ID CHEB1_METHJ Reviewed; 342 AA. AC Q2FMT2; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 21-MAR-2006, sequence version 1. DT 18-JUN-2025, entry version 100. 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=Mhun_0109; OS Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / OS JF-1). OC Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group; OC Methanomicrobia; Methanomicrobiales; Methanospirillaceae; Methanospirillum. OX NCBI_TaxID=323259; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27890 / DSM 864 / NBRC 100397 / JF-1; RX PubMed=26744606; DOI=10.1186/s40793-015-0124-8; RA Gunsalus R.P., Cook L.E., Crable B., Rohlin L., McDonald E., Mouttaki H., RA Sieber J.R., Poweleit N., Zhou H., Lapidus A.L., Daligault H.E., Land M., RA Gilna P., Ivanova N., Kyrpides N., Culley D.E., McInerney M.J.; RT "Complete genome sequence of Methanospirillum hungatei type strain JF1."; RL Stand. Genomic Sci. 11:2-2(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: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; CP000254; ABD39887.1; -; Genomic_DNA. DR RefSeq; WP_011447183.1; NC_007796.1. DR AlphaFoldDB; Q2FMT2; -. DR SMR; Q2FMT2; -. DR STRING; 323259.Mhun_0109; -. DR EnsemblBacteria; ABD39887; ABD39887; Mhun_0109. DR GeneID; 3923804; -. DR KEGG; mhu:Mhun_0109; -. DR eggNOG; arCOG02382; Archaea. DR HOGENOM; CLU_000445_51_0_2; -. DR InParanoid; Q2FMT2; -. DR OrthoDB; 2857at2157; -. DR Proteomes; UP000001941; 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 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..342 FT /note="Protein-glutamate methylesterase/protein-glutamine FT glutaminase 1" FT /id="PRO_0000264338" FT DOMAIN 3..121 FT /note="Response regulatory" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099" FT DOMAIN 141..340 FT /note="CheB-type methylesterase" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099" FT ACT_SITE 153 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099" FT ACT_SITE 180 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099" FT ACT_SITE 282 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099" FT MOD_RES 54 FT /note="4-aspartylphosphate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099" SQ SEQUENCE 342 AA; 36666 MW; 791684F85B83EEB0 CRC64; MIRVLVIDDS LFIRTVVQDM LSDDPDIQIV GVASDGLEAL DKIRELKPDL ITLDIEMPRL DGLSMLERKK EIDRFPKTLV LSSLTSEGAE MTKRAIALGA DDFMLKPRGI KNIREIGGEL KHKIKNICTI AYITAKPVLK DSNARNVVLI GSSAGGPPML DTIVSKLPSD LNAAVIITQH MPKGGFTAAL AARLNRISPL QIRETENGDV LKNGTVLVSR AGFHTIISSV LDKGGSQSGK IILTDSPPVH NVKPAVDKTF ISAAQVFGNH CVTAILSGMG NDGGEGTEAI KKAGGVTIVC REEDCLVYGM ARSALSRNCV DHVLSLQAIP EKIVETIRAM NG //