ID A0A074MYN9_ERYLO Unreviewed; 348 AA.
AC A0A074MYN9;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, 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=EH31_06885 {ECO:0000313|EMBL:KEO90757.1};
OS Erythrobacter longus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=1044 {ECO:0000313|EMBL:KEO90757.1, ECO:0000313|Proteomes:UP000027647};
RN [1] {ECO:0000313|EMBL:KEO90757.1, ECO:0000313|Proteomes:UP000027647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6997 {ECO:0000313|EMBL:KEO90757.1,
RC ECO:0000313|Proteomes:UP000027647};
RA Zheng Q.;
RT "A comprehensive comparison of genomes of Erythrobacter spp. strains.";
RL Submitted (APR-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};
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00050}.
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:KEO90757.1}.
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DR EMBL; JMIW01000002; KEO90757.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074MYN9; -.
DR STRING; 1044.EH31_06885; -.
DR eggNOG; COG2201; Bacteria.
DR OrthoDB; 9793421at2; -.
DR Proteomes; UP000027647; 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:UniProtKB-EC.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
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:SF3; PROTEIN-GLUTAMATE METHYLESTERASE_PROTEIN-GLUTAMINE GLUTAMINASE 1; 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};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000027647}.
FT DOMAIN 5..122
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 158..342
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT MOD_RES 56
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 348 AA; 35803 MW; F1450F7A8146C1BD CRC64;
MRDTRVMVVD DSAAMRALFS GILENAKGVS VCGVASSAAE AREMIAELKP DVLTLDVEMP
VMTGMEFLEE IMEKRPMPVI MLSSIAQAGS GTAAKALELG AVHCFPKPLR TTPEEFDATV
AKLGDIVIKA AKGELSPADA GADSDDEVSN YEPDGSPVVM ACGEAGIEPL KQVIAAYPVN
CPPTTIVVDA DRVSVDPVLA ELQSSAKCAV AEATDGALLE PGKVYLAFDK ASHVIVEAGS
PPRLRLAARD PVAGLRPCAD LLFGSIARAR IAVHAGLLSG AGADGAKGLQ ILMQTGAKVF
LEDPADGAPR DRINAVHALG VGAADMPVGD LAAWLLNGTA KSGEAKAA
//
