ID A0A097EKG1_9SPHN Unreviewed; 346 AA.
AC A0A097EKG1;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=protein-glutamate methylesterase {ECO:0000256|ARBA:ARBA00039140};
DE EC=3.1.1.61 {ECO:0000256|ARBA:ARBA00039140};
GN ORFNames=MC45_06420 {ECO:0000313|EMBL:AIT08050.1};
OS Sphingomonas taxi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1549858 {ECO:0000313|EMBL:AIT08050.1, ECO:0000313|Proteomes:UP000033200};
RN [1] {ECO:0000313|EMBL:AIT08050.1, ECO:0000313|Proteomes:UP000033200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55669 {ECO:0000313|EMBL:AIT08050.1,
RC ECO:0000313|Proteomes:UP000033200};
RA Zhou Y., Ma T., Liu T.;
RT "Using Illumina technology Improving SMRT sequencing Genome Assembly by
RT RASTools.";
RL Submitted (SEP-2014) 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; CP009571; AIT08050.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A097EKG1; -.
DR STRING; 1549858.MC45_06420; -.
DR KEGG; stax:MC45_06420; -.
DR eggNOG; COG2201; Bacteria.
DR HOGENOM; CLU_000445_51_0_5; -.
DR Proteomes; UP000033200; 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:UP000033200}.
FT DOMAIN 1..118
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 152..337
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT ACT_SITE 165
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 192
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 289
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT MOD_RES 51
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 346 AA; 35182 MW; 7587BA95A045D2D7 CRC64;
MLIVDDSAVA RAVMERIIAA TDRYVVVASV STASAALAVL ARERVQFVLL DVQMPGVDGL
TALPGLIAAG QGANVLVVSG QAAEGAATTV QALALGATDT VFKPASGERL GQFGEILIDK
LDRLASVACA GRPAPAVVPL RTAATPVPRA VPAADEYDVM AIGASTGGIH ALSALLAQIP
ATFRLPILIT QHLPASFMPY FAAQLAVIGN RPCEVAIDRL RLRPGRIIVA PGDAHMRCVA
LGDGSAAIRL THDAAASGCT PSVDPMFASL AEVFGARMLA VVLSGMGRDG AEGARLVRQA
GGCVLVQDQA SSVIWGMPGA VADGGSADAV LPPDAIGRLA AARRRP
//