(data stored in ACNUC7421 zone)

SWISSPROT: C3MG04_SINFN

ID   C3MG04_SINFN            Unreviewed;       350 AA.
AC   C3MG04;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   30-AUG-2017, entry version 65.
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=cheB2 {ECO:0000313|EMBL:ACP24055.1};
GN   Synonyms=cheB {ECO:0000256|HAMAP-Rule:MF_00099};
GN   OrderedLocusNames=NGR_c02570 {ECO:0000313|EMBL:ACP24055.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP24055.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP24055.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
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; CP001389; ACP24055.1; -; Genomic_DNA.
DR   RefSeq; WP_012706840.1; NC_012587.1.
DR   RefSeq; YP_002824808.1; NC_012587.1.
DR   ProteinModelPortal; C3MG04; -.
DR   STRING; 394.NGR_c02570; -.
DR   EnsemblBacteria; ACP24055; ACP24055; NGR_c02570.
DR   GeneID; 7790835; -.
DR   KEGG; rhi:NGR_c02570; -.
DR   PATRIC; fig|394.7.peg.3058; -.
DR   eggNOG; ENOG4105CMP; Bacteria.
DR   eggNOG; COG2201; LUCA.
DR   HOGENOM; HOG000151424; -.
DR   KO; K03412; -.
DR   OMA; MLEMHRA; -.
DR   OrthoDB; POG091H045J; -.
DR   Proteomes; UP000001054; 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; C3MG04.
DR   SWISS-2DPAGE; C3MG04.
KW   Chemotaxis {ECO:0000256|HAMAP-Rule:MF_00099, ECO:0000256|PROSITE-
KW   ProRule:PRU00050, ECO:0000256|SAAS:SAAS00706681};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001054};
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   ECO:0000313|EMBL:ACP24055.1};
KW   Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00099};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001054}.
FT   DOMAIN        6    123       Response regulatory.
FT                                {ECO:0000259|PROSITE:PS50110}.
FT   DOMAIN      153    345       CheB-type methylesterase.
FT                                {ECO:0000259|PROSITE:PS50122}.
FT   ACT_SITE    165    165       {ECO:0000256|HAMAP-Rule:MF_00099,
FT                                ECO:0000256|PROSITE-ProRule:PRU00050}.
FT   ACT_SITE    191    191       {ECO:0000256|HAMAP-Rule:MF_00099,
FT                                ECO:0000256|PROSITE-ProRule:PRU00050}.
FT   ACT_SITE    287    287       {ECO:0000256|HAMAP-Rule:MF_00099,
FT                                ECO:0000256|PROSITE-ProRule:PRU00050}.
FT   MOD_RES      57     57       4-aspartylphosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00099, ECO:0000256|PROSITE-
FT                                ProRule:PRU00169}.
SQ   SEQUENCE   350 AA;  36958 MW;  EC7FDC7505BE6F22 CRC64;
     MNAPARVLVV DDSPTMRGLI SAVLNADPEV KVVGQAADAL EARQAIKQLD PDVVTLDIEM
     PNMNGLEFLD KIMRLRPMPV IMVSTLTHKG AEATIAALEI GAFDCVGKPH PGDPNPFGGL
     VDKVKAAARS QRKSMITSNR AASAPAVATA SDYRAGRKII AIGASTGGVE ALIAVLQKFP
     ANCPPTVITQ HMPHTFTKSF SERLNRLCAP TVEEATDGAR LEVGKVYLAP GGDRHLQIAN
     ASAPCCRLVD REPVNGHRPS VDVLFDSVAE LAGRNAIGVI LTGMGRDGAA GLLKMRHAGA
     RTFGQNEKTC VVYGMPRVAH ELGAVEMQLP LGSIGEEILK SAAARKEGNE
//

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