ID CHEB1_VIBVU Reviewed; 376 AA. AC Q8DB67; DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 10-JUN-2026, entry version 129. 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=VV1_1956; OS Vibrio vulnificus (strain CMCP6). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=216895; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CMCP6; RA Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.; RT "Complete genome sequence of Vibrio vulnificus CMCP6."; RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases. 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; AE016795; AAO10356.1; -; Genomic_DNA. DR RefSeq; WP_011079855.1; NC_004459.3. DR AlphaFoldDB; Q8DB67; -. DR SMR; Q8DB67; -. DR KEGG; vvu:VV1_1956; -. DR HOGENOM; CLU_000445_51_0_6; -. DR Proteomes; UP000002275; 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; 3.40.50.2300:FF:000077; Chemotaxis response regulator; 1. DR FunFam; 3.40.50.180:FF:000001; 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 PANTHER; PTHR42872; PROTEIN-GLUTAMATE METHYLESTERASE/PROTEIN-GLUTAMINE GLUTAMINASE; 1. DR PANTHER; PTHR42872:SF3; PROTEIN-GLUTAMATE METHYLESTERASE_PROTEIN-GLUTAMINE GLUTAMINASE 1; 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..376 FT /note="Protein-glutamate methylesterase/protein-glutamine FT glutaminase 1" FT /id="PRO_0000158039" FT DOMAIN 4..121 FT /note="Response regulatory" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099" FT DOMAIN 183..376 FT /note="CheB-type methylesterase" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099" FT REGION 138..174 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 141..158 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 195 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099" FT ACT_SITE 222 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099" FT ACT_SITE 318 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099" FT MOD_RES 55 FT /note="4-aspartylphosphate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099" SQ SEQUENCE 376 AA; 40498 MW; 56EA7200D76EFD7C CRC64; MAIKVLVVDD SSFFRRRVSE IINAESRLEV IDVAVNGKEA VEKAKRLKPD VITMDIEMPV MDGISAVREI MASVPTPILM FSSLTHDGAK ATLDALDAGA LDFLPKKFED IARNRDEAVS LLQQRVIQIA SKRAFMRRPV ASSTPVQERP QSTLNRPTTG LRREAPAQAP VSRAPVAAKF RASGKKYQLT AIGTSTGGPV ALQKILTKLP ANYPHPIVLI QHMPATFTAA FASRLNSLCK IQVKEAEDGD VLQAGVAYLA PGGKQMMIDG RPGAARLRII DGGERMNYKP CVDVTFGSAA KIYADKVLSM VLTGMGADGR EGARMLKSAG ATIWAQDEDS CVVYGMPQAV AKAGLSTEDL PLERIAERML VEVGLA //