ID A0A410PS12_9CLOT Unreviewed; 193 AA.
AC A0A410PS12;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=protein-glutamate methylesterase {ECO:0000256|ARBA:ARBA00039140};
DE EC=3.1.1.61 {ECO:0000256|ARBA:ARBA00039140};
GN ORFNames=EQM05_09955 {ECO:0000313|EMBL:QAT41675.1};
OS Clostridium sp. JN-9.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=2507159 {ECO:0000313|EMBL:QAT41675.1, ECO:0000313|Proteomes:UP000287890};
RN [1] {ECO:0000313|EMBL:QAT41675.1, ECO:0000313|Proteomes:UP000287890}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN-9 {ECO:0000313|EMBL:QAT41675.1,
RC ECO:0000313|Proteomes:UP000287890};
RA Ma S.;
RT "Draft genomes of a novel of Clostridium strains.";
RL Submitted (JAN-2019) 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; CP035280; QAT41675.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A410PS12; -.
DR OrthoDB; 9793421at2; -.
DR Proteomes; UP000287890; 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; cd16432; CheB_Rec; 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:UP000287890}.
FT DOMAIN 11..193
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT ACT_SITE 16
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 43
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 136
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 193 AA; 20831 MW; 8122F9827C2A5156 CRC64;
MNTSHNKINA VVIGASTGGP KALYAVITLL PKDLGVPVFV VQHMPVGFTK AFAERLNSNS
EITVVEAKDK DDIVKNVVYM APGGYHMEVG SDKKIHLNID PPIWGVRPAV DKLFISSSKV
YKENLMSVVL TGMGKDGANG TIEVKKNGGY TVSEHESTCT IYGMPKAAFE TGMVDKVLPL
DEISREIINA VKI
//
