ID A0A402D764_9BACT Unreviewed; 221 AA.
AC A0A402D764;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE RecName: Full=protein-glutamate methylesterase {ECO:0000256|ARBA:ARBA00039140};
DE EC=3.1.1.61 {ECO:0000256|ARBA:ARBA00039140};
GN ORFNames=CCAX7_36050 {ECO:0000313|EMBL:BDI31554.1}, CCAX7_65630
GN {ECO:0000313|EMBL:GCE58049.1};
OS Capsulimonas corticalis.
OC Bacteria; Armatimonadota; Armatimonadia; Capsulimonadales;
OC Capsulimonadaceae; Capsulimonas.
OX NCBI_TaxID=2219043 {ECO:0000313|EMBL:GCE58049.1};
RN [1] {ECO:0000313|EMBL:GCE58049.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX-7 {ECO:0000313|EMBL:GCE58049.1};
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:BDI31554.1, ECO:0000313|Proteomes:UP000287394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX-7 {ECO:0000313|EMBL:BDI31554.1,
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:BDI31554.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AX-7 {ECO:0000313|EMBL:BDI31554.1};
RA Li J., Tonouchi A.;
RL Submitted (MAY-2022) to the EMBL/GenBank/DDBJ databases.
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};
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DR EMBL; AP025739; BDI31554.1; -; Genomic_DNA.
DR EMBL; BHFQ01000043; GCE58049.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A402D764; -.
DR KEGG; ccot:CCAX7_36050; -.
DR InParanoid; A0A402D764; -.
DR OrthoDB; 9793421at2; -.
DR Proteomes; UP000287394; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro.
DR GO; GO:0008984; F:protein-glutamate methylesterase activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-UniRule.
DR CDD; cd16433; CheB; 1.
DR Gene3D; 3.40.50.180; Methylesterase CheB, C-terminal domain; 1.
DR InterPro; IPR035909; CheB_C.
DR InterPro; IPR000673; Sig_transdc_resp-reg_Me-estase.
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 SUPFAM; SSF52738; Methylesterase CheB, C-terminal domain; 1.
DR PROSITE; PS50122; CHEB; 1.
PE 4: Predicted;
KW Chemotaxis {ECO:0000256|PROSITE-ProRule:PRU00050};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00050}; Reference proteome {ECO:0000313|Proteomes:UP000287394}.
FT DOMAIN 27..209
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT ACT_SITE 36
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 63
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 156
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 221 AA; 23023 MW; 8A512A668F8C70F2 CRC64;
MTLNSKAIIE YGCSKVIVGQ RYNGSTPLQV VAIGASAGGL QAIKNILSAL PPDFPAAIII
LQHASPNHKS LLAEILNHMT SLFVKEAEDN DQLAGGTVYV APPGKHILIS PYGAVSFSNS
PKVHFVRPSL DVLFHSLAIS LGDCVIGVVL TGGDGDGAEG IRAIKSRGGT TIAQNEESSE
FPSMPRAAAR TGDVDYVLPL SLIAPKLASI CARTIASVEP E
//
