ID A0A345WKN8_9SPHN Unreviewed; 361 AA.
AC A0A345WKN8;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=protein-glutamate methylesterase {ECO:0000256|ARBA:ARBA00039140};
DE EC=3.1.1.61 {ECO:0000256|ARBA:ARBA00039140};
GN ORFNames=DM480_00745 {ECO:0000313|EMBL:AXJ94240.1};
OS Sphingomonas sp. FARSPH.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=2219696 {ECO:0000313|EMBL:AXJ94240.1, ECO:0000313|Proteomes:UP000254856};
RN [1] {ECO:0000313|EMBL:AXJ94240.1, ECO:0000313|Proteomes:UP000254856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FARSPH {ECO:0000313|EMBL:AXJ94240.1,
RC ECO:0000313|Proteomes:UP000254856};
RA Bendezu Eguis J., Morales Ruiz S., Montesinos R., Quispe Conislla J.,
RA Tataje-Lavanda L., Fernandez-Sanchez M., Fernandez-Diaz M.;
RT "Cell Culture Contaminant.";
RL Submitted (JUN-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};
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DR EMBL; CP029985; AXJ94240.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A345WKN8; -.
DR KEGG; sphf:DM480_00745; -.
DR OrthoDB; 9793421at2; -.
DR Proteomes; UP000254856; Chromosome.
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:UP000254856}.
FT DOMAIN 18..136
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 168..361
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT ACT_SITE 180
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 207
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 304
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT MOD_RES 69
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 361 AA; 36317 MW; 7CCE51D12938C2CF CRC64;
MAVATPRLEP QDVDPPLRVL IVDDSAVARA VMTRIVEADA RFAVKGSVAT ASAALALLAQ
ERVDLVLLDL QMPGIDGLTA LPDLIAAGRG AKILVVSAQA GEGAESTLQA LALGAADTLV
KPAAGERMAA FGDGLIGKLV RLGHSGLDVP PLPAALPPIA PVSAAGRGRS DYDLVAIGAS
TGGIHALSQL LRALPATFRV PILITQHLPA SFMPYFAAQI ATLSGRPCDV ATDLMRVQPG
RIVVAPGDAH LRCVALPDGA AAIRLSHAPA ASGCLPSVDP MFASAAAVFG ARMLAIVLSG
MGRDGAEGAK AVREAGGCVV VQDQTTSVVW GMPGAVAAIG AADAILTPDA IGRLAISGAR
P
//