ID A0A2Z6DVU3_HYDTE Unreviewed; 191 AA.
AC A0A2Z6DVU3;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=protein-glutamate methylesterase {ECO:0000256|ARBA:ARBA00039140};
DE EC=3.1.1.61 {ECO:0000256|ARBA:ARBA00039140};
GN ORFNames=HPTL_0245 {ECO:0000313|EMBL:BBD76515.1};
OS Hydrogenophilus thermoluteolus (Pseudomonas hydrogenothermophila).
OC Bacteria; Pseudomonadota; Hydrogenophilia; Hydrogenophilales;
OC Hydrogenophilaceae; Hydrogenophilus.
OX NCBI_TaxID=297 {ECO:0000313|EMBL:BBD76515.1, ECO:0000313|Proteomes:UP000262004};
RN [1] {ECO:0000313|EMBL:BBD76515.1, ECO:0000313|Proteomes:UP000262004}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TH-1 {ECO:0000313|EMBL:BBD76515.1,
RC ECO:0000313|Proteomes:UP000262004};
RA Arai H.;
RT "Complete genome sequence of Hydrogenophilus thermoluteolus TH-1.";
RL Submitted (APR-2018) 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; AP018558; BBD76515.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z6DVU3; -.
DR KEGG; htl:HPTL_0245; -.
DR OrthoDB; 5291131at2; -.
DR Proteomes; UP000262004; 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:SF6; PROTEIN-GLUTAMATE METHYLESTERASE_PROTEIN-GLUTAMINE GLUTAMINASE; 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:UP000262004}.
FT DOMAIN 1..191
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT ACT_SITE 13
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 39
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 135
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 191 AA; 19883 MW; 00A0E56ECC339509 CRC64;
MGRAPQVIVV GSSTGGTAVV ETILAKLPRT VPAIVIVQHM PAGFTHPFAQ RLDMLSALDV
VEASHRTVLR PGLVLIAPGG HHLRLAPRGN AYCVEVIDGP PVNYHKPSID VLFHSAAQIA
GRRALGILLT GMGNDGAAGL KAMHDAGAHT IVQDEASCVV FGMPKAAIAL GGVDEVLPPA
AIAQRIIRTR E
//