ID A0A1G0M000_9DELT Unreviewed; 355 AA. AC A0A1G0M000; DT 15-FEB-2017, integrated into UniProtKB/TrEMBL. DT 15-FEB-2017, sequence version 1. DT 03-MAY-2023, entry version 26. DE RecName: Full=Protein-glutamate methylesterase/protein-glutamine glutaminase {ECO:0000256|HAMAP-Rule:MF_00099}; DE EC=3.1.1.61 {ECO:0000256|HAMAP-Rule:MF_00099}; DE EC=3.5.1.44 {ECO:0000256|HAMAP-Rule:MF_00099}; GN Name=cheB {ECO:0000256|HAMAP-Rule:MF_00099}; GN ORFNames=A2075_10405 {ECO:0000313|EMBL:OGU04560.1}; OS Geobacteraceae bacterium GWC2_58_44. OC Bacteria; Pseudomonadota; Deltaproteobacteria; Desulfuromonadales; OC Geobacteraceae. OX NCBI_TaxID=1798318 {ECO:0000313|EMBL:OGU04560.1, ECO:0000313|Proteomes:UP000176728}; RN [1] {ECO:0000313|EMBL:OGU04560.1, ECO:0000313|Proteomes:UP000176728} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=27774985; DOI=10.1038/ncomms13219; RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J., RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L., RA Williams K.H., Hubbard S.S., Banfield J.F.; RT "Thousands of microbial genomes shed light on interconnected biogeochemical RT processes in an aquifer system."; RL Nat. Commun. 7:13219-13219(2016). 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:0000256|HAMAP-Rule:MF_00099}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + L-glutaminyl-[protein] = 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:0000256|HAMAP- CC Rule:MF_00099}; CC -!- CATALYTIC ACTIVITY: CC Reaction=[protein]-L-glutamate 5-O-methyl ester + H2O = H(+) + L- CC glutamyl-[protein] + methanol; 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; CC Evidence={ECO:0000256|ARBA:ARBA00000941, ECO:0000256|HAMAP- CC Rule:MF_00099}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00099}. CC -!- DOMAIN: Contains a C-terminal catalytic domain, and an N-terminal CC region which modulates catalytic activity. {ECO:0000256|HAMAP- CC Rule:MF_00099}. CC -!- PTM: Phosphorylated by CheA. Phosphorylation of the N-terminal CC regulatory domain activates the methylesterase activity. CC {ECO:0000256|HAMAP-Rule:MF_00099}. CC -!- SIMILARITY: Belongs to the CheB family. {ECO:0000256|HAMAP- CC Rule:MF_00099}. 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:OGU04560.1}. 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; MGZL01000147; OGU04560.1; -; Genomic_DNA. DR AlphaFoldDB; A0A1G0M000; -. DR STRING; 1798318.A2075_10405; -. DR EnsemblBacteria; OGU04560; OGU04560; A2075_10405. DR Proteomes; UP000176728; Unassembled WGS sequence. 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 GO; GO:0018277; P:protein deamination; IEA:UniProtKB-UniRule. DR GO; GO:0006482; P:protein demethylation; 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 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 {ECO:0000256|ARBA:ARBA00022500, ECO:0000256|HAMAP- KW Rule:MF_00099}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00099}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00099}; KW Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00099, ECO:0000256|PROSITE- KW ProRule:PRU00169}. FT DOMAIN 6..123 FT /note="Response regulatory" FT /evidence="ECO:0000259|PROSITE:PS50110" FT DOMAIN 165..355 FT /note="CheB-type methylesterase" FT /evidence="ECO:0000259|PROSITE:PS50122" FT ACT_SITE 177 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00099, FT ECO:0000256|PROSITE-ProRule:PRU00050" FT ACT_SITE 203 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00099, FT ECO:0000256|PROSITE-ProRule:PRU00050" FT ACT_SITE 299 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00099, FT ECO:0000256|PROSITE-ProRule:PRU00050" FT MOD_RES 57 FT /note="4-aspartylphosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00099, FT ECO:0000256|PROSITE-ProRule:PRU00169" SQ SEQUENCE 355 AA; 38635 MW; 2F80D36B7A8D2081 CRC64; MTKKIKVLIV DDSAVVRQTM AEILSSDPQI EVMSTASDPF IAAERIRHEV PDVITLDVEM PRMDGITFLH KIMSQHPIPV VMCSSLTEKG SETALKALEY GAVEIIQKPR LGTKTFLEES RLRICDAVKA ASQARVRRVS AVSHTVSPKL TADVIMEKPK DRAMIQTTEK VVVIGASTGG TEALRIFLES LPADCPGIVI VQHMPEGFTR AFSQRLDGLC RITVKEAENN DTVVRGRALI AAGNHHLLLK RSGARYYVEI KDGPLVSRHR PSVDVLFRSA ARYAGKNAVG VIMTGMGDDG ARGMLEMKQA GAVNIAQDEA SCIVFGMPNE AIKLGGVNII RPLDGICREV LRLCA //