(data stored in ACNUC7421 zone)

SWISSPROT: C8W0W6_DESAS

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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