ID A0A0C1YB14_9CYAN Unreviewed; 362 AA. AC A0A0C1YB14; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 24-JUN-2015, entry version 4. 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, ECO:0000256|SAAS:SAAS00070601}; GN Name=cheB {ECO:0000256|HAMAP-Rule:MF_00099}; GN ORFNames=QQ91_12395 {ECO:0000313|EMBL:KIF42405.1}; OS Lyngbya confervoides BDU141951. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales; OC Lyngbya. OX NCBI_TaxID=1574623 {ECO:0000313|EMBL:KIF42405.1}; RN [1] {ECO:0000313|EMBL:KIF42405.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BDU141951 {ECO:0000313|EMBL:KIF42405.1}; RA Malar M.C., Sen D., Tripathy S.; RT "Draft genome sequence of Lyngbya confervoides BDU141951."; RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases. 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:SAAS00132519}. 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:SAAS00132521}. 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:SAAS00132518}. CC -!- SIMILARITY: Contains response regulatory domain. CC {ECO:0000256|SAAS:SAAS00132517}. 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:KIF42405.1}. 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; JTHE01000261; KIF42405.1; -; Genomic_DNA. 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:SAAS00132526}; 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:SAAS00132523}. FT DOMAIN 167 357 CheB-type methylesterase. FT {ECO:0000256|HAMAP-Rule:MF_00099}. FT ACT_SITE 179 179 {ECO:0000256|HAMAP-Rule:MF_00099}. FT ACT_SITE 206 206 {ECO:0000256|HAMAP-Rule:MF_00099}. FT ACT_SITE 299 299 {ECO:0000256|HAMAP-Rule:MF_00099}. FT MOD_RES 58 58 4-aspartylphosphate. {ECO:0000256|HAMAP- FT Rule:MF_00099}. SQ SEQUENCE 362 AA; 39112 MW; 8DEB1F83099C4758 CRC64; MASRPIRLLL VEDSPVALAI LQRLLRDHPA IEIVGIAANG VEALQLIPQV DPQIICTDLH MPKMDGLTLT REVMARFPRP ILVVSASVQD EDTQNVFRLL EAGALDIFPK PRTGLAAEYE KVQQELINKI RVLSGVSVFT QHRREVRPTP LPPPPPASAI AASHQLDIRA PRVLAIGAST GGPQALQTIL QALPKQFPVP ILCVQHISSG FLQGLIDWLN LKSALHIKIA VAGEMPAPGT VYFPPERHHM QIDRYGRFEL TQSPPVAGHC PSVTVLLESV AAYYRRSAVG IVLTGMGRDG AEGLHAIALA GGTTIAQDEA TCVVFGMPKE AIALNAAQHI LPIDNIAPFL LNRVFASALQ NF //