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Database: UniProt
Entry: A0A110B2Z0_9SPHI
LinkDB: A0A110B2Z0_9SPHI
Original site: A0A110B2Z0_9SPHI 
ID   A0A110B2Z0_9SPHI        Unreviewed;       609 AA.
AC   A0A110B2Z0;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=protein-glutamate O-methyltransferase {ECO:0000256|ARBA:ARBA00012534};
DE            EC=2.1.1.80 {ECO:0000256|ARBA:ARBA00012534};
GN   Name=cheR {ECO:0000313|EMBL:BAU54038.1};
GN   ORFNames=MgSA37_02209 {ECO:0000313|EMBL:BAU54038.1};
OS   Mucilaginibacter gotjawali.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Mucilaginibacter.
OX   NCBI_TaxID=1550579 {ECO:0000313|EMBL:BAU54038.1, ECO:0000313|Proteomes:UP000218263};
RN   [1] {ECO:0000313|EMBL:BAU54038.1, ECO:0000313|Proteomes:UP000218263}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SA3-7 {ECO:0000313|EMBL:BAU54038.1,
RC   ECO:0000313|Proteomes:UP000218263};
RA   Lee J.S., Lee K.C., Kim K.K., Lee B.W.;
RT   "Genome sequence of Mucilaginibacter gotjawali.";
RL   Submitted (DEC-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}.
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DR   EMBL; AP017313; BAU54038.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A110B2Z0; -.
DR   KEGG; mgot:MgSA37_02209; -.
DR   OrthoDB; 9813151at2; -.
DR   Proteomes; UP000218263; 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:UniProtKB-EC.
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; 3.40.50.180; Methylesterase CheB, C-terminal 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; 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   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   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:BAU54038.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000218263};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:BAU54038.1}.
FT   DOMAIN          25..214
FT                   /note="CheB-type methylesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50122"
FT   DOMAIN          221..493
FT                   /note="CheR-type methyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50123"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..26
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   609 AA;  68252 MW;  321CDC92689A1AF6 CRC64;
     MKKATNHTES KKMAASQPAD TSPHQQSAAF VVGIGASAGG LEALKILFDH MPPDSGMAFV
     IVQHLDPTHR SMLTDLISPH TKMMVKEIIN GTTVKPDCVY VIPPDRELAI SEQRLFLAAM
     PDERIKRRPI DSFFRSLAED LKENAIGIIL SGTGTEGTLG LKEIKAAGGL AIVQDPETAL
     FDGMPRSAIT ARVADYIMPP GKIPEKLLDY INKKQNNDGR IVSGPPDLVE NDLKGIFQAI
     RTQTGYDFTN YKTNTIARRI SKRIALNGFN AVEDYTKFLQ DHPNEITKLY KDFLIGVTSF
     FRDKEVFNSF EKKAVPHLLE KCRDRQELRA WICGCSTGEE AYSLAIILKE ALEKNRQYLK
     VTIFASDIDD EAIEFARNGI YNESALADVS PERLAQYFVK KENGYQPKKE IREMVVFAHH
     NLIKDPPFSK MDLISCRNLL IYIKGDLQKK VIPVFHYSLN TDGLLLLGTS ESIGEHGDLF
     TPIDAKHKIF KKKNINSRKP YPIFDLPFVE RKLDVKKQDM SSVVSKITRV SDIAEKLLAE
     PSQPPSVIID MNNDALYFSG NTGIYLAPPD GVANWNILEM AKKGLRTVLE KAIKKHALPK
     RPLKKIALR
//
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