ID F1Z3U2_9SPHN Unreviewed; 357 AA. AC F1Z3U2; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 05-DEC-2018, entry version 45. 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 CC various stimuli. Catalyzes the demethylation of specific CC methylglutamate residues introduced into the chemoreceptors CC (methyl-accepting chemotaxis proteins or MCP) by CheR. Also CC mediates the irreversible deamidation of specific glutamine CC residues to glutamic acid. {ECO:0000256|HAMAP-Rule:MF_00099, CC ECO:0000256|SAAS:SAAS01100814}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + CC NH4(+); Xref=Rhea:RHEA:16441, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:28938, ChEBI:CHEBI:29973, ChEBI:CHEBI:30011, CC Rhea:RHEA-COMP:10207, Rhea:RHEA-COMP:10208; EC=3.5.1.44; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00099, CC ECO:0000256|SAAS:SAAS01100816}; CC -!- CATALYTIC ACTIVITY: CC Reaction=[protein]-L-glutamate O(5)-methyl ester + H2O = H(+) + L- CC glutamyl-[protein] + methanol; Xref=Rhea:RHEA:23236, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17790, CC ChEBI:CHEBI:29973, ChEBI:CHEBI:82795, Rhea:RHEA-COMP:10208, CC Rhea:RHEA-COMP:10311; EC=3.1.1.61; Evidence={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: 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 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 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; POG091H045J; -. 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: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, ECO:0000256|PROSITE- KW ProRule:PRU00050, ECO:0000256|SAAS:SAAS00706681}; KW Complete proteome {ECO:0000313|Proteomes:UP000004728}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00099, KW ECO:0000256|SAAS:SAAS00485815}; 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}; KW Reference proteome {ECO:0000313|Proteomes:UP000004728}. FT DOMAIN 6 123 Response regulatory. FT {ECO:0000259|PROSITE:PS50110}. FT DOMAIN 166 353 CheB-type methylesterase. FT {ECO:0000259|PROSITE:PS50122}. FT ACT_SITE 178 178 {ECO:0000256|HAMAP-Rule:MF_00099, FT ECO:0000256|PROSITE-ProRule:PRU00050}. FT ACT_SITE 204 204 {ECO:0000256|HAMAP-Rule:MF_00099, FT ECO:0000256|PROSITE-ProRule:PRU00050}. FT ACT_SITE 300 300 {ECO:0000256|HAMAP-Rule:MF_00099, FT ECO:0000256|PROSITE-ProRule:PRU00050}. FT MOD_RES 57 57 4-aspartylphosphate. {ECO:0000256|HAMAP- FT Rule:MF_00099, ECO:0000256|PROSITE- FT 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 //