ID A0A316G4I8_9RHOB Unreviewed; 1129 AA.
AC A0A316G4I8;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Two-component system CheB/CheR fusion protein {ECO:0000313|EMBL:PWK55809.1};
GN ORFNames=C8D95_106205 {ECO:0000313|EMBL:PWK55809.1};
OS Silicimonas algicola.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=1826607 {ECO:0000313|EMBL:PWK55809.1, ECO:0000313|Proteomes:UP000245390};
RN [1] {ECO:0000313|EMBL:PWK55809.1, ECO:0000313|Proteomes:UP000245390}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 103371 {ECO:0000313|EMBL:PWK55809.1,
RC ECO:0000313|Proteomes:UP000245390};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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:PWK55809.1}.
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DR EMBL; QGGV01000006; PWK55809.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316G4I8; -.
DR Proteomes; UP000245390; 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:RHEA.
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; 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; IPR000700; PAS-assoc_C.
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 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.
DR PROSITE; PS50113; PAC; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chemotaxis {ECO:0000256|PROSITE-ProRule:PRU00050};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00050};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000245390};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..190
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT DOMAIN 204..465
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT DOMAIN 768..819
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT COILED 636..698
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 807..834
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 13
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 40
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 132
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 1129 AA; 126599 MW; 623E04DC26064E46 CRC64;
MDTSLPIIGV GASAGGLEAL RELFAGYKGT TGMAFVVIQH LDPNHESLMA QLIERYTSMH
VRQAEGGEAL EADHVYVIPP GHGLVVGDRT LHLTEFVDPR GLRRPIDDFF ESLAEDVGAL
SACVILSGTG GDGSRGLRAI KENGGVCLAQ EPETARYDGM PVSAMRTGLV DVVAPPSEML
SYLRRFFNFQ PGEPNGGPAE IVDHLEDLCQ SLSQATGHDF SGYKRSTMAR RVARRMQVLG
IDSATTYADR VHKDDGECMA LFSDLLINVT KFFRDTHEFE ALREIVVAPL VERAMEDDEI
RVWVAGCSSG EEAYSMAMLF ADEIEKRNRR LNVQIFATDI DEKMLSIARS GTYPLSSLSD
IPAEYRQRFT IGNNQHVVIA PKIRDMVRFS LHSLIKDPPF SSMDLISCRN LLIYFEETLQ
RQVVPLFHFA LRQDGFLFLG SSEAIQRYED LFEVVDQSAR VFLRRTVQGR YNLQIAQPRA
RRAERLPGLS DQVMSQRREV SAEADALRRI AESYAPVSLL VDAEGNLLSR WGKVGRYLDF
PDRIERTVHV PSLARAGLRD VLGGLLRDVV KGAARAIVRD VEVHTDFGLM TVNVMCEPID
DDAYLLVIRE SGELTPIDTD DYLEVRPEEG QVRYLEEELQ ATRYRLRTAI EELETTNEEL
KSSNEEMMSM NEELQSTNEE LTTVNDELKT KVDQLIVANA DLTNFFTSTE LVVVVVDRDL
RVRSTSSSVD RVFPGAGDKD GTALDQLEAN LTDSEFVERL TQAAKQDTSS EFRATSSDGT
REFLGRATPY KKKDGSTDGA ILVLTDVTET LALARDLEEE RERLRLALEV ARIGIWEYEP
DTDFTRLDKT ERWLLNLGEG EGDTMERILS RMTAEDRDRV NTALRQAMDG TRDFDEVFSI
PLGGGRRRWL HGLGKRHFRH RGRKFIGVTY DVTAERELLS QRELMIREMN HRLKNLFAII
SALVSICARE AQDVDDFAME LRSRIRALGQ SHSLTNEGTE VRQATLRGIV ETVLEPARDQ
QSFVYEGLDL EVDTSQLTSL ALIFHEWATN ATKYGALTVP DGIVTVRVED GEDTVRVEWI
ESGKDRSRSS GSGFGTALIE ATALQLRATV EGEETDEGFR RTLVFPKLV
//
