ID CHEB1_RHIJ3 Reviewed; 347 AA. AC Q1MLG8; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2006, sequence version 1. DT 28-JAN-2026, entry version 108. 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=RL0691; OS Rhizobium johnstonii (strain DSM 114642 / LMG 32736 / 3841) (Rhizobium OS leguminosarum bv. viciae). OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium; OC Rhizobium johnstonii. OX NCBI_TaxID=216596; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 114642 / LMG 32736 / 3841; RX PubMed=16640791; DOI=10.1186/gb-2006-7-4-r34; RA Young J.P.W., Crossman L.C., Johnston A.W.B., Thomson N.R., Ghazoui Z.F., RA Hull K.H., Wexler M., Curson A.R.J., Todd J.D., Poole P.S., Mauchline T.H., RA East A.K., Quail M.A., Churcher C., Arrowsmith C., Cherevach I., RA Chillingworth T., Clarke K., Cronin A., Davis P., Fraser A., Hance Z., RA Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H., RA Rabbinowitsch E., Sanders M., Simmonds M., Whitehead S., Parkhill J.; RT "The genome of Rhizobium leguminosarum has recognizable core and accessory RT components."; RL Genome Biol. 7:R34.1-R34.20(2006). 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; AM236080; CAK06185.1; -; Genomic_DNA. DR RefSeq; WP_011650462.1; NC_008380.1. DR AlphaFoldDB; Q1MLG8; -. DR SMR; Q1MLG8; -. DR EnsemblBacteria; CAK06185; CAK06185; RL0691. DR GeneID; 303205706; -. DR KEGG; rle:RL0691; -. DR eggNOG; COG2201; Bacteria. DR HOGENOM; CLU_000445_51_0_5; -. DR Proteomes; UP000006575; Chromosome. 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 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..347 FT /note="Protein-glutamate methylesterase/protein-glutamine FT glutaminase 1" FT /id="PRO_0000264302" FT DOMAIN 6..123 FT /note="Response regulatory" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099" FT DOMAIN 150..342 FT /note="CheB-type methylesterase" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099" FT ACT_SITE 162 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099" FT ACT_SITE 188 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099" FT ACT_SITE 284 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 347 AA; 36689 MW; 9D99731BDBB60E3E CRC64; MSAPARVLVV DDSATMRGLI TAVLSSDPEV NVIGQAGDAL EAREAIKRLN PDVLTLDIEM PNMNGLDFLE KIMTLRPMPV IMVSTMTHRG AEATLAALEI GAFDCVGKPA PGELRPFGDL AEKVKAAART QRQYSQPVVA VAPPPSVADF RVGRKIVAIG SSTGGVEALI AVLQKFPANC PPTVITQHMP PTFTKSFAER LNRLCAPVVQ EATDGARLEI GKIYLAPGGE RHLQVSGASA PCCRLIDRAP VNGHRPSVDV LFDSVAELAG RNAVGVILTG MGRDGAAGLL KMRHAGARTL GQNEKTCVVY GMPRVAHELG AVEQQLPLSA IGEEILKMTA ARKEGTE //