ID D7AP61_THEM3 Unreviewed; 194 AA.
AC D7AP61;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=protein-glutamate methylesterase {ECO:0000256|ARBA:ARBA00039140};
DE EC=3.1.1.61 {ECO:0000256|ARBA:ARBA00039140};
GN OrderedLocusNames=Tmath_1262 {ECO:0000313|EMBL:ADH60977.1};
OS Thermoanaerobacter mathranii subsp. mathranii (strain DSM 11426 / CCUG
OS 53645 / CIP 108742 / A3).
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacter.
OX NCBI_TaxID=583358 {ECO:0000313|EMBL:ADH60977.1, ECO:0000313|Proteomes:UP000002064};
RN [1] {ECO:0000313|EMBL:ADH60977.1, ECO:0000313|Proteomes:UP000002064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11426 / CIP 108742 / A3
RC {ECO:0000313|Proteomes:UP000002064};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Held B., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Zhou J., Hemme C., Woyke T.;
RT "Complete sequence of Thermoanaerobacter mathranii subsp. mathranii
RT mathranii str. A3.";
RL Submitted (MAY-2010) 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; CP002032; ADH60977.1; -; Genomic_DNA.
DR RefSeq; WP_013150333.1; NC_014209.1.
DR AlphaFoldDB; D7AP61; -.
DR STRING; 583358.Tmath_1262; -.
DR KEGG; tmt:Tmath_1262; -.
DR HOGENOM; CLU_000445_51_2_9; -.
DR Proteomes; UP000002064; 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:UniProtKB-EC.
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}.
FT DOMAIN 1..191
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT ACT_SITE 12
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 39
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 133
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 194 AA; 21357 MW; 8955A55A4B18763C CRC64;
MKNDCLVIIG ASTGGPKALQ YILTNLPDEF FASIIVIQHM TQKFTKLMAE RLNQNCKLKV
KEAVDGEVIL KNVAYIAPGD KNLLLIEEND KIKIKLSTDF ESVYKPSIDA TFISASQINA
CIIAVILTGM GSDGSKGLKY LKEKGSFIIC QDIDSSLAKG MPYNAIKTGY VDKVLSLDKI
PAEIIEKVRE FYGK
//
