ID CHEB1_PSEPU Reviewed; 374 AA. AC O52262; Q9L942; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 16-JUN-2009, entry version 65. DE RecName: Full=Chemotaxis response regulator protein-glutamate methylesterase of group 1 operon; DE EC=3.1.1.61; GN Name=cheB; OS Pseudomonas putida. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=303; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=PRS2000; RX MEDLINE=98164369; PubMed=9503621; RX DOI=10.1111/j.1574-6968.1998.tb12871.x; RA Ditty J.L., Grimm A.C., Harwood C.S.; RT "Identification of a chemotaxis gene region from Pseudomonas putida."; RL FEMS Microbiol. Lett. 159:267-273(1998). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=MK1; RX MEDLINE=20253319; PubMed=10792727; RX DOI=10.1046/j.1365-2958.2000.01859.x; RA Pandza S., Baetens M., Park C.H., Au T., Keyhan M., Matin A.; RT "The G-protein FlhF has a role in polar flagellar placement and RT general stress response induction in Pseudomonas putida."; RL Mol. Microbiol. 36:414-423(2000). CC -!- FUNCTION: Involved in the modulation of the chemotaxis system; CC catalyzes the demethylation of specific methylglutamate residues CC introduced into the chemoreceptors (methyl-accepting chemotaxis CC proteins) by cheR (By similarity). CC -!- CATALYTIC ACTIVITY: Protein L-glutamate O(5)-methyl ester + H(2)O CC = protein L-glutamate + methanol. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- DOMAIN: The N-terminal regulatory domain inhibits the activity of CC the C-terminal effector domain. CC -!- PTM: Phosphorylated by cheA. Phosphorylation suppresses the CC inhibitory activity of the N-terminal domain (By similarity). CC -!- SIMILARITY: Contains 1 cheB-type methylesterase domain. CC -!- SIMILARITY: Contains 1 response regulatory domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF031898; AAC08065.1; -; Genomic_DNA. DR EMBL; AF183382; AAF67048.1; -; Genomic_DNA. DR HSSP; P04042; 1CHD. DR BRENDA; 3.1.1.61; 403. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008984; F:protein-glutamate methylesterase activity; IEA:HAMAP. DR GO; GO:0000156; F:two-component response regulator activity; IEA:InterPro. DR GO; GO:0006935; P:chemotaxis; IEA:HAMAP. DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro. DR GO; GO:0007606; P:sensory perception of chemical stimulus; IEA:HAMAP. DR GO; GO:0000160; P:two-component signal transduction system (p...; IEA:HAMAP. DR HAMAP; MF_00099; -; 1. DR InterPro; IPR008248; Sig_transdc_resp-reg_CheB. DR InterPro; IPR000673; Sig_transdc_resp-reg_Me-estase. DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver. DR Gene3D; G3DSA:3.40.50.180; Chemotax_RR_pGlu_Me-esterase; 1. DR Pfam; PF01339; CheB_methylest; 1. DR Pfam; PF00072; Response_reg; 1. DR PIRSF; PIRSF000876; RR_chemtxs_CheB; 1. DR ProDom; PD005328; CheB_methylest; 1. DR ProDom; PD000039; Response_reg; 1. DR SMART; SM00448; REC; 1. DR PROSITE; PS50122; CHEB; 1. DR PROSITE; PS50110; RESPONSE_REGULATORY; 1. PE 3: Inferred from homology; KW Chemotaxis; Cytoplasm; Hydrolase; Phosphoprotein. FT CHAIN 1 374 Chemotaxis response regulator protein- FT glutamate methylesterase of group 1 FT operon. FT /FTId=PRO_0000158013. FT DOMAIN 4 121 Response regulatory. FT DOMAIN 183 374 CheB-type methylesterase. FT ACT_SITE 198 198 By similarity. FT ACT_SITE 225 225 By similarity. FT ACT_SITE 318 318 By similarity. FT MOD_RES 55 55 4-aspartylphosphate (By similarity). FT VARIANT 141 147 RPAPVAA -> LAGAGRR (in MK1). FT VARIANT 193 194 VA -> LR (in MK1). SQ SEQUENCE 374 AA; 39696 MW; 47ED6595DF7BE388 CRC64; MAVKVLVVDD SGFFRRRVSE ILSADPTIQV VGTATNGKEA IDQALALKPD VITMDYEMPM MDGITAVRHI MQRCPTPVLM FSSLTHEGAR VTLDALDAGA VDYLPKNFED ISRNPDKVKQ MLCEKVHTIS RSNRRLGSYA RPAPVAAPVP ASSPAPASSF ASPAPARPAA TARAAAPAAS HSPAPKRKPY KLVAIGTSTG GPVALQRVLT QLPANFPAPI VLIQHMPAAF TKAFAERLDK LCRINVKEAE DGDMLRPGLA LLAPGGKQMM IDGRGTVKIL PGDERLNYKP CVDITFGSAA KSYGDKVLSV VLTGMGADGR EGARLLKQGG STVWAQDEAS CVIYGMPMAI VKANLADAVY SLDDIGKHLV EACV //