ID A0A3D8IR85_9HELI Unreviewed; 254 AA.
AC A0A3D8IR85;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=protein-glutamate methylesterase {ECO:0000256|ARBA:ARBA00039140};
DE EC=3.1.1.61 {ECO:0000256|ARBA:ARBA00039140};
GN ORFNames=CQA53_00990 {ECO:0000313|EMBL:RDU67613.1};
OS Helicobacter didelphidarum.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=2040648 {ECO:0000313|EMBL:RDU67613.1, ECO:0000313|Proteomes:UP000256379};
RN [1] {ECO:0000313|EMBL:RDU67613.1, ECO:0000313|Proteomes:UP000256379}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 17-337 {ECO:0000313|EMBL:RDU67613.1,
RC ECO:0000313|Proteomes:UP000256379};
RA Mannion A.J., Shen Z., Fox J.G.;
RT "Novel Campyloabacter and Helicobacter Species and Strains.";
RL Submitted (APR-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:RDU67613.1}.
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DR EMBL; NXLQ01000001; RDU67613.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D8IR85; -.
DR OrthoDB; 9793421at2; -.
DR Proteomes; UP000256379; 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; cd16432; CheB_Rec; 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:UP000256379}.
FT DOMAIN 31..224
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT REGION 234..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 43
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 70
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 166
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 254 AA; 28074 MW; 7571A2C2D0BE45BD CRC64;
MALDRKVNNI LSKQVEEKYH PDTVLEKKPC SLSREKLIVI GSSTGGTEAL NKILSTLPSK
GLPPIVIVQH IPKMFSSSLT ARLDSNSQLQ VFEINSKVQL QNDCVYVANG DSHALLSYKE
GKYYVAPFEA NRVSRHRPSV DILFRSANNI SGKNTLAIIL TGMGDDGMIG MKELFDNGAY
TIAQDEQTCV VFGMPKKAIE IGAVREILPL QQIPKRIMDY ASNKINLLKP KEPDINTPNI
LSATSEEKDS DKEN
//
