ID A0A0C1YB14_9CYAN Unreviewed; 362 AA. AC A0A0C1YB14; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 07-OCT-2020, entry version 31. DE RecName: Full=Protein-glutamate methylesterase/protein-glutamine glutaminase {ECO:0000256|HAMAP-Rule:MF_00099}; DE EC=3.1.1.61 {ECO:0000256|HAMAP-Rule:MF_00099}; DE EC=3.5.1.44 {ECO:0000256|HAMAP-Rule:MF_00099}; 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 Oscillatoriaceae; Lyngbya. OX NCBI_TaxID=1574623 {ECO:0000313|EMBL:KIF42405.1, ECO:0000313|Proteomes:UP000031561}; RN [1] {ECO:0000313|EMBL:KIF42405.1, ECO:0000313|Proteomes:UP000031561} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BDU141951 {ECO:0000313|EMBL:KIF42405.1, RC ECO:0000313|Proteomes:UP000031561}; 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 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:0000256|HAMAP-Rule:MF_00099}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + L-glutaminyl-[protein] = 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:0000256|HAMAP- CC Rule:MF_00099}; CC -!- CATALYTIC ACTIVITY: CC Reaction=[protein]-L-glutamate 5-O-methyl ester + H2O = H(+) + L- CC glutamyl-[protein] + methanol; 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; CC Evidence={ECO:0000256|ARBA:ARBA00000941, ECO:0000256|HAMAP- CC Rule:MF_00099}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00099}. CC -!- DOMAIN: Contains a C-terminal catalytic domain, and an N-terminal CC region which modulates catalytic activity. {ECO:0000256|HAMAP- CC Rule:MF_00099}. CC -!- PTM: Phosphorylated by CheA. Phosphorylation of the N-terminal CC regulatory domain activates the methylesterase activity. CC {ECO:0000256|HAMAP-Rule:MF_00099}. CC -!- SIMILARITY: Belongs to the CheB family. {ECO:0000256|HAMAP- CC Rule:MF_00099}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {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 RefSeq; WP_039724775.1; NZ_JTHE02000002.1. DR EnsemblBacteria; KIF42405; KIF42405; QQ91_12395. DR OrthoDB; 1655418at2; -. DR Proteomes; UP000031561; 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:0050568; F:protein-glutamine glutaminase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-UniRule. DR GO; GO:0018277; P:protein deamination; IEA:UniProtKB-UniRule. DR GO; GO:0006482; P:protein demethylation; 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_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 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, ECO:0000256|PROSITE- KW ProRule:PRU00050}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00099}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00099, KW ECO:0000256|PROSITE-ProRule:PRU00050}; KW Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00099, ECO:0000256|PROSITE- KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000031561}. FT DOMAIN 7..125 FT /note="Response regulatory" FT /evidence="ECO:0000259|PROSITE:PS50110" FT DOMAIN 167..357 FT /note="CheB-type methylesterase" FT /evidence="ECO:0000259|PROSITE:PS50122" FT ACT_SITE 179 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00099, FT ECO:0000256|PROSITE-ProRule:PRU00050" FT ACT_SITE 206 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00099, FT ECO:0000256|PROSITE-ProRule:PRU00050" FT ACT_SITE 299 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00099, FT ECO:0000256|PROSITE-ProRule:PRU00050" FT MOD_RES 58 FT /note="4-aspartylphosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00099, FT ECO:0000256|PROSITE-ProRule:PRU00169" 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 //