ID CHEB1_BURTA Reviewed; 364 AA. AC Q2STS8; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2006, sequence version 1. DT 28-JAN-2026, entry version 114. DE RecName: Full=Protein-glutamate methylesterase/protein-glutamine glutaminase 1 {ECO:0000255|HAMAP-Rule:MF_00099}; DE EC=3.1.1.61 {ECO:0000255|HAMAP-Rule:MF_00099}; DE EC=3.5.1.44 {ECO:0000255|HAMAP-Rule:MF_00099}; GN Name=cheB1 {ECO:0000255|HAMAP-Rule:MF_00099}; GN OrderedLocusNames=BTH_I3177; OS Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CCUG 48851 / OS CIP 106301 / E264). OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria; OC Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=271848; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700388 / DSM 13276 / CCUG 48851 / CIP 106301 / E264; RX PubMed=16336651; DOI=10.1186/1471-2164-6-174; RA Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C., RA DeShazer D.; RT "Bacterial genome adaptation to niches: divergence of the potential RT virulence genes in three Burkholderia species of different survival RT strategies."; RL BMC Genomics 6:174-174(2005). CC -!- FUNCTION: Involved in chemotaxis. Part of a chemotaxis signal CC transduction system that modulates chemotaxis in response to various CC stimuli. Catalyzes the demethylation of specific methylglutamate CC residues introduced into the chemoreceptors (methyl-accepting CC chemotaxis proteins or MCP) by CheR. Also mediates the irreversible CC deamidation of specific glutamine residues to glutamic acid. CC {ECO:0000255|HAMAP-Rule:MF_00099}. CC -!- CATALYTIC ACTIVITY: CC Reaction=[protein]-L-glutamate 5-O-methyl ester + H2O = L-glutamyl- CC [protein] + methanol + H(+); Xref=Rhea:RHEA:23236, Rhea:RHEA- CC COMP:10208, Rhea:RHEA-COMP:10311, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17790, ChEBI:CHEBI:29973, CC ChEBI:CHEBI:82795; EC=3.1.1.61; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00099}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-glutaminyl-[protein] + H2O = L-glutamyl-[protein] + NH4(+); CC Xref=Rhea:RHEA:16441, Rhea:RHEA-COMP:10207, Rhea:RHEA-COMP:10208, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29973, CC ChEBI:CHEBI:30011; EC=3.5.1.44; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00099}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00099}. CC -!- DOMAIN: Contains a C-terminal catalytic domain, and an N-terminal CC region which modulates catalytic activity. {ECO:0000255|HAMAP- CC Rule:MF_00099}. CC -!- PTM: Phosphorylated by CheA. Phosphorylation of the N-terminal CC regulatory domain activates the methylesterase activity. CC {ECO:0000255|HAMAP-Rule:MF_00099}. CC -!- SIMILARITY: Belongs to the CheB family. {ECO:0000255|HAMAP- CC Rule:MF_00099}. 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; CP000086; ABC38609.1; -; Genomic_DNA. DR RefSeq; WP_009910098.1; NC_007651.1. DR AlphaFoldDB; Q2STS8; -. DR SMR; Q2STS8; -. DR GeneID; 45122859; -. DR KEGG; bte:BTH_I3177; -. DR HOGENOM; CLU_000445_51_0_4; -. DR Proteomes; UP000001930; Chromosome I. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro. DR GO; GO:0008984; F:protein-glutamate methylesterase activity; IEA:UniProtKB-UniRule. DR GO; GO:0050568; F:protein-glutamine glutaminase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-UniRule. DR CDD; cd16432; CheB_Rec; 1. DR CDD; cd17541; REC_CheB-like; 1. DR FunFam; 3.40.50.180:FF:000001; Protein-glutamate methylesterase/protein-glutamine glutaminase; 1. DR FunFam; 3.40.50.2300:FF:000060; Protein-glutamate methylesterase/protein-glutamine glutaminase; 1. DR Gene3D; 3.40.50.2300; -; 1. DR Gene3D; 3.40.50.180; Methylesterase CheB, C-terminal domain; 1. DR HAMAP; MF_00099; CheB_chemtxs; 1. DR InterPro; IPR008248; CheB-like. DR InterPro; IPR035909; CheB_C. DR InterPro; IPR011006; CheY-like_superfamily. DR InterPro; IPR000673; Sig_transdc_resp-reg_Me-estase. DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver. DR NCBIfam; NF001965; PRK00742.1; 1. DR NCBIfam; NF009206; PRK12555.1; 1. DR PANTHER; PTHR42872; PROTEIN-GLUTAMATE METHYLESTERASE/PROTEIN-GLUTAMINE GLUTAMINASE; 1. DR PANTHER; PTHR42872:SF6; PROTEIN-GLUTAMATE METHYLESTERASE_PROTEIN-GLUTAMINE GLUTAMINASE; 1. DR Pfam; PF01339; CheB_methylest; 1. DR Pfam; PF00072; Response_reg; 1. DR PIRSF; PIRSF000876; RR_chemtxs_CheB; 1. DR SMART; SM00448; REC; 1. DR SUPFAM; SSF52172; CheY-like; 1. DR SUPFAM; SSF52738; Methylesterase CheB, C-terminal domain; 1. DR PROSITE; PS50122; CHEB; 1. DR PROSITE; PS50110; RESPONSE_REGULATORY; 1. PE 3: Inferred from homology; KW Chemotaxis; Cytoplasm; Hydrolase; Phosphoprotein; Reference proteome. FT CHAIN 1..364 FT /note="Protein-glutamate methylesterase/protein-glutamine FT glutaminase 1" FT /id="PRO_0000264267" FT DOMAIN 6..123 FT /note="Response regulatory" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099" FT DOMAIN 165..357 FT /note="CheB-type methylesterase" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099" FT ACT_SITE 177 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099" FT ACT_SITE 203 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099" FT ACT_SITE 299 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099" FT MOD_RES 57 FT /note="4-aspartylphosphate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099" SQ SEQUENCE 364 AA; 39087 MW; A625E0BA909A1BEB CRC64; MQKKIKVLCV DDSALIRSLM TEIINSQPDM EVCATAPDPL VARELIKQHN PDVLTLDVEM PRMDGLDFLE KLMRLRPMPV VMVSSLTERG SEITLRALEL GAVDFVTKPR VGIRDGMLEY AEKLADKVRA ASRARVRQNP QPHAAAAAAA HGQTAAAAPL INNPLVSTEK LIIVGASTGG TEAIREVLTP LPPDAPAVLI AQHMPPGFTR SFAQRLNGLC RISVKEAEHG ERVLPGHAYI APGHAHLLLA RSGANYIAHL SDDPPVNRHR PSVDVLFRSA AQHAGKNALG VILTGMGRDG AAGLLEMKKA GAYTFAQDEA SCVVFGMPRE AIAMGGVDDV APLSDMSRRI MARLASMGDR VQRV //