(data stored in ACNUC7421 zone)

SWISSPROT: A0A0H2ZJB1_PSEAB

ID   A0A0H2ZJB1_PSEAB        Unreviewed;       200 AA.
AC   A0A0H2ZJB1;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   30-AUG-2017, entry version 11.
DE   RecName: Full=Probable chemoreceptor glutamine deamidase CheD {ECO:0000256|HAMAP-Rule:MF_01440};
DE            EC=3.5.1.44 {ECO:0000256|HAMAP-Rule:MF_01440};
GN   Name=cheD {ECO:0000256|HAMAP-Rule:MF_01440,
GN   ECO:0000313|EMBL:ABJ15131.1};
GN   OrderedLocusNames=PA14_02190 {ECO:0000313|EMBL:ABJ15131.1};
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963 {ECO:0000313|EMBL:ABJ15131.1, ECO:0000313|Proteomes:UP000000653};
RN   [1] {ECO:0000313|EMBL:ABJ15131.1, ECO:0000313|Proteomes:UP000000653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14 {ECO:0000313|EMBL:ABJ15131.1,
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: Probably deamidates glutamine residues to glutamate on
CC       methyl-accepting chemotaxis receptors (MCPs), playing an important
CC       role in chemotaxis. {ECO:0000256|HAMAP-Rule:MF_01440}.
CC   -!- CATALYTIC ACTIVITY: Protein L-glutamine + H(2)O = protein L-
CC       glutamate + NH(3). {ECO:0000256|HAMAP-Rule:MF_01440,
CC       ECO:0000256|SAAS:SAAS00850914}.
CC   -!- SIMILARITY: Belongs to the CheD family. {ECO:0000256|HAMAP-
CC       Rule:MF_01440, ECO:0000256|SAAS:SAAS00850918}.
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DR   EMBL; CP000438; ABJ15131.1; -; Genomic_DNA.
DR   RefSeq; WP_003137051.1; NC_008463.1.
DR   EnsemblBacteria; ABJ15131; ABJ15131; PA14_02190.
DR   KEGG; pau:PA14_02190; -.
DR   KO; K03411; -.
DR   OMA; VGMADLN; -.
DR   Proteomes; UP000000653; Chromosome.
DR   GO; GO:0050568; F:protein-glutamine glutaminase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-HAMAP.
DR   CDD; cd16352; CheD; 1.
DR   HAMAP; MF_01440; CheD; 1.
DR   InterPro; IPR005659; Chemorcpt_Glu_NH3ase_CheD.
DR   InterPro; IPR011324; Cytotoxic_necrot_fac-like_cat.
DR   PANTHER; PTHR35147; PTHR35147; 1.
DR   Pfam; PF03975; CheD; 1.
DR   SUPFAM; SSF64438; SSF64438; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0H2ZJB1.
DR   SWISS-2DPAGE; A0A0H2ZJB1.
KW   Chemotaxis {ECO:0000256|HAMAP-Rule:MF_01440,
KW   ECO:0000256|SAAS:SAAS00850903};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000653};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01440,
KW   ECO:0000256|SAAS:SAAS00850913}.
SQ   SEQUENCE   200 AA;  22234 MW;  946397732A58E1E9 CRC64;
     MNLQAREGAP LNRYYDPYFA CDAVKLLPGE YFASGEDLVI VTVLGSCVSV CLRDPLNGIA
     GMNHFMLPER GLGGDPASPS ARYGSHAMEL LINRMLALGA NRERLQAKVF GGGSVLRQIS
     AAIGQRNVEF TLDYLATERI PLLASDVLEA FPRKIYFFPR NGRVLVKSLV ELKNDTVLQR
     ERDYRRRIDR NADGGPIDLF
//

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