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Database: UniProt
Entry: A0A0E9MLK7_9SPHN
LinkDB: A0A0E9MLK7_9SPHN
Original site: A0A0E9MLK7_9SPHN 
ID   A0A0E9MLK7_9SPHN        Unreviewed;       364 AA.
AC   A0A0E9MLK7;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
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:GAO38311.1};
GN   ORFNames=SCH01S_12_00050 {ECO:0000313|EMBL:GAO38311.1};
OS   Sphingomonas changbaiensis NBRC 104936.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1219043 {ECO:0000313|EMBL:GAO38311.1, ECO:0000313|Proteomes:UP000033202};
RN   [1] {ECO:0000313|EMBL:GAO38311.1, ECO:0000313|Proteomes:UP000033202}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 104936 {ECO:0000313|EMBL:GAO38311.1,
RC   ECO:0000313|Proteomes:UP000033202};
RA   Katano-Makiyama Y., Hosoyama A., Hashimoto M., Noguchi M., Tsuchikane K.,
RA   Ohji S., Yamazoe A., Ichikawa N., Kimura A., Fujita N.;
RT   "Whole genome shotgun sequence of Sphingomonas changbaiensis NBRC 104936.";
RL   Submitted (APR-2015) 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:GAO38311.1}.
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DR   EMBL; BBWU01000012; GAO38311.1; -; Genomic_DNA.
DR   RefSeq; WP_046347173.1; NZ_BBWU01000012.1.
DR   AlphaFoldDB; A0A0E9MLK7; -.
DR   STRING; 1219043.SCH01S_12_00050; -.
DR   OrthoDB; 9793421at2; -.
DR   Proteomes; UP000033202; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; 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   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}; Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033202}.
FT   DOMAIN          20..138
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          177..353
FT                   /note="CheB-type methylesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50122"
FT   ACT_SITE        182
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT   ACT_SITE        209
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT   ACT_SITE        305
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT   MOD_RES         71
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   364 AA;  37788 MW;  91193B0A171E7D5E CRC64;
     MPHRALTSAR RAAAETKPIR LLIVDDSAVA RAVFTRMVGE RPEFQLAATV PSAQAALTFL
     ARNRVDIIIL DIEMPGQDGL SAMPALIAAS RGARVLIVSS SAEQGAAASI QAMTLGAADT
     LAKPGAGAFG GRFAQVLAEK LIRIGHAPDA EAGDNRSPEP MPQVRLRRME EGRVSCVAIG
     ASTGGLHALS DLLRALPQAF GAPILITQHL PPSFMNIFAT QVQEMSGRPT SVARAGSPLA
     RGRILIAPGE GHLSVEMTGG MPRARITAER VESGCLPSVD PMLASVGETF GASAIGIVLS
     GMGRDGLRGA ERMAHAGSDI FVQDRASSVV WGMPGVVAQA GLASAMLPPV QIADLLARRE
     RIAA
//
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