ID S9RWK3_9RHOB Unreviewed; 1154 AA.
AC S9RWK3;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Chemotaxis protein methyltransferase CheR {ECO:0000313|EMBL:EPX78394.1};
DE EC=2.1.1.80 {ECO:0000313|EMBL:EPX78394.1};
GN ORFNames=Salmuc_03502 {ECO:0000313|EMBL:EPX78394.1};
OS Salipiger mucosus DSM 16094.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Salipiger.
OX NCBI_TaxID=1123237 {ECO:0000313|EMBL:EPX78394.1, ECO:0000313|Proteomes:UP000015347};
RN [1] {ECO:0000313|Proteomes:UP000015347}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16094 {ECO:0000313|Proteomes:UP000015347};
RX PubMed=25197501; DOI=10.4056/sigs.4909790;
RA Riedel T., Spring S., Fiebig A., Petersen J., Kyrpides N.C., Goker M.,
RA Klenk H.P.;
RT "Genome sequence of the exopolysaccharide-producing Salipiger mucosus type
RT strain (DSM 16094(T)), a moderately halophilic member of the Roseobacter
RT clade.";
RL Stand. Genomic Sci. 9:1331-1343(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
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:EPX78394.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; APVH01000039; EPX78394.1; -; Genomic_DNA.
DR RefSeq; WP_020039150.1; NZ_KE557280.1.
DR AlphaFoldDB; S9RWK3; -.
DR STRING; 1123237.Salmuc_03502; -.
DR eggNOG; COG1352; Bacteria.
DR eggNOG; COG2201; Bacteria.
DR eggNOG; COG2202; Bacteria.
DR HOGENOM; CLU_000892_0_2_5; -.
DR Proteomes; UP000015347; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro.
DR GO; GO:0004673; F:protein histidine kinase 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: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; 3.30.565.10; 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; IPR036890; HATPase_C_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR011102; Sig_transdc_His_kinase_HWE.
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; PF07536; HWE_HK; 1.
DR Pfam; PF13596; PAS_10; 1.
DR PRINTS; PR00996; CHERMTFRASE.
DR SMART; SM00911; HWE_HK; 1.
DR SMART; SM00138; MeTrc; 1.
DR SMART; SM00091; PAS; 3.
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; 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.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chemotaxis {ECO:0000256|PROSITE-ProRule:PRU00050};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00050};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:EPX78394.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000015347};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EPX78394.1}.
FT DOMAIN 24..207
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT DOMAIN 221..483
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT REGION 495..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 637..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 1154 AA; 128949 MW; 51BFA6B7DB09151E CRC64;
MSHDDRPDES LISEAETASE RTCIVGVGAS AGGLEAIREM LSEADASSNF AYVVVQHLDP
NHESLLAELL GRHTDLEVLQ AAGGERIQRG RVYIIPPGHG LLVRDGELTL TDFEQPRGLR
RPIDDFFESL AEDQGRFAAC VILSGTGADG SAGLRAIKEH GGLCLVQDPD TAKYDGMPVS
AQNTGMVDFV RRPSRIIESI HQYYARTVYR ISDEKLARTI EDSVDDICAV LKKTVGHDFS
GYKKSTLVRR IQRRIQVLDL RDAEDYLRRV RTDSDECEVL FRELLINVTR FFRDPEHFEA
LRREVVPDLV RDFEGEELRV WVPGCSSGEE AYTMAMIFAH ELHEQRRSFK VQVFATDIDE
QMLRIAREGV YPHAALADVP EELRDRYTIA REGSFQIPAQ IRDMIRFSVH SVVRDPPFSN
IDLLSCRNLL IYFGEKLQTQ ALPIFHYSLK PGGILFLGPS ETVGRFDELF PPINQQARIF
RRNNARTEYP LHLRTMPSNR LPSPRRSALG GGSREAARNT LENTDVAERV LQSYAPATLH
LTPSGQILAS TGRLGKYVEL QPGQVEDQHV QSIARPGLRE AVSALIRKAG RVSHKSVTRD
LVAQSEFGRQ QLDLVADPLP DGTLLLVFRD RDRFEAHDED DVEEVEPSDS HVQSLEDELR
STRARLHTTV EELETANEEL KSSNEEMMSM NEELQSTNEE LATVNDELKT KVDELSVANA
DLSNFFASTT LPLVVVDAKG KIRNFTEAIN SIYPLRKTDR GRPLAEVTSA LNESREVIGA
IEEVMATSEL RNMRVTEIEG DRTWTLAITP YLSRDGSREG ATLVFTELTR ALYLQAELDR
ERERLQLALE VAEMGVWELD PSKGTLMLDS KGRELFEFAP DGAEPRVPDI LATLCEGDRE
RLEAALQATS DGAPVDETFT LTERHNGRSL RFVGNQTDHG RETRFLGVVF DVTAEIEARR
VREVMIREMN HRVKNFFSII SGMVRVAGRT SESVPDLVQG IESRVNALAR SHDMTQRPAE
RGPVTMTDAV GAALEPYTDS AETEVEGPQV LIAAKDLTAL SLLLHEWATN AAKYGVLGPV
EGRLEVHWAY AQDGKVTLVW NEIYAEALGE VTQGKAGFGS TLVRLAATQL GGEVTVDSSV
EQRTTRLTYD PREL
//
