ID CHEB1_HAHCH Reviewed; 361 AA. AC Q2SPQ1; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2006, sequence version 1. DT 18-JUN-2025, entry version 112. 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=HCH_00463; OS Hahella chejuensis (strain KCTC 2396). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Oceanospirillales; Hahellaceae; Hahella. OX NCBI_TaxID=349521; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KCTC 2396; RX PubMed=16352867; DOI=10.1093/nar/gki1016; RA Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G., RA Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K., RA Oh T.K., Kim J.F.; RT "Genomic blueprint of Hahella chejuensis, a marine microbe producing an RT algicidal agent."; RL Nucleic Acids Res. 33:7066-7073(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; CP000155; ABC27373.1; -; Genomic_DNA. DR RefSeq; WP_011394450.1; NC_007645.1. DR AlphaFoldDB; Q2SPQ1; -. DR SMR; Q2SPQ1; -. DR STRING; 349521.HCH_00463; -. DR KEGG; hch:HCH_00463; -. DR eggNOG; COG2201; Bacteria. DR HOGENOM; CLU_000445_51_0_6; -. DR OrthoDB; 9793421at2; -. DR Proteomes; UP000000238; 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..361 FT /note="Protein-glutamate methylesterase/protein-glutamine FT glutaminase 1" FT /id="PRO_0000264281" FT DOMAIN 10..127 FT /note="Response regulatory" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099" FT DOMAIN 167..359 FT /note="CheB-type methylesterase" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099" FT ACT_SITE 179 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099" FT ACT_SITE 205 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099" FT ACT_SITE 301 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099" FT MOD_RES 61 FT /note="4-aspartylphosphate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099" SQ SEQUENCE 361 AA; 39023 MW; 254F5C128A8D3941 CRC64; MSSGAGKVYK VLVVDDSALM RKILVEILNQ SPCLEVVDTA GDPYQARDKI KALSPDVITL DVEMPRMDGL TFLRNLMRLR PMPVVMISSL TEQGAAVTLD ALEYGAVDFI AKPKIDLREG IEEKAQEIID KVITAARIPH DKLLLKQQRL QTQHQKAAVG ERPQPVFATT DKLIAVGAST GGLDAIRDLL DGLNMDLPGI VIAQHIPGAF SRSFAERLDR RLPMKVEEAY DNAPITMGRV YIAPGEYHLE VVRTGAKYVC RLSEAPPVNR HRPSVDVLFD SIVSAAGANA MAALLTGMGK DGAAGLLRLH EAGAYTIAQD EASSVVWGMP GAAVKLNAAD DVLPLEKIAA SVKRWYAENP G //