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Database: UniProt
Entry: A0A3R9YP46_9SPHN
LinkDB: A0A3R9YP46_9SPHN
Original site: A0A3R9YP46_9SPHN 
ID   A0A3R9YP46_9SPHN        Unreviewed;       346 AA.
AC   A0A3R9YP46;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-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   Name=cheB {ECO:0000313|EMBL:RST32179.1};
GN   ORFNames=HMF7854_07705 {ECO:0000313|EMBL:RST32179.1};
OS   Sphingomonas ginkgonis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=2315330 {ECO:0000313|EMBL:RST32179.1, ECO:0000313|Proteomes:UP000274661};
RN   [1] {ECO:0000313|EMBL:RST32179.1, ECO:0000313|Proteomes:UP000274661}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HMF7854 {ECO:0000313|EMBL:RST32179.1,
RC   ECO:0000313|Proteomes:UP000274661};
RA   Cha I., Kang H., Kim H., Kang J., Joh K.;
RT   "Sphingomonas sp. HMF7854 Genome sequencing and assembly.";
RL   Submitted (DEC-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: 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:RST32179.1}.
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DR   EMBL; RWJF01000001; RST32179.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3R9YP46; -.
DR   OrthoDB; 9793421at2; -.
DR   Proteomes; UP000274661; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
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   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd16432; CheB_Rec; 1.
DR   CDD; cd17541; REC_CheB-like; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.40.50.180; Methylesterase CheB, C-terminal domain; 1.
DR   InterPro; IPR008248; CheB-like.
DR   InterPro; IPR035909; CheB_C.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR000673; Sig_transdc_resp-reg_Me-estase.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
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   Pfam; PF00072; Response_reg; 1.
DR   PIRSF; PIRSF000876; RR_chemtxs_CheB; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF52738; Methylesterase CheB, C-terminal domain; 1.
DR   PROSITE; PS50122; CHEB; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Chemotaxis {ECO:0000256|ARBA:ARBA00022500, ECO:0000256|PROSITE-
KW   ProRule:PRU00050}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU00050}; Methyltransferase {ECO:0000313|EMBL:RST32179.1};
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW   Reference proteome {ECO:0000313|Proteomes:UP000274661};
KW   Transferase {ECO:0000313|EMBL:RST32179.1}.
FT   DOMAIN          1..117
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          149..346
FT                   /note="CheB-type methylesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50122"
FT   ACT_SITE        166
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT   ACT_SITE        193
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT   ACT_SITE        289
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT   MOD_RES         50
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   346 AA;  35848 MW;  E7B78980BD24E66D CRC64;
     MLVDDSLVAR AVLSRMLESD GGFEIAAVAG TAEDAIEALA HVRVDIILLD LEMPGAGGLK
     MLPHIIAAAR GARVMIVSSL AEEGAEQTIA ALALGAADTL PKPGTGRFNG RFSEVLLSRL
     RALGHAEATA AEPVEQRRAE RPATPIRSPL RAMSNDRLQL LAIGASTGGI HALGAFFAAL
     PMRIGVPILV TQHLPSPFMT VFARQLASPA RRRVLVAEDG MDLLPDLVLV APGDAHLTVE
     LLGDAPRVRL DRRAAKSGCL PSVDPMFATA GAAYGTGALG VVLSGMGRDG TEGSQRLVAC
     GGSVIVQDEP TCAVWGMPRA VAEAGLAAAI LPPDKLARRV ATRVGD
//
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