ID F4CBR3_SPHS2 Unreviewed; 200 AA.
AC F4CBR3;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=protein-glutamate methylesterase {ECO:0000256|ARBA:ARBA00039140};
DE EC=3.1.1.61 {ECO:0000256|ARBA:ARBA00039140};
GN OrderedLocusNames=Sph21_2096 {ECO:0000313|EMBL:ADZ78655.1};
OS Sphingobacterium sp. (strain 21).
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Sphingobacterium.
OX NCBI_TaxID=743722 {ECO:0000313|EMBL:ADZ78655.1};
RN [1] {ECO:0000313|EMBL:ADZ78655.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=21 {ECO:0000313|EMBL:ADZ78655.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Siebers A.K.,
RA Allgaier M., Thelen M.P., Hugenholtz P., Woyke T.;
RT "Complete sequence of Sphingobacterium sp. 21.";
RL Submitted (MAR-2011) 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};
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DR EMBL; CP002584; ADZ78655.1; -; Genomic_DNA.
DR AlphaFoldDB; F4CBR3; -.
DR STRING; 743722.Sph21_2096; -.
DR KEGG; shg:Sph21_2096; -.
DR PATRIC; fig|743722.3.peg.2237; -.
DR eggNOG; COG2201; Bacteria.
DR HOGENOM; CLU_000445_51_2_10; -.
DR OrthoDB; 649924at2; -.
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; cd16434; CheB-CheR_fusion; 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}.
FT DOMAIN 10..193
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT ACT_SITE 16
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 43
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 135
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 200 AA; 21736 MW; 0FBF62A96FEFCE32 CRC64;
MKTEVNDFFL VGIGGSSGGI QAMQTFFESM PFLPNIAFVA ITHLSRGYAS NLSAILARYT
PYRVIAVKED MHLASGNIYV ITEDSYLECA DGKLLKRPRP KESDINRAVD IFLLSLAETF
RERAIAIILS GGGNDGLKGA VAVEKQGGLV MSQSPISSQF PQMPLAVIRD NNPSAVLEPA
ALAEAVVQRV HEKSINRIRK
//
