ID   CHEB1_XANOM             Reviewed;         351 AA.
AC   Q2P5Q6;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Protein-glutamate methylesterase/protein-glutamine glutaminase 1 {ECO:0000255|HAMAP-Rule:MF_00099};
DE            EC=3.1.1.61 {ECO:0000255|HAMAP-Rule:MF_00099};
DE            EC=3.5.1.44 {ECO:0000255|HAMAP-Rule:MF_00099};
GN   Name=cheB1 {ECO:0000255|HAMAP-Rule:MF_00099}; OrderedLocusNames=XOO1366;
OS   Xanthomonas oryzae pv. oryzae (strain MAFF 311018).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=342109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAFF 311018;
RA   Ochiai H., Inoue Y., Takeya M., Sasaki A., Kaku H.;
RT   "Genome sequence of Xanthomonas oryzae pv. oryzae suggests contribution of
RT   large numbers of effector genes and insertion sequences to its race
RT   diversity.";
RL   Jpn. Agric. Res. Q. 39:275-287(2005).
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:0000255|HAMAP-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; Evidence={ECO:0000255|HAMAP-
CC         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:0000255|HAMAP-
CC         Rule:MF_00099};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00099}.
CC   -!- DOMAIN: Contains a C-terminal catalytic domain, and an N-terminal
CC       region which modulates catalytic activity. {ECO:0000255|HAMAP-
CC       Rule:MF_00099}.
CC   -!- PTM: Phosphorylated by CheA. Phosphorylation of the N-terminal
CC       regulatory domain activates the methylesterase activity.
CC       {ECO:0000255|HAMAP-Rule:MF_00099}.
CC   -!- SIMILARITY: Belongs to the CheB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00099}.
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DR   EMBL; AP008229; BAE68121.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2P5Q6; -.
DR   SMR; Q2P5Q6; -.
DR   KEGG; xom:XOO1366; -.
DR   HOGENOM; CLU_000445_51_0_6; -.
DR   OMA; HAMAQTT; -.
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   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; Cytoplasm; Hydrolase; Phosphoprotein.
FT   CHAIN           1..351
FT                   /note="Protein-glutamate methylesterase/protein-glutamine
FT                   glutaminase 1"
FT                   /id="PRO_0000264333"
FT   DOMAIN          1..115
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT   DOMAIN          161..351
FT                   /note="CheB-type methylesterase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT   ACT_SITE        173
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT   ACT_SITE        199
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT   ACT_SITE        295
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT   MOD_RES         49
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
SQ   SEQUENCE   351 AA;  37242 MW;  980FA18F3C3AEF56 CRC64;
     MVDDSAVVRQ VLVNVLNDAA DIEVIATAAD PLLAIEKMRK QWPDVIVLDV EMPRMDGITF
     LRKIMSERPT PVVICSTLTE KGARVTMDAL AAGAVAVVTK PRLGLKQFLT ESADELVATV
     RSAARANVKR LAARVTAAPL EAEVKHTADV ILPAQSGRAM AQTTERIVAI GTSTGGTQAL
     EEVLTALPRV CPGIVIVQHM PEKFTAAFAA RLNGLCQIAV KEAANNDRVM PGRALIAPGG
     KHLLLRRSGA QYFVEVLEGP PVNRHRPSVD VLFRSAARAA GSNALGIIMT GMGDDGAAGL
     LEMRQAGART VAQDEQTSIV FGMPKEAIKR GGADRILALG AMAREIVTQL Q