ID A0A402CU46_9BACT Unreviewed; 387 AA.
AC A0A402CU46;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
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 Synonyms=cheB2 {ECO:0000313|EMBL:BDI28873.1};
GN ORFNames=CCAX7_009240 {ECO:0000313|EMBL:BDI28873.1}, CCAX7_20110
GN {ECO:0000313|EMBL:GCE53497.1};
OS Capsulimonas corticalis.
OC Bacteria; Armatimonadota; Armatimonadia; Capsulimonadales;
OC Capsulimonadaceae; Capsulimonas.
OX NCBI_TaxID=2219043 {ECO:0000313|EMBL:GCE53497.1};
RN [1] {ECO:0000313|EMBL:GCE53497.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX-7 {ECO:0000313|EMBL:GCE53497.1};
RA Li J., Tonouchi A.;
RT "Draft Genome Sequence of Capsulimonas corticalis strain AX-7.";
RL Int. J. Syst. Evol. Microbiol. 0:0-0(2018).
RN [2] {ECO:0000313|EMBL:BDI28873.1, ECO:0000313|Proteomes:UP000287394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX-7 {ECO:0000313|EMBL:BDI28873.1,
RC ECO:0000313|Proteomes:UP000287394};
RA Li J., Kudo C., Tonouchi A.;
RT "Capsulimonas corticalis gen. nov., sp. nov., an aerobic capsulated
RT bacterium, of a novel bacterial order, Capsulimonadales ord. nov., of the
RT class Armatimonadia of the phylum Armatimonadetes.";
RL Int. J. Syst. Evol. Microbiol. 69:220-226(2019).
RN [3] {ECO:0000313|EMBL:BDI28873.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AX-7 {ECO:0000313|EMBL:BDI28873.1};
RA Li J., Tonouchi A.;
RL Submitted (MAY-2022) to the EMBL/GenBank/DDBJ databases.
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}.
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};
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;
CC Evidence={ECO:0000256|ARBA:ARBA00000941, ECO:0000256|HAMAP-
CC Rule:MF_00099};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00099}.
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}.
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DR EMBL; AP025739; BDI28873.1; -; Genomic_DNA.
DR EMBL; BHFQ01000004; GCE53497.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A402CU46; -.
DR KEGG; ccot:CCAX7_009240; -.
DR InParanoid; A0A402CU46; -.
DR OrthoDB; 9793421at2; -.
DR Proteomes; UP000287394; Chromosome.
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 CDD; cd16432; CheB_Rec; 1.
DR CDD; cd17541; REC_CheB-like; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.40.50.180; Methylesterase CheB, C-terminal domain; 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 PANTHER; PTHR42872; PROTEIN-GLUTAMATE METHYLESTERASE/PROTEIN-GLUTAMINE GLUTAMINASE; 1.
DR PANTHER; PTHR42872:SF3; PROTEIN-GLUTAMATE METHYLESTERASE_PROTEIN-GLUTAMINE GLUTAMINASE 1; 1.
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; CheY-like; 1.
DR SUPFAM; SSF52738; Methylesterase CheB, C-terminal domain; 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}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00099};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00099};
KW Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00099, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000287394}.
FT DOMAIN 6..123
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 197..381
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT ACT_SITE 203
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00099,
FT ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 230
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00099,
FT ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 323
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 387 AA; 40321 MW; 19FF0E32095EB711 CRC64;
MPEPTKVLVV DDSAFMRKMI TEIVSRDAGM TVVGQARDGA DALQKLDSLQ PDVITLDIEM
PVKDGYTTLT EIMQKRPTAV VMLSSLTQAG ADMTMRCLEA GAVDFVGKPS GSISLDIEKV
AAELLVKIRM AATARLRHAP FRPSARAASV PDFVIKRPEP AAPEAPARRA PLGLSAAPAA
PPVAASVMHG GSRAGGILVV GSSTGGPRAL QTLIPSLPAG LNVPILIVQH MPPGFTASLA
KRLDAESPFE VREAAEGDLL RAGCALVAPG GRHLEVDGHG AIHLTDEPPV HGVRPSVDVT
LASIHRLYGA RATVVLLTGM GKDGARGMKA LHDLGSVTFA EDESTCVVYG MPKAAVDLGG
VTHLLPLHDL ASAVTDSLRS RSVAAMR
//
