(data stored in SCRATCH zone)

SWISSPROT: A0A0H2ZKW7_PSEAB

ID   A0A0H2ZKW7_PSEAB        Unreviewed;       343 AA.
AC   A0A0H2ZKW7;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   07-JUN-2017, entry version 15.
DE   RecName: Full=Protein-glutamate methylesterase {ECO:0000256|SAAS:SAAS00706697};
DE            EC=3.1.1.61 {ECO:0000256|SAAS:SAAS00706697};
GN   OrderedLocusNames=PA14_05400 {ECO:0000313|EMBL:ABJ15381.1};
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963 {ECO:0000313|EMBL:ABJ15381.1, ECO:0000313|Proteomes:UP000000653};
RN   [1] {ECO:0000313|EMBL:ABJ15381.1, ECO:0000313|Proteomes:UP000000653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14 {ECO:0000313|EMBL:ABJ15381.1,
RC   ECO:0000313|Proteomes:UP000000653};
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
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|SAAS:SAAS00407323}.
CC   -!- CATALYTIC ACTIVITY: Protein L-glutamate O(5)-methyl ester + H(2)O
CC       = protein L-glutamate + methanol. {ECO:0000256|SAAS:SAAS00706688}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00407336}.
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DR   EMBL; CP000438; ABJ15381.1; -; Genomic_DNA.
DR   RefSeq; WP_004365048.1; NC_008463.1.
DR   EnsemblBacteria; ABJ15381; ABJ15381; PA14_05400.
DR   KEGG; pau:PA14_05400; -.
DR   KO; K06597; -.
DR   OMA; SIDQMML; -.
DR   Proteomes; UP000000653; 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-EC.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.180; -; 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   Pfam; PF01339; CheB_methylest; 1.
DR   PIRSF; PIRSF000876; RR_chemtxs_CheB; 1.
DR   SUPFAM; SSF52172; SSF52172; 1.
DR   SUPFAM; SSF52738; SSF52738; 1.
DR   PROSITE; PS50122; CHEB; 1.
PE   4: Predicted;
DR   PRODOM; A0A0H2ZKW7.
DR   SWISS-2DPAGE; A0A0H2ZKW7.
KW   Chemotaxis {ECO:0000256|PROSITE-ProRule:PRU00050,
KW   ECO:0000256|SAAS:SAAS00706681};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000653};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS00485815};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00050,
KW   ECO:0000256|SAAS:SAAS00706700}.
FT   DOMAIN      141    335       CheB-type methylesterase.
FT                                {ECO:0000259|PROSITE:PS50122}.
FT   ACT_SITE    157    157       {ECO:0000256|PROSITE-ProRule:PRU00050}.
FT   ACT_SITE    184    184       {ECO:0000256|PROSITE-ProRule:PRU00050}.
FT   ACT_SITE    277    277       {ECO:0000256|PROSITE-ProRule:PRU00050}.
SQ   SEQUENCE   343 AA;  37166 MW;  598DFD622C67ADA9 CRC64;
     MSERATPRVA VIADTSLQRH VLQQALLGHG YEVVLNADPA RVDDAALECA PDLWLVDLTQ
     QDDSPLLDSL LEQDCAPVLF GEGHAPERHT EHYPRWERRL IGKLKRLIGD PSDGVGDSLG
     ALLDEERPPR LEIPGDLAAM PLQAGEAARE VWLLAASLGG PAAVKAFLDA LPGGLPIGFL
     YAQHIDASFE QNLPQAVGRH SQWHVKNVRD GEALRCGEVM VVPVLHELGF HHDGRLKCSQ
     RPWPEPYTPS IDQMMLNLAQ QFGPDCGVIV FSGMGSDGSA AAAYVRRQGG EVWTQRADSC
     VCSSMPDSLR EAGYSSFNAS PRELAEALVK HLAARCAPTG VET
//

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