVADGV
HVINAQHKLF RRKGPSVLLP AARRIADVAR PLPTGKTMPV VRQRRQAPGA FSEAGLQTLM
ARFAPPAMLV NAHHEVLHLY GAVSRYFRAK EGVASLDVCR LLPDELVPVA SALLYKVERD
RTSLSSNVLA VQVPGEGRVG LRLSAHPVES DGEACLTLLC FESEETTQEG VTETPPAINV
HSEAADRLAI LERELAATRE NLQATIEELE ASNEELQATN EEMMASNEEL QSSNEELQSV
NEEMSTVNAE LQEKMLLLSR VNADLDSMAK AAGVATVFVD GHFNITRFSP DATQIFKLRE
TDLGRQLDDI THVLDYPELM EDLGRTLKLQ RLLEREVLSA DGKRTFLVRM LPYLVPSSID
RGAVATFVDV TAIHDARRLQ AIIDALPEHI AVVDPVGVIC MVNAAWRRFA QANGDPDMVR
TGVGVNYLEV CQVRHPPDQS PIDTVLKGLR QVLDGSLPRF SLEYSCHSPT EQRWFVMHAA
PIIGVEYGAV ISHVNITSWY LKEAS
//
