CHEB2_AZOBR
ID CHEB2_AZOBR Reviewed; 394 AA.
AC Q8VL08;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Protein-glutamate methylesterase/protein-glutamine glutaminase {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=cheB {ECO:0000255|HAMAP-Rule:MF_00099};
OS Azospirillum brasilense.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=192;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29145 / DSM 1690 / IMET 11303 / Sp7;
RX PubMed=11934495; DOI=10.1111/j.1574-6968.2002.tb11061.x;
RA Hauwaerts D., Alexandre G., Das S.K., Vanderleyden J., Zhulin I.B.;
RT "A major chemotaxis gene cluster in Azospirillum brasilense and
RT relationships between chemotaxis operons in alpha-proteobacteria.";
RL FEMS Microbiol. Lett. 208:61-67(2002).
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; AF450326; AAL47024.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8VL08; -.
DR SMR; Q8VL08; -.
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..394
FT /note="Protein-glutamate methylesterase/protein-glutamine
FT glutaminase"
FT /id="PRO_0000157974"
FT DOMAIN 27..145
FT /note="Response regulatory"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT DOMAIN 191..393
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 211
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT ACT_SITE 238
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT ACT_SITE 335
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT MOD_RES 78
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
SQ SEQUENCE 394 AA; 40986 MW; 55FBCF8D432A02BD CRC64;
MSDGFGRPPP PAPAGHPTGA AGGDPVRVMV VDDSAVIRGL LTRALEGDTE IRVVASVGDG
QMAVNALQRN SLDVIVLDIE MPVMDGLTAI PKLLAVAPQV KIIMASTLTL RGADISMRCL
SAGAADYIPK PTSTREIGGA DAFKRELVSK VKALGAAARR AGSRTRGELR PLNPVPAAFL
KREPPPVTLR PAPAVGSVGQ VKPDVIAIGS STGGPQALFE VLAHLKTGVT QPILITQHMP
ATFTTILAEH ITRQCGMNAQ EAKDGEPVVP GRCYIAPGDF HMLVTQRAGA NVISLTKDPP
ENFCRPAVDP MMRSILRAFG GRKVLACILT GMGQDGLKGC TEVVNAGGTL IAQDEASSVV
WGMPGAVAQA GICSAVLPLK EIGPYIRKFA SRAA
