ID A0A1G0M000_9DELT Unreviewed; 355 AA. AC A0A1G0M000; DT 15-FEB-2017, integrated into UniProtKB/TrEMBL. DT 15-FEB-2017, sequence version 1. DT 28-FEB-2018, entry version 8. DE RecName: Full=Chemotaxis response regulator protein-glutamate methylesterase {ECO:0000256|HAMAP-Rule:MF_00099}; DE EC=3.1.1.61 {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; Proteobacteria; 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., RA Brodie E.L., Williams K.H., Hubbard S.S., Banfield J.F.; RT "Thousands of microbial genomes shed light on interconnected RT biogeochemical processes in an aquifer system."; RL Nat. Commun. 7:13219-13219(2016). 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. {ECO:0000256|HAMAP-Rule:MF_00099, CC ECO:0000256|SAAS:SAAS00407323}. CC -!- CATALYTIC ACTIVITY: Protein L-glutamate O(5)-methyl ester + H(2)O CC = protein L-glutamate + methanol. {ECO:0000256|HAMAP- CC Rule:MF_00099, ECO:0000256|SAAS:SAAS00706688}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00099, CC ECO:0000256|SAAS:SAAS00407336}. CC -!- DOMAIN: The N-terminal regulatory domain inhibits the activity of CC the C-terminal effector domain. {ECO:0000256|HAMAP-Rule:MF_00099}. CC -!- PTM: Phosphorylated by CheA. Phosphorylation suppresses the CC inhibitory activity of the N-terminal domain. {ECO:0000256|HAMAP- CC Rule:MF_00099}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 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:0006935; P:chemotaxis; IEA:UniProtKB-UniRule. DR CDD; cd16432; CheB_Rec; 1. DR CDD; cd00156; REC; 1. DR Gene3D; 3.40.50.180; -; 1. DR HAMAP; MF_00099; CheB_methylest; 1. DR InterPro; IPR035909; CheB_C. DR InterPro; IPR011006; CheY-like_superfamily. 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 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; SSF52172; 1. DR SUPFAM; SSF52738; SSF52738; 1. DR PROSITE; PS50122; CHEB; 1. DR PROSITE; PS50110; RESPONSE_REGULATORY; 1. PE 3: Inferred from homology; KW Chemotaxis {ECO:0000256|HAMAP-Rule:MF_00099, KW ECO:0000256|SAAS:SAAS00706681}; KW Complete proteome {ECO:0000313|Proteomes:UP000176728}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00099, KW ECO:0000256|SAAS:SAAS00485815}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00099, KW ECO:0000256|SAAS:SAAS00706700}; KW Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00099}; KW Reference proteome {ECO:0000313|Proteomes:UP000176728}. FT DOMAIN 6 123 Response regulatory. FT {ECO:0000259|PROSITE:PS50110}. FT DOMAIN 165 355 CheB-type methylesterase. FT {ECO:0000259|PROSITE:PS50122}. FT ACT_SITE 177 177 {ECO:0000256|HAMAP-Rule:MF_00099}. FT ACT_SITE 203 203 {ECO:0000256|HAMAP-Rule:MF_00099}. FT ACT_SITE 299 299 {ECO:0000256|HAMAP-Rule:MF_00099}. FT MOD_RES 57 57 4-aspartylphosphate. 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 //