ID U2J6I3_9SPHI Unreviewed; 192 AA.
AC U2J6I3;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=protein-glutamate methylesterase {ECO:0000256|ARBA:ARBA00039140};
DE EC=3.1.1.61 {ECO:0000256|ARBA:ARBA00039140};
GN ORFNames=M472_05750 {ECO:0000313|EMBL:ERJ58263.1};
OS Sphingobacterium paucimobilis HER1398.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Sphingobacterium.
OX NCBI_TaxID=1346330 {ECO:0000313|EMBL:ERJ58263.1, ECO:0000313|Proteomes:UP000016584};
RN [1] {ECO:0000313|EMBL:ERJ58263.1, ECO:0000313|Proteomes:UP000016584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HER1398 {ECO:0000313|EMBL:ERJ58263.1,
RC ECO:0000313|Proteomes:UP000016584};
RX PubMed=23929486;
RA White R.A.III., Suttle C.A.;
RT "The Draft Genome Sequence of Sphingomonas paucimobilis Strain HER1398
RT (Proteobacteria), Host to the Giant PAU Phage, Indicates That It Is a
RT Member of the Genus Sphingobacterium (Bacteroidetes).";
RL Genome Announc. 1:e00598-13(2013).
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:ERJ58263.1}.
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DR EMBL; ATDL01000017; ERJ58263.1; -; Genomic_DNA.
DR RefSeq; WP_021071457.1; NZ_ATDL01000017.1.
DR AlphaFoldDB; U2J6I3; -.
DR STRING; 1346330.M472_05750; -.
DR PATRIC; fig|1346330.5.peg.3319; -.
DR eggNOG; COG2201; Bacteria.
DR OrthoDB; 1524092at2; -.
DR Proteomes; UP000016584; 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:UP000016584}.
FT DOMAIN 2..181
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT ACT_SITE 14
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 41
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 134
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 192 AA; 20976 MW; 236C2136ACAB4039 CRC64;
MKGSAENIVL IGGSAGSLLL ITEILENLPK KIDYALCIVI HRSPVFSTGI ENNLSKKLNR
TIIAVTDKTP IKEGTIYFAP PGYHLLIEPD RSFALDSSEE VNYSRPSIDV LFETCAQVYG
KNCSAFLLSG ANTDGAHGLK TIEEFGGSTF IQNPEDALID TMPKSGILES NTSTILKNQE
IIRYFSHNLQ LP
//
