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Database: UniProt
Entry: A0A1G8MG83_9RHOB
LinkDB: A0A1G8MG83_9RHOB
Original site: A0A1G8MG83_9RHOB 
ID   A0A1G8MG83_9RHOB        Unreviewed;      1046 AA.
AC   A0A1G8MG83;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=MCP methyltransferase/methylesterase, CheR/CheB with PAS/PAC sensor {ECO:0000313|EMBL:SDI66845.1};
GN   ORFNames=SAMN04487993_100828 {ECO:0000313|EMBL:SDI66845.1};
OS   Salipiger marinus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Salipiger.
OX   NCBI_TaxID=555512 {ECO:0000313|EMBL:SDI66845.1, ECO:0000313|Proteomes:UP000199093};
RN   [1] {ECO:0000313|EMBL:SDI66845.1, ECO:0000313|Proteomes:UP000199093}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26424 {ECO:0000313|EMBL:SDI66845.1,
RC   ECO:0000313|Proteomes:UP000199093};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FNEJ01000008; SDI66845.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G8MG83; -.
DR   STRING; 555512.SAMN04487993_100828; -.
DR   Proteomes; UP000199093; 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: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   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; IPR001610; PAC.
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   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR24422; CHEMOTAXIS PROTEIN METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR24422:SF25; CONSERVED HYPOTHETICAL CHEMOTAXIS PROTEIN; 1.
DR   Pfam; PF01339; CheB_methylest; 1.
DR   Pfam; PF01739; CheR; 1.
DR   Pfam; PF03705; CheR_N; 1.
DR   Pfam; PF08447; PAS_3; 1.
DR   PRINTS; PR00996; CHERMTFRASE.
DR   SMART; SM00138; MeTrc; 1.
DR   SMART; SM00086; PAC; 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   PROSITE; PS50122; CHEB; 1.
DR   PROSITE; PS50123; CHER; 1.
DR   PROSITE; PS50113; PAC; 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:0000313|EMBL:SDI66845.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199093};
KW   Transferase {ECO:0000313|EMBL:SDI66845.1}.
FT   DOMAIN          4..187
FT                   /note="CheB-type methylesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50122"
FT   DOMAIN          216..450
FT                   /note="CheR-type methyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50123"
FT   DOMAIN          883..935
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   COILED          613..686
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   ACT_SITE        16
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT   ACT_SITE        43
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT   ACT_SITE        136
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ   SEQUENCE   1046 AA;  113132 MW;  890DC13F33EB7A69 CRC64;
     MTDSGQGPVL VGIAASAGGL EACMTLLRAL PAGCGGSFVL AQHMAPDHQS LLPDLLGHDM
     PLAVRELSGP TEPQPGCLYL PPPGWDVVLD QGRIRPVAPQ AQGTAPKPSA DRLFQSLAAG
     RGEDCIGIVL SGTGSDGTYG LLSIREAGGL TLAQDPATAR YEAMPHSAIR SGGVDLVLTP
     QRIGAHLATL LCRPQAAIPL DLDRAEGGSG AELFALLQAR QGADFRGYKD STLTRRLQRR
     MVARDVADLG AYVALCREDA AELDALFRDL LISVTRFFRD PEAFAALAEQ LDARVAQATR
     PGAPLRLWVP GCATGEEAWS LAILAAEALG GLHQLDRARL QVFATDIDDR ALDLARQASY
     PASALAQIPP AYRRYFDMAG ERITVGSRLR NVVTFSHHNV VQDPAFLSLD LVSLRNVLIY
     FDTGLQEQVL SRLHYALAPR GLLFLGSAET TGPLDSQFAP LPPRHRIFAK RTGAVAPRAA
     LPGPAQADPG FDALARAVVP QGFLCGADGR ILKIYGDLAP FVALTDPFHG GMTLAALRGP
     LAGAATALLH LALHGGQRQT GLWKDLEGRD FDRVRLRAYP VAREAGPPLI LFGVETGTRP
     RAEAAPLDRA AYLEHLETEL ARTRDRLAST SGQLRSTGET LQTLIEALQV ANEDLQSANQ
     ELETSNEELQ STNEELITVN EELILKSAEL QRMTAELDGL VRELPTETMM LGPDLMIRHA
     SERAIRTFRL RRDSAGFGHL TQCHMPPGLP ALAAICTQAL REGTPQQHQY EDRDQLYTVT
     VTPLVAADDP PVGLTVVLSV AEMRYDRMLS QAIRSFGPIG IWQVEIGKGT VDWSEETFVI
     HGMQPSGAPV PVETAVAMFH EDDRLMVRQL AQAAIADDRD NKFHFFARLR RIDGRIIVVE
     SAGAIIRDEA GRGVGLVGVV RDCTRHRSED ILLRQLNSLL ALEGSGFWSY TFTSGLSYFS
     PLACAHLGLD VETAPQLEEI LARIDPQDRA HCRWLLTEAP CGTPLVAELS ASGRRFRLSL
     YGSPDSSQRF GLLTAIPDLA QRPEDV
//
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