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Database: UniProt
Entry: A0A5B1BMA3_9FLAO
LinkDB: A0A5B1BMA3_9FLAO
Original site: A0A5B1BMA3_9FLAO 
ID   A0A5B1BMA3_9FLAO        Unreviewed;       914 AA.
AC   A0A5B1BMA3;
DT   13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2019, sequence version 1.
DT   02-APR-2025, entry version 17.
DE   RecName: Full=protein-glutamate O-methyltransferase {ECO:0000256|ARBA:ARBA00012534};
DE            EC=2.1.1.80 {ECO:0000256|ARBA:ARBA00012534};
GN   ORFNames=F0000_00450 {ECO:0000313|EMBL:KAA1248099.1};
OS   Aquimarina sp. RZ0.
OC   Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Aquimarina.
OX   NCBI_TaxID=2607730 {ECO:0000313|EMBL:KAA1248099.1, ECO:0000313|Proteomes:UP000323420};
RN   [1] {ECO:0000313|EMBL:KAA1248099.1, ECO:0000313|Proteomes:UP000323420}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RZ0 {ECO:0000313|EMBL:KAA1248099.1,
RC   ECO:0000313|Proteomes:UP000323420};
RA   Chen X.-Y.;
RL   Submitted (SEP-2019) 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: 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:KAA1248099.1}.
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DR   EMBL; VTZU01000001; KAA1248099.1; -; Genomic_DNA.
DR   RefSeq; WP_149622720.1; NZ_VTZU01000001.1.
DR   AlphaFoldDB; A0A5B1BMA3; -.
DR   Proteomes; UP000323420; 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; cd02440; AdoMet_MTases; 1.
DR   CDD; cd16434; CheB-CheR_fusion; 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; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR050903; Bact_Chemotaxis_MeTrfase.
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; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR000673; Sig_transdc_resp-reg_Me-estase.
DR   PANTHER; PTHR24422; CHEMOTAXIS PROTEIN METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR24422:SF27; PROTEIN-GLUTAMATE O-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; 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:UP000323420};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          24..207
FT                   /note="CheB-type methylesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50122"
FT   DOMAIN          225..465
FT                   /note="CheR-type methyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50123"
FT   COILED          661..741
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   ACT_SITE        30
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT   ACT_SITE        57
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT   ACT_SITE        149
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ   SEQUENCE   914 AA;  104956 MW;  566A7F01E6DD9E93 CRC64;
     MKNTLTNKID KKKHGDLQNE QFFIIGIGAS AGGLEALKLF FDYVPSDCKH SFVIVQHLSP
     DYKSLMVELL AKNTSLPIFE VKNNMVVAPG SIYLIPARKN MKFKNGRLSL TDKPQSHHLN
     LPIDIFFHSL AEELKERSIA IILSGTGTDG SRGVHAVKEM GGMVMVQSPA TAKFDGMPNS
     AIAIGVVDYI VPVAQMPKEL LDYIATPHSI DTDESVKMLS DEYSLSKILS RIKEHTNLDF
     YGYKRPTLIR RIARRMYATQ HKNLKEYYNY IKENDAEVQL LYREFLIGVT KFFRDNDAFQ
     ILENKVLPEL VAKKKTDQEF KVWCIGCSTG EEVYSIAILL DEILERKGKK LNVRIFGTDI
     EPDNLEKASK AIYSGNITKD VSFDRLQKYF IKKGNQYYVN QKIRNKAIFS CHDVLKDPTI
     NKLDLVICRN MLIYINTEMQ QKVLSKIHYA LNKDSILFLG SSETIGDAGN LFNTIDKKWK
     LYRTKEIPFR SARDFTRYSD IHKHGLLERS AFKVVARKKP LENNLSEILN ETLLDQFGVA
     GIYIDEHYHI MHAVGDFKKY IEIPDDQFSL NLLKMLPENL FIPTSTAIRK VIKQNEKVIY
     EGVKWRTKNT IRTINILVNP FELNTTRLNC FLVVFIEEKV EKETATIIKN TLDNPKTAKL
     LVAIEEELKL TKESLQTTIE EVETSNEELQ TTNEELLSSN EELQSTNEEL QSVNEELHTV
     NAEHQNKIGE LLKLNNDIEN LIQSTHIPTI FLDSDLNIRK FTPNITEQFN LLDTDIGRPI
     SHFTSKFGEE DSSNFLQIID RVLGSNKPEQ KEIQISEGKW YLQRIFPFID HSSHNNSGGV
     VITFVDINAI KIGQEKMRLK TQELESSNDK LSRFNKAAVG REERMIELKK IINEQCEQLN
     REPLFDLNFT KNEL
//
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