ID H8H1H7_DEIGI Unreviewed; 352 AA.
AC H8H1H7;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=protein-glutamate methylesterase {ECO:0000256|ARBA:ARBA00039140};
DE EC=3.1.1.61 {ECO:0000256|ARBA:ARBA00039140};
GN Name=cheB {ECO:0000313|EMBL:AFD27374.1};
GN OrderedLocusNames=DGo_PB0105 {ECO:0000313|EMBL:AFD27374.1};
OS Deinococcus gobiensis (strain DSM 21396 / JCM 16679 / CGMCC 1.7299 / I-0).
OG Plasmid P2 {ECO:0000313|EMBL:AFD27374.1,
OG ECO:0000313|Proteomes:UP000007575}.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=745776 {ECO:0000313|EMBL:AFD27374.1, ECO:0000313|Proteomes:UP000007575};
RN [1] {ECO:0000313|EMBL:AFD27374.1, ECO:0000313|Proteomes:UP000007575}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21396 / JCM 16679 / CGMCC 1.7299 / I-0
RC {ECO:0000313|Proteomes:UP000007575};
RC PLASMID=Plasmid P2 {ECO:0000313|Proteomes:UP000007575};
RX PubMed=22470573; DOI=10.1371/journal.pone.0034458;
RA Yuan M., Chen M., Zhang W., Lu W., Wang J., Yang M., Zhao P., Tang R.,
RA Li X., Hao Y., Zhou Z., Zhan Y., Yu H., Teng C., Yan Y., Ping S., Wang Y.,
RA Lin M.;
RT "Genome sequence and transcriptome analysis of the radioresistant bacterium
RT Deinococcus gobiensis: insights into the extreme environmental
RT adaptations.";
RL PLoS ONE 7:E34458-E34458(2012).
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; CP002193; AFD27374.1; -; Genomic_DNA.
DR RefSeq; WP_014686470.1; NC_017791.1.
DR AlphaFoldDB; H8H1H7; -.
DR KEGG; dgo:DGo_PB0105; -.
DR PATRIC; fig|745776.4.peg.3500; -.
DR HOGENOM; CLU_000445_51_1_0; -.
DR OrthoDB; 9793421at2; -.
DR Proteomes; UP000007575; Plasmid P2.
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; cd16433; CheB; 1.
DR Gene3D; 3.40.50.180; Methylesterase CheB, C-terminal domain; 1.
DR InterPro; IPR035909; CheB_C.
DR InterPro; IPR011247; Chemotax_prot-Glu_Me-esterase.
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 PIRSF; PIRSF036461; Chmtx_methlestr; 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}; Plasmid {ECO:0000313|EMBL:AFD27374.1}.
FT DOMAIN 1..189
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 131
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 352 AA; 37903 MW; 198446528E92E052 CRC64;
METQRVIVIG TSAGGMQPLL ELAAGLPADF PAAVCIVMHI PAYIPSFLPN ILGRAGPLSA
VHPANGDPIL PGRIYCAPPD QHLLIENGRL NLTRGPKENR MRPAVDTLFR SAAYSAGSNV
IGVVLSGLLD DGTSGLWAIK QFGGTTVVQD PRDAQFDSMP ASALNQVQID HVVTARHLAA
LLVQLVAEPV QAPREAGMNE QVRKRLITEI SIASGGHAFK KGVMTFGKVT PQTCPECGGV
LVQIQEGGFT RYRCHTGHAY TGDTLLVSVT EAIEDKLWAT LRALEEASML LENTGQEFEA
AGNARLAGEY RRRAKEMEAR SALIFENVAR NRSLSVEQLE YEASQKESPQ SD
//
