ID N2J893_9PSED Unreviewed; 340 AA.
AC N2J893;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=protein-glutamate methylesterase {ECO:0000256|ARBA:ARBA00039140};
DE EC=3.1.1.61 {ECO:0000256|ARBA:ARBA00039140};
GN ORFNames=HMPREF1487_05170 {ECO:0000313|EMBL:ENA35812.1};
OS Pseudomonas sp. HPB0071.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1203578 {ECO:0000313|EMBL:ENA35812.1, ECO:0000313|Proteomes:UP000017050};
RN [1] {ECO:0000313|EMBL:ENA35812.1, ECO:0000313|Proteomes:UP000017050}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HPB0071 {ECO:0000313|EMBL:ENA35812.1,
RC ECO:0000313|Proteomes:UP000017050};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Schmidt T., Dover J., Dai D.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Pseudomonas sp. HPB0071.";
RL Submitted (MAR-2013) 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:ENA35812.1}.
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DR EMBL; AQFP01000004; ENA35812.1; -; Genomic_DNA.
DR RefSeq; WP_010795383.1; NZ_KI517367.1.
DR AlphaFoldDB; N2J893; -.
DR PATRIC; fig|1203578.3.peg.851; -.
DR HOGENOM; CLU_064504_0_0_6; -.
DR OrthoDB; 9793421at2; -.
DR Proteomes; UP000017050; 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 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00050}; Reference proteome {ECO:0000313|Proteomes:UP000017050}.
FT DOMAIN 147..337
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT ACT_SITE 159
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 186
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 279
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 340 AA; 37193 MW; 742FC27A164E3A53 CRC64;
MTEKAIVRVA ILADTSLQRY VLQQVLAGNG YQVVFNSDPT RLDVEALRAC ETDLWLVDLA
ESEDSNVLED LLEHTSTPVL FGEGQAPEFS SDLFPRWERR LITKLKHLVG DTTEAVGPSL
QALLADTERP ERLSLPASLA STPLQMGESA KEVWLLAASL GGPDAVKTFL DALPGGLPIG
FLYAQHIDAN FEATLPMAVG RHSQWHVQIA QPGLEVRCGE VIVVPTQNEL SFRNDSKLDV
LSRKWPEPYT PSVDQMMLNL AQHFGSRCGM IIFSGMGNDG SSSAAYMRRR GAEIWTQSAD
SCSCASMPET LREAGFSSFT SDPRGLAEAL VNRLAKQHAH
//
