ID F1Z3U2_9SPHN Unreviewed; 357 AA. AC F1Z3U2; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 11-DEC-2019, entry version 49. 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=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, ECO:0000313|Proteomes:UP000004728}; RN [1] {ECO:0000313|EMBL:EGD60734.1, ECO:0000313|Proteomes:UP000004728} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19370 {ECO:0000313|EMBL:EGD60734.1, RC ECO:0000313|Proteomes:UP000004728}; 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 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, ECO:0000256|SAAS:SAAS01100814}. 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, ECO:0000256|SAAS:SAAS01116312}; 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; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00099, ECO:0000256|SAAS:SAAS01130167}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00099, CC ECO:0000256|SAAS:SAAS00132521}. 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, ECO:0000256|SAAS:SAAS01100824}. 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: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 RefSeq; WP_008068722.1; NZ_GL876932.1. DR STRING; 983920.Y88_1815; -. DR EnsemblBacteria; EGD60734; EGD60734; Y88_1815. DR eggNOG; ENOG4105CMP; Bacteria. DR eggNOG; COG2201; LUCA. DR OrthoDB; 1655418at2; -. DR BioCyc; NNIT983920:G1GS7-1951-MONOMER; -. DR Proteomes; UP000004728; 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, ECO:0000256|SAAS:SAAS00706681}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00099, ECO:0000256|SAAS:SAAS00132526}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00099, ECO:0000256|PROSITE- KW ProRule:PRU00050, ECO:0000256|SAAS:SAAS00706700}; KW Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00099, ECO:0000256|PROSITE- KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000004728}. FT DOMAIN 6..123 FT /note="Response regulatory" FT /evidence="ECO:0000259|PROSITE:PS50110" FT DOMAIN 166..353 FT /note="CheB-type methylesterase" FT /evidence="ECO:0000259|PROSITE:PS50122" FT ACT_SITE 178 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00099, FT ECO:0000256|PROSITE-ProRule:PRU00050" FT ACT_SITE 204 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00099, FT ECO:0000256|PROSITE-ProRule:PRU00050" FT ACT_SITE 300 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00099, FT ECO:0000256|PROSITE-ProRule:PRU00050" FT MOD_RES 57 FT /note="4-aspartylphosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00099, FT ECO:0000256|PROSITE-ProRule:PRU00169" 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 //