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ID C8W0W6_DESAS Unreviewed; 347 AA.
AC C8W0W6;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 08-MAY-2019, entry version 72.
DE RecName: Full=Protein-glutamate methylesterase/protein-glutamine glutaminase {ECO:0000256|HAMAP-Rule:MF_00099};
DE EC=3.1.1.61 {ECO:0000256|HAMAP-Rule:MF_00099};
DE EC=3.5.1.44 {ECO:0000256|HAMAP-Rule:MF_00099};
GN Name=cheB {ECO:0000256|HAMAP-Rule:MF_00099};
GN OrderedLocusNames=Dtox_0615 {ECO:0000313|EMBL:ACV61535.1};
OS Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS B-1644) (Desulfofarcimen acetoxidans).
OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC Desulfofarcimen.
OX NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV61535.1, ECO:0000313|Proteomes:UP000002217};
RN [1] {ECO:0000313|EMBL:ACV61535.1, ECO:0000313|Proteomes:UP000002217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC {ECO:0000313|Proteomes:UP000002217};
RX PubMed=21304664; DOI=10.4056/sigs.39508;
RA Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT (5575).";
RL Stand. Genomic Sci. 1:242-253(2009).
CC -!- FUNCTION: Involved in chemotaxis. Part of a chemotaxis signal
CC transduction system that modulates chemotaxis in response to
CC various stimuli. Catalyzes the demethylation of specific
CC methylglutamate residues introduced into the chemoreceptors
CC (methyl-accepting chemotaxis proteins or MCP) by CheR. Also
CC mediates the irreversible deamidation of specific glutamine
CC residues to glutamic acid. {ECO:0000256|HAMAP-Rule:MF_00099,
CC ECO:0000256|SAAS:SAAS01100814}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] +
CC NH4(+); Xref=Rhea:RHEA:16441, Rhea:RHEA-COMP:10207, Rhea:RHEA-
CC COMP:10208, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29973, ChEBI:CHEBI:30011; EC=3.5.1.44;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00099,
CC ECO:0000256|SAAS:SAAS01116312};
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; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00099, ECO:0000256|SAAS:SAAS01130167};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00099,
CC ECO:0000256|SAAS:SAAS00132521}.
CC -!- DOMAIN: Contains a C-terminal catalytic domain, and an N-terminal
CC region which modulates catalytic activity. {ECO:0000256|HAMAP-
CC Rule:MF_00099}.
CC -!- PTM: Phosphorylated by CheA. Phosphorylation of the N-terminal
CC regulatory domain activates the methylesterase activity.
CC {ECO:0000256|HAMAP-Rule:MF_00099}.
CC -!- SIMILARITY: Belongs to the CheB family. {ECO:0000256|HAMAP-
CC Rule:MF_00099, ECO:0000256|SAAS:SAAS01100824}.
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DR EMBL; CP001720; ACV61535.1; -; Genomic_DNA.
DR RefSeq; WP_015756254.1; NC_013216.1.
DR STRING; 485916.Dtox_0615; -.
DR EnsemblBacteria; ACV61535; ACV61535; Dtox_0615.
DR KEGG; dae:Dtox_0615; -.
DR eggNOG; ENOG4105CMP; Bacteria.
DR eggNOG; COG2201; LUCA.
DR HOGENOM; HOG000151423; -.
DR KO; K03412; -.
DR OMA; YGMPMAV; -.
DR OrthoDB; 1655418at2; -.
DR BioCyc; DACE485916:G1GFV-621-MONOMER; -.
DR Proteomes; UP000002217; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro.
DR GO; GO:0008984; F:protein-glutamate methylesterase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0050568; F:protein-glutamine glutaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-UniRule.
DR GO; GO:0018277; P:protein deamination; IEA:UniProtKB-UniRule.
DR GO; GO:0006482; P:protein demethylation; IEA:UniProtKB-UniRule.
DR CDD; cd16432; CheB_Rec; 1.
DR CDD; cd00156; REC; 1.
DR Gene3D; 3.40.50.180; -; 1.
DR HAMAP; MF_00099; CheB_chemtxs; 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 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; SSF52172; 1.
DR SUPFAM; SSF52738; SSF52738; 1.
DR PROSITE; PS50122; CHEB; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 3: Inferred from homology;
DR PRODOM; C8W0W6.
DR SWISS-2DPAGE; C8W0W6.
KW Chemotaxis {ECO:0000256|HAMAP-Rule:MF_00099, ECO:0000256|PROSITE-
KW ProRule:PRU00050, ECO:0000256|SAAS:SAAS00706681};
KW Complete proteome {ECO:0000313|Proteomes:UP000002217};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00099,
KW ECO:0000256|SAAS:SAAS00132526};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00099, ECO:0000256|PROSITE-
KW ProRule:PRU00050, ECO:0000256|SAAS:SAAS00706700,
KW ECO:0000313|EMBL:ACV61535.1};
KW Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00099, ECO:0000256|PROSITE-
KW ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000002217}.
FT DOMAIN 7 120 Response regulatory.
FT {ECO:0000259|PROSITE:PS50110}.
FT DOMAIN 151 343 CheB-type methylesterase.
FT {ECO:0000259|PROSITE:PS50122}.
FT ACT_SITE 163 163 {ECO:0000256|HAMAP-Rule:MF_00099,
FT ECO:0000256|PROSITE-ProRule:PRU00050}.
FT ACT_SITE 189 189 {ECO:0000256|HAMAP-Rule:MF_00099,
FT ECO:0000256|PROSITE-ProRule:PRU00050}.
FT ACT_SITE 285 285 {ECO:0000256|HAMAP-Rule:MF_00099,
FT ECO:0000256|PROSITE-ProRule:PRU00050}.
FT MOD_RES 58 58 4-aspartylphosphate. {ECO:0000256|HAMAP-
FT Rule:MF_00099, ECO:0000256|PROSITE-
FT ProRule:PRU00169}.
SQ SEQUENCE 347 AA; 37408 MW; B75723F416B38703 CRC64;
MIKKKIKVLV VDDSLVFRET LAKSISKDPG IEVVGTASDP FMARDKILEL EPDVLTLDVE
MPKMSGIEFL KRLMPQYPIP VIMVSSVGEN VFDALNAGAV DFVAKPNFGI EKGIDALINE
LIVKIKIAST ARLSHWKNKS TCSGIVGKDN GHAGNSIIAI GASTGGTEAI LSILKQFPGN
MPGIVIVQHM PPVFTKMYAQ RLNNSCLLEV KEAQKGDRVL PGTVLIAPGD YHMRIKKAGD
NYSVECLKGE KVNGHCPSVD VLFESVAEKA GSAAIGVILT GMGHDGARGL LSMRKKGALT
IGQNEETCVV YGMPKVAYEI GAVQKQSSLL SIPQLIYSML DNIQKYR
//
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