CHEB2_CUPPJ
ID CHEB2_CUPPJ Reviewed; 356 AA.
AC Q46PH7;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Protein-glutamate methylesterase/protein-glutamine glutaminase 2 {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=cheB2 {ECO:0000255|HAMAP-Rule:MF_00099}; OrderedLocusNames=Reut_B5612;
OS Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS (strain JMP 134)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=264198;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMP134 / LMG 1197;
RX PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA Kyrpides N.C.;
RT "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT versatile pollutant degrader.";
RL PLoS ONE 5:E9729-E9729(2010).
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; CP000091; AAZ64957.1; -; Genomic_DNA.
DR RefSeq; WP_011301720.1; NC_007348.1.
DR AlphaFoldDB; Q46PH7; -.
DR SMR; Q46PH7; -.
DR STRING; 264198.Reut_B5612; -.
DR EnsemblBacteria; AAZ64957; AAZ64957; Reut_B5612.
DR KEGG; reu:Reut_B5612; -.
DR eggNOG; COG2201; Bacteria.
DR HOGENOM; CLU_000445_51_0_4; -.
DR OMA; MLEMHRA; -.
DR OrthoDB; 1655418at2; -.
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..356
FT /note="Protein-glutamate methylesterase/protein-glutamine
FT glutaminase 2"
FT /id="PRO_0000225480"
FT DOMAIN 7..124
FT /note="Response regulatory"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT DOMAIN 157..349
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT ACT_SITE 169
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT ACT_SITE 195
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT ACT_SITE 291
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT MOD_RES 58
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
SQ SEQUENCE 356 AA; 38528 MW; C1161602E3DEE9DF CRC64;
MTAAKIKVLC VDDSALIRSL MTEIINSQPD MEVVGTAPDP LVAREMIKQL NPDVLTLDVE
MPRMDGLDFL ERLMRLRPMP VLMVSSLTER GSEITMRALE LGAVDFVTKP KLGIRDGLME
YTDTIADKIR AASRARVRQA PQAASGTPAT PMLRSPLLST EKLIILGAST GGTEAIKDFL
MPLPPDSPAV LIVQHMPAGF TRSFAQRLDG LCRITVKEAE HGERVLPGYA YIAPGDSHLR
LARSGANYVA HLSQEAPVNR HRPSVDVLFD SAAEHGGKNV IGVILTGMGK DGAKGMLRMR
EAGAYNLAQD ESTCIVFGMP KEAIAAGGVH EVVPLHSMTQ RVMARLATYG TRAQRV
