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Database: UniProt
Entry: A0A223P3I5_9SPHI
LinkDB: A0A223P3I5_9SPHI
Original site: A0A223P3I5_9SPHI 
ID   A0A223P3I5_9SPHI        Unreviewed;      1222 AA.
AC   A0A223P3I5;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=protein-glutamate O-methyltransferase {ECO:0000256|ARBA:ARBA00012534};
DE            EC=2.1.1.80 {ECO:0000256|ARBA:ARBA00012534};
GN   ORFNames=MuYL_4727 {ECO:0000313|EMBL:ASU36610.1};
OS   Mucilaginibacter xinganensis.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Mucilaginibacter.
OX   NCBI_TaxID=1234841 {ECO:0000313|EMBL:ASU36610.1, ECO:0000313|Proteomes:UP000215002};
RN   [1] {ECO:0000313|EMBL:ASU36610.1, ECO:0000313|Proteomes:UP000215002}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BJC16-A31 {ECO:0000313|EMBL:ASU36610.1,
RC   ECO:0000313|Proteomes:UP000215002};
RG   Henan University of Science and Technology;
RA   You X.;
RT   "Complete genome sequence of Mucilaginibacter sp. strain BJC16-A31.";
RL   Submitted (AUG-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; CP022743; ASU36610.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A223P3I5; -.
DR   KEGG; muc:MuYL_4727; -.
DR   OrthoDB; 9813151at2; -.
DR   Proteomes; UP000215002; Chromosome.
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:UniProtKB-UniRule.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd16434; CheB-CheR_fusion; 1.
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; 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; 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; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013655; PAS_fold_3.
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   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08447; PAS_3; 1.
DR   PRINTS; PR00996; CHERMTFRASE.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00138; MeTrc; 1.
DR   SMART; SM00091; PAS; 2.
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); 2.
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.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 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:UP000215002};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          2..196
FT                   /note="CheB-type methylesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50122"
FT   DOMAIN          210..482
FT                   /note="CheR-type methyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50123"
FT   DOMAIN          871..942
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          947..1000
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          1011..1222
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          650..737
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          854..881
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   ACT_SITE        26
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT   ACT_SITE        53
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT   ACT_SITE        143
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ   SEQUENCE   1222 AA;  137998 MW;  CF3B6E972E8D44C4 CRC64;
     MPLPNLVDKD LVLSDNQFPV VGIGASAGGI EAFKLFLQSV PEKSGMAYVF VQHLSPDYNS
     YLPEIFKKST KIPVLLIADN IHLEPDHVYI IPPGYILTAT DGILKLEPIK NKKVKTIDIF
     FSSLAVVHQS FAIGIVLSGA LDDGTVGLQV IKAYGGLTFA QSEDSATFDS MPRSAIRSGA
     VDFILPAEQI MSKLISINQP FNDGTIEGQI GKNEPEHDEE IFKQLLTVLR IRRGVDFVNY
     KQSTIKRRIV RRMALVKIEK PKEYLNFLRE NKPEQDALYN DMLISVTNFF RDPQSFEVLC
     ESILPAILIH KTPNEAIRIW VAGCATGEEA YSIAICLQEY LGDKASARKI QIFATDVSEI
     AIARARTGIY RQNDLGGLST LQIQQFFNKL DGSYQVNKTI RDMCVFAHHN LLKDPPFSRI
     DLVSCRNVMI YLEPVLQKRA LSTFHYALNE RGYLMLGKSE TIGTSTDIFT HVNKTQKIYQ
     SKGPHGRVRA VTSERSEQTL KAIDQIIPEN SSENDINKVA DALLLSKYTP AGVMVNQSFD
     ITQFRGKTDP WLAVSPGKPS FNVLKMAREG LSFEIRSLLH LAKTKQEAMR KEGISFKIDN
     ERHYVNIEVV PLSDTEDNYY LILFQNSMLS EPSSLTDSSK LNSRHTPENI NAWVQQIDQL
     EKELTQTRED MRSITETQEA ANEELQSANE ELLSGSEELR SLNEELETST EELQSSNEEI
     TIVNNELLDR NEQLNNSRKY TEEIFNTIHD PLVILDKDLV VLRATDGFYN MFRVNEEDTE
     GKFIYDLGNK QWDIPALREQ LEKTLPQQGF FKAFEVDHIF STIGRRIMQL TARQFDTYTD
     EKLTLLAIHD ITDKRKVEEG LAEAERLLAE SKERLHFAIE SAGIGAWDFN PITKELIWDN
     RCKELYGLAP ADSIDYAGFL SYIHTDDRSA TDNSINKTLK GANRGEFNEE YRTIGKNDQK
     LRWIKSKGKA YFDKDNKATR FIGTVLDVSI EKDAEQSTIE MLRKKDEFIS IASHELKTPV
     TSLKASLQLL DRMKNDPSPM LPRFLDQANR SMLKITHLID ELLNVNSMKE GQLRLNKSVF
     VIAGMLKDCC GHVRAAGVHE LVVQGDETLK VDADEDRIEQ VVVNLVNNVV KYAPESKNIY
     FIVEKEGNTA KVSVKDTGLG ISADKIPHLF DRYYRADYGG GQYSGMGLGL YISSEIIKRH
     GGKIGVQSEV GKGSTFWFTL PL
//
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