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Database: UniProt
Entry: A0A327VA13_9ACTN
LinkDB: A0A327VA13_9ACTN
Original site: A0A327VA13_9ACTN 
ID   A0A327VA13_9ACTN        Unreviewed;       191 AA.
AC   A0A327VA13;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=protein-glutamate methylesterase {ECO:0000256|ARBA:ARBA00039140};
DE            EC=3.1.1.61 {ECO:0000256|ARBA:ARBA00039140};
GN   ORFNames=K377_08043 {ECO:0000313|EMBL:RAJ69467.1};
OS   Streptomyces sp. PsTaAH-137.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1305830 {ECO:0000313|EMBL:RAJ69467.1, ECO:0000313|Proteomes:UP000249376};
RN   [1] {ECO:0000313|EMBL:RAJ69467.1, ECO:0000313|Proteomes:UP000249376}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PsTaAH-137 {ECO:0000313|EMBL:RAJ69467.1,
RC   ECO:0000313|Proteomes:UP000249376};
RA   Currie C.;
RT   "Biomass-degrading enzyme discovery via genome sequencing of insect-
RT   associated Streptomyces.";
RL   Submitted (JUN-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};
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00050}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RAJ69467.1}.
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DR   EMBL; QLLY01000043; RAJ69467.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A327VA13; -.
DR   Proteomes; UP000249376; Unassembled WGS sequence.
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:InterPro.
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: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   Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT   DOMAIN          1..175
FT                   /note="CheB-type methylesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50122"
SQ   SEQUENCE   191 AA;  19823 MW;  A5F22A4C74A78CCF CRC64;
     MQGLGTLLGG LQNDLPVPVL VAQHLNRNRE TRIVPILTRF TALTVKLADD GETPQAGTVY
     IAPPDQHLCV GADGVLFLTR EERVNSARPA ADPLFEAAAE VYGKSIIACV LTGADGDGAR
     GVEAVKAHGG TVIVEDPETA AVKGMPKAAV RTGKVDHVLP LAAIAPAITR LVHVNDAADQ
     ADRPVPPSQP G
//
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