(data stored in SCRATCH zone)

SWISSPROT: C6B1C5_RHILS

ID   C6B1C5_RHILS            Unreviewed;       347 AA.
AC   C6B1C5;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   30-AUG-2017, entry version 64.
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=Rleg_0333 {ECO:0000313|EMBL:ACS54644.1};
OS   Rhizobium leguminosarum bv. trifolii (strain WSM1325).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=395491 {ECO:0000313|EMBL:ACS54644.1, ECO:0000313|Proteomes:UP000002256};
RN   [1] {ECO:0000313|EMBL:ACS54644.1, ECO:0000313|Proteomes:UP000002256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM1325 {ECO:0000313|EMBL:ACS54644.1,
RC   ECO:0000313|Proteomes:UP000002256};
RX   PubMed=21304718;
RA   Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K.,
RA   Tiwari R., Copeland A., Nolan M., Han C., Brettin T., Land M.,
RA   Ovchinikova G., Ivanova N., Mavromatis K., Markowitz V., Kyrpides N.,
RA   Melino V., Denton M., Yates R., Howieson J.;
RT   "Complete genome sequence of Rhizobium leguminosarum bv. trifolii
RT   strain WSM1325, an effective microsymbiont of annual Mediterranean
RT   clovers.";
RL   Stand. Genomic Sci. 2:347-356(2010).
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; CP001622; ACS54644.1; -; Genomic_DNA.
DR   RefSeq; WP_012756047.1; NC_012850.1.
DR   EnsemblBacteria; ACS54644; ACS54644; Rleg_0333.
DR   KEGG; rlg:Rleg_0333; -.
DR   HOGENOM; HOG000151424; -.
DR   KO; K03412; -.
DR   OMA; YGMPMAV; -.
DR   OrthoDB; POG091H045J; -.
DR   Proteomes; UP000002256; 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; C6B1C5.
DR   SWISS-2DPAGE; C6B1C5.
KW   Chemotaxis {ECO:0000256|HAMAP-Rule:MF_00099, ECO:0000256|PROSITE-
KW   ProRule:PRU00050, ECO:0000256|SAAS:SAAS00706681};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002256};
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:ACS54644.1};
KW   Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00099}.
FT   DOMAIN        6    123       Response regulatory.
FT                                {ECO:0000259|PROSITE:PS50110}.
FT   DOMAIN      150    342       CheB-type methylesterase.
FT                                {ECO:0000259|PROSITE:PS50122}.
FT   ACT_SITE    162    162       {ECO:0000256|HAMAP-Rule:MF_00099,
FT                                ECO:0000256|PROSITE-ProRule:PRU00050}.
FT   ACT_SITE    188    188       {ECO:0000256|HAMAP-Rule:MF_00099,
FT                                ECO:0000256|PROSITE-ProRule:PRU00050}.
FT   ACT_SITE    284    284       {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   347 AA;  36730 MW;  B6507A1E333A7F4E CRC64;
     MSAPARVLVV DDSPTMRGLI TAVLSSDPEV NVIGQAGDAL EAREAIKRLN PDVLTLDIEM
     PNMNGLDFLE KIMTLRPMPV IMVSTMTHRG AEATLAALEI GAFDCVGKPA PGELRPFGDL
     AEKVKAAART QRQYSQPVAA VAPPPSVGDF RVGRKIVAIG SSTGGVEALI AVLQKFPANC
     PPTVITQHMP PTFTKSFAER LNRLCAPVVQ EATDGARLEI GKIYLAPGGE RHLQVSNASA
     PCCRLIDRAP VNGHRPSVDV LFDSVAELAG RNAVGVILTG MGRDGAAGLL KMRHAGARTL
     GQNEKTCVVY GMPRVAHELG AVEQQLPLSA IGEEILKMTA ARKEGTE
//

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