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Database: UniProt
Entry: A0A2Z6DVU3_HYDTE
LinkDB: A0A2Z6DVU3_HYDTE
Original site: A0A2Z6DVU3_HYDTE 
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
//
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