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Database: UniProt
Entry: D8FCI9_9DELT
LinkDB: D8FCI9_9DELT
Original site: D8FCI9_9DELT 
ID   D8FCI9_9DELT            Unreviewed;       335 AA.
AC   D8FCI9;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   RecName: Full=protein-glutamate methylesterase {ECO:0000256|ARBA:ARBA00039140};
DE            EC=3.1.1.61 {ECO:0000256|ARBA:ARBA00039140};
GN   ORFNames=NPH_6187 {ECO:0000313|EMBL:EFK06546.1};
OS   delta proteobacterium NaphS2.
OC   Bacteria; Deltaproteobacteria.
OX   NCBI_TaxID=88274 {ECO:0000313|EMBL:EFK06546.1, ECO:0000313|Proteomes:UP000003834};
RN   [1] {ECO:0000313|EMBL:EFK06546.1, ECO:0000313|Proteomes:UP000003834}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NaphS2 {ECO:0000313|EMBL:EFK06546.1,
RC   ECO:0000313|Proteomes:UP000003834};
RX   PubMed=21124915; DOI=10.1371/journal.pone.0014072;
RA   Didonato R.J., Young N.D., Butler J.E., Chin K.J., Hixson K.K., Mouser P.,
RA   Lipton M.S., Deboy R., Methe B.A.;
RT   "Genome Sequence of the Deltaproteobacterial Strain NaphS2 and Analysis of
RT   Differential Gene Expression during Anaerobic Growth on Naphthalene.";
RL   PLoS ONE 5:E14072-E14072(2010).
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:EFK06546.1}.
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DR   EMBL; ADZZ01000631; EFK06546.1; -; Genomic_DNA.
DR   AlphaFoldDB; D8FCI9; -.
DR   OrthoDB; 9793421at2; -.
DR   Proteomes; UP000003834; 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|PROSITE-ProRule:PRU00050};
KW   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:UP000003834}.
FT   DOMAIN          2..119
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          145..335
FT                   /note="CheB-type methylesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50122"
FT   ACT_SITE        160
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT   ACT_SITE        187
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT   ACT_SITE        280
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT   MOD_RES         53
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   335 AA;  36291 MW;  0A98EDFF6B79D59A CRC64;
     MRIAIVNDMS RAVDILKRII LDNSVHKLAW IAKTGSEAVR KCEEDQPDLI LMDLFMPDMD
     GVEATRRIMY ATPCPILLVT ATMEDHAGKI FEAMGHGALD AINTPMMGSG ENALKSRDAL
     LKKISIIEKL SINSKNAPKK EQTKPARAAK VSSLIVMGAS TGGPKALADI LSRMPVDLRA
     GILIAQHVDG EFSAGMARWL DEQSPLKIRI AKEGAYPLQG TAFLAGKNDH LVLTSHLNLA
     YTKEPIATPF RPSVDVLFKS VAAHWPSMGV AVLLTGMGKD GAEGMKMLHR VGWHTIAQDE
     ATSVVYGMPK AARDLVATSE ILPVDRIASA ILRRL
//
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