ID A0A437MNL7_9PROT Unreviewed; 347 AA.
AC A0A437MNL7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=protein-glutamate methylesterase {ECO:0000256|ARBA:ARBA00039140};
DE EC=3.1.1.61 {ECO:0000256|ARBA:ARBA00039140};
GN ORFNames=EOD42_03825 {ECO:0000313|EMBL:RVT99238.1};
OS Rhodovarius crocodyli.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Rhodovarius.
OX NCBI_TaxID=1979269 {ECO:0000313|EMBL:RVT99238.1, ECO:0000313|Proteomes:UP000282957};
RN [1] {ECO:0000313|EMBL:RVT99238.1, ECO:0000313|Proteomes:UP000282957}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCP-6 {ECO:0000313|EMBL:RVT99238.1,
RC ECO:0000313|Proteomes:UP000282957};
RA Chen W.-M.;
RL Submitted (JAN-2019) 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:RVT99238.1}.
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DR EMBL; SACL01000001; RVT99238.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A437MNL7; -.
DR OrthoDB; 9793421at2; -.
DR Proteomes; UP000282957; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro.
DR GO; GO:0008984; F:protein-glutamate methylesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-UniRule.
DR CDD; cd16432; CheB_Rec; 1.
DR CDD; cd17541; REC_CheB-like; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.40.50.180; Methylesterase CheB, C-terminal domain; 1.
DR InterPro; IPR008248; CheB-like.
DR InterPro; IPR035909; CheB_C.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR000673; Sig_transdc_resp-reg_Me-estase.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
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 Pfam; PF00072; Response_reg; 1.
DR PIRSF; PIRSF000876; RR_chemtxs_CheB; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF52738; Methylesterase CheB, C-terminal domain; 1.
DR PROSITE; PS50122; CHEB; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Chemotaxis {ECO:0000256|ARBA:ARBA00022500, ECO:0000256|PROSITE-
KW ProRule:PRU00050}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00050}; Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000282957}.
FT DOMAIN 7..125
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 154..314
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT ACT_SITE 166
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 192
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 285
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT MOD_RES 58
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 347 AA; 35170 MW; 0967C98AD3820495 CRC64;
MSTAPIRVMV VDDSAFMRLA LRRIIEADGD LRVVGEAPDG AAALEQMTRL QPDVIAMDIE
MPGLDGLEAT RRIMAAPSPP AVVMVSHHTS EGSAMALAAM RAGATDWVSK ETGLGGLDLG
HLDRELRGRL RHWGAAHQAR RAAAPPVPGA EPPPRGAAEI VVVGASTGGP DALGELLSAM
GRPPLPVVVA QHMPAGMAPD LARALSRQSG IAVSVAADGL RLAEGQVVLI PGGEDGALVR
RSDGFWLRLS ARSSAAHPSV DVLFASAAIA ARGGIAVVLT GMGQDGAQGA AGLARRGFAL
LAQSAASCVV PGMPGALLAV APDAETGTPT ELGRRINTLA AVPAPGP
//
