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Database: UniProt
Entry: A0A225DZL1_9BACT
LinkDB: A0A225DZL1_9BACT
Original site: A0A225DZL1_9BACT 
ID   A0A225DZL1_9BACT        Unreviewed;       184 AA.
AC   A0A225DZL1;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=protein-glutamate methylesterase {ECO:0000256|ARBA:ARBA00039140};
DE            EC=3.1.1.61 {ECO:0000256|ARBA:ARBA00039140};
GN   ORFNames=FRUB_00102 {ECO:0000313|EMBL:OWK46403.1};
OS   Fimbriiglobus ruber.
OC   Bacteria; Planctomycetota; Planctomycetia; Gemmatales; Gemmataceae;
OC   Fimbriiglobus.
OX   NCBI_TaxID=1908690 {ECO:0000313|EMBL:OWK46403.1, ECO:0000313|Proteomes:UP000214646};
RN   [1] {ECO:0000313|Proteomes:UP000214646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SP5 {ECO:0000313|Proteomes:UP000214646};
RA   Ravin N.V., Rakitin A.L., Ivanova A.A., Beletsky A.V., Kulichevskaya I.S.,
RA   Mardanov A.V., Dedysh S.N.;
RT   "Genome analysis of Fimbriiglobus ruber SP5, the first member of the order
RT   Planctomycetales with confirmed chitinolytic capability.";
RL   Submitted (JUN-2017) 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:OWK46403.1}.
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DR   EMBL; NIDE01000001; OWK46403.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A225DZL1; -.
DR   Proteomes; UP000214646; 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: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; 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:UP000214646}.
FT   DOMAIN          1..184
FT                   /note="CheB-type methylesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50122"
FT   ACT_SITE        6
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT   ACT_SITE        33
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT   ACT_SITE        126
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ   SEQUENCE   184 AA;  19357 MW;  2287784C8772D388 CRC64;
     MVVGASAGAL EALSVLLPAL PTDYPLPVLV VVHLPPDKKS VMAELLQQKC RVGVREAEDK
     EPIRAGIVYF APPDYHLLVE PDRRLSLSSE EPVLYSRPSI DVLFETAADA YGPGLIGVVL
     TGANSDGSRG LRAVLSAGGT GLVQWPDLAY ASAMPQAALD ACPGARVLSL PEIATYLLEC
     VTPV
//
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