(data stored in SCRATCH zone)

SWISSPROT: D3F410_CONWI

ID   D3F410_CONWI            Unreviewed;       376 AA.
AC   D3F410;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   30-AUG-2017, entry version 51.
DE   RecName: Full=Chemotaxis response regulator protein-glutamate methylesterase {ECO:0000256|HAMAP-Rule:MF_00099};
DE            EC=3.1.1.61 {ECO:0000256|HAMAP-Rule:MF_00099};
GN   Name=cheB {ECO:0000256|HAMAP-Rule:MF_00099};
GN   OrderedLocusNames=Cwoe_0057 {ECO:0000313|EMBL:ADB48493.1};
OS   Conexibacter woesei (strain DSM 14684 / JCM 11494 / NBRC 100937 /
OS   ID131577).
OC   Bacteria; Actinobacteria; Thermoleophilia; Solirubrobacterales;
OC   Conexibacteraceae; Conexibacter.
OX   NCBI_TaxID=469383 {ECO:0000313|EMBL:ADB48493.1, ECO:0000313|Proteomes:UP000008229};
RN   [1] {ECO:0000313|Proteomes:UP000008229}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14684 / JCM 11494 / NBRC 100937 / ID131577
RC   {ECO:0000313|Proteomes:UP000008229};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA   Ivanova N., Mikhailova N., Chertkov O., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA   Hugenholtz P., Woyke T., Wu D., Pukall R., Steenblock K.,
RA   Schneider S., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Conexibacter woesei DSM 14684.";
RL   Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the modulation of the chemotaxis system;
CC       catalyzes the demethylation of specific methylglutamate residues
CC       introduced into the chemoreceptors (methyl-accepting chemotaxis
CC       proteins) by CheR. {ECO:0000256|HAMAP-Rule:MF_00099,
CC       ECO:0000256|SAAS:SAAS00407323}.
CC   -!- CATALYTIC ACTIVITY: Protein L-glutamate O(5)-methyl ester + H(2)O
CC       = protein L-glutamate + methanol. {ECO:0000256|HAMAP-
CC       Rule:MF_00099, ECO:0000256|SAAS:SAAS00706688}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00099,
CC       ECO:0000256|SAAS:SAAS00407336}.
CC   -!- DOMAIN: The N-terminal regulatory domain inhibits the activity of
CC       the C-terminal effector domain. {ECO:0000256|HAMAP-Rule:MF_00099}.
CC   -!- PTM: Phosphorylated by CheA. Phosphorylation suppresses the
CC       inhibitory activity of the N-terminal domain. {ECO:0000256|HAMAP-
CC       Rule:MF_00099}.
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DR   EMBL; CP001854; ADB48493.1; -; Genomic_DNA.
DR   RefSeq; WP_012931546.1; NC_013739.1.
DR   STRING; 469383.Cwoe_0057; -.
DR   EnsemblBacteria; ADB48493; ADB48493; Cwoe_0057.
DR   KEGG; cwo:Cwoe_0057; -.
DR   eggNOG; ENOG4105CMP; Bacteria.
DR   eggNOG; COG2201; LUCA.
DR   HOGENOM; HOG000151424; -.
DR   KO; K03412; -.
DR   OMA; YGMPMAV; -.
DR   OrthoDB; POG091H045J; -.
DR   Proteomes; UP000008229; 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-HAMAP.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-HAMAP.
DR   CDD; cd16432; CheB_Rec; 1.
DR   CDD; cd00156; REC; 1.
DR   Gene3D; 3.40.50.180; -; 1.
DR   HAMAP; MF_00099; CheB_methylest; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR008248; Sig_transdc_resp-reg_CheB.
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; D3F410.
DR   SWISS-2DPAGE; D3F410.
KW   Chemotaxis {ECO:0000256|HAMAP-Rule:MF_00099, ECO:0000256|PROSITE-
KW   ProRule:PRU00050, ECO:0000256|SAAS:SAAS00706681};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008229};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00099,
KW   ECO:0000256|SAAS:SAAS00485815};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00099, ECO:0000256|PROSITE-
KW   ProRule:PRU00050, ECO:0000256|SAAS:SAAS00706700};
KW   Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00099};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008229}.
FT   DOMAIN        8    126       Response regulatory.
FT                                {ECO:0000259|PROSITE:PS50110}.
FT   DOMAIN      186    376       CheB-type methylesterase.
FT                                {ECO:0000259|PROSITE:PS50122}.
FT   ACT_SITE    198    198       {ECO:0000256|HAMAP-Rule:MF_00099,
FT                                ECO:0000256|PROSITE-ProRule:PRU00050}.
FT   ACT_SITE    225    225       {ECO:0000256|HAMAP-Rule:MF_00099,
FT                                ECO:0000256|PROSITE-ProRule:PRU00050}.
FT   ACT_SITE    319    319       {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   376 AA;  38378 MW;  46FC28ECE4E342F6 CRC64;
     MSSATATRVV VADDSGLMRR VVTATLEHSG FTVVGAAKDG DEALALCERE RPDAMTLDLA
     MPGLDGIGVL RALRRQGERA TPVVVVSAFS PAHGARAVDA LAEGAFDLVA KPAVGDGIER
     FTNELSDKVR LAAASRRGRT RPHGGRAGTG AAAAAGRAAA APAAARPRTA AGSGAVRRAE
     RRVRAHAGTR RVVVIACSTG GPKALAELVP ALPAPLGAGT LIVQHMPPGF TNSLAARLDR
     ASNLNVREAA GGEALDPKVA LLAPGGAHLR LAEPSRVVSL SDAPEIGGLR PRADLTIADA
     AKAFGERMVL VVLTGMGKDG LEGAREVRRR GGRVLVEAES TCTVYGMPRA VAEADLADEI
     LPLHELPAAI AAEAGA
//

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