ID F1Z3U2_9SPHN Unreviewed; 357 AA. AC F1Z3U2; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 01-OCT-2014, entry version 20. 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=Y88_1815 {ECO:0000313|EMBL:EGD60734.1}; OS Novosphingobium nitrogenifigens DSM 19370. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Novosphingobium. OX NCBI_TaxID=983920 {ECO:0000313|EMBL:EGD60734.1}; RN [1] {ECO:0000313|EMBL:EGD60734.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 19370 {ECO:0000313|EMBL:EGD60734.1}; RX PubMed=22156397; DOI=10.1128/JB.06381-11; RA Strabala T.J., Macdonald L., Liu V., Smit A.M.; RT "Draft Genome Sequence of Novosphingobium nitrogenifigens Y88T."; RL J. Bacteriol. 194:201-201(2012). 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:SAAS00070596}. 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:SAAS00070602}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00099, CC ECO:0000256|SAAS:SAAS00070604}. 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 -!- SIMILARITY: Contains 1 cheB-type methylesterase domain. CC {ECO:0000256|HAMAP-Rule:MF_00099}. CC -!- SIMILARITY: Contains 1 response regulatory domain. CC {ECO:0000256|HAMAP-Rule:MF_00099}. CC -!- SIMILARITY: Contains cheB-type methylesterase domain. CC {ECO:0000256|SAAS:SAAS00070607}. CC -!- SIMILARITY: Contains response regulatory domain. CC {ECO:0000256|SAAS:SAAS00070603}. 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:EGD60734.1}. 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; AEWJ01000013; EGD60734.1; -; Genomic_DNA. DR EnsemblBacteria; EGD60734; EGD60734; Y88_1815. DR PATRIC; 46737210; VBINovNit182528_1955. 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-HAMAP. DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.180; -; 1. DR HAMAP; MF_00099; CheB_methylest; 1. 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:SAAS00070605}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00099, KW ECO:0000256|SAAS:SAAS00070584}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00099, KW ECO:0000256|SAAS:SAAS00070587}; KW Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00099, KW ECO:0000256|SAAS:SAAS00070606}. FT ACT_SITE 178 178 {ECO:0000256|HAMAP-Rule:MF_00099}. FT ACT_SITE 204 204 {ECO:0000256|HAMAP-Rule:MF_00099}. FT ACT_SITE 300 300 {ECO:0000256|HAMAP-Rule:MF_00099}. FT MOD_RES 57 57 4-aspartylphosphate. {ECO:0000256|HAMAP- FT Rule:MF_00099}. SQ SEQUENCE 357 AA; 38068 MW; 9826F5D8DD960038 CRC64; MGRKIRVLVV DDSASVRQTM TAILSADPEI EVIAAASDPF AAARYIKDEL PDVVTLDVEM PRMDGITFLR KLMSQCPVPV VMCSSLTEEG SETLLQALEA GAVDVILKPR AGVADFLAEQ NQRIRDVVKG AAHAKVSRRA DRAPLRPEGK LTADAMLPPP IARAMSRTTE MVVCIGASTG GTEALREVLE ALPANAPGIV VVQHMPEQFT RSFAARLNAR CEVDVKEAED GDTVMRGHVL IAPGGRHTLL ARQGARYVVS VREGPLVSRH RPSVNVLFRS AAQWAGANAV GVIMTGMGDD GAQGLLEMRQ AGARTIAQNE ATSVVFGMPR EAIALGAAER IVPLGAIARE MIQAGMR //