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Database: UniProt
Entry: Q1R429_ECOUT
LinkDB: Q1R429_ECOUT
Original site: Q1R429_ECOUT 
ID   Q1R429_ECOUT            Unreviewed;       306 AA.
AC   Q1R429;
DT   16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2006, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   SubName: Full=Putative lipase {ECO:0000313|EMBL:ABE09885.1};
DE            EC=3.1.1.- {ECO:0000313|EMBL:ABE09885.1};
GN   OrderedLocusNames=UTI89_C4473 {ECO:0000313|EMBL:ABE09885.1};
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106 {ECO:0000313|EMBL:ABE09885.1, ECO:0000313|Proteomes:UP000001952};
RN   [1] {ECO:0000313|EMBL:ABE09885.1, ECO:0000313|Proteomes:UP000001952}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTI89 / UPEC {ECO:0000313|Proteomes:UP000001952};
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA   Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA   Gordon J.I.;
RT   "Identification of genes subject to positive selection in uropathogenic
RT   strains of Escherichia coli: a comparative genomics approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
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DR   EMBL; CP000243; ABE09885.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1R429; -.
DR   ESTHER; ecoli-C4836; Hormone-sensitive_lipase_like.
DR   KEGG; eci:UTI89_C4473; -.
DR   HOGENOM; CLU_012494_6_4_6; -.
DR   Proteomes; UP000001952; Chromosome.
DR   GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR013094; AB_hydrolase_3.
DR   InterPro; IPR033140; Lipase_GDXG_put_SER_AS.
DR   PANTHER; PTHR48081; AB HYDROLASE SUPERFAMILY PROTEIN C4A8.06C; 1.
DR   PANTHER; PTHR48081:SF8; STERYL ACETYL HYDROLASE MUG81-RELATED; 1.
DR   Pfam; PF07859; Abhydrolase_3; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   PROSITE; PS01174; LIPASE_GDXG_SER; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:ABE09885.1};
KW   Serine esterase {ECO:0000256|ARBA:ARBA00022487}.
FT   DOMAIN          79..284
FT                   /note="Alpha/beta hydrolase fold-3"
FT                   /evidence="ECO:0000259|Pfam:PF07859"
FT   ACT_SITE        157
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10038"
SQ   SEQUENCE   306 AA;  34027 MW;  2AD3938DDC9CE02C CRC64;
     MSSTMALEKG IAELVEEFIA AGRPSSRQQS ITQRREGYIA SAVLAGETET RVDIQTIELE
     GMTLRIVSPL NAPTLLPTII YYYGGCFVSG GFATHDNQLR QLAYYGQCRI IAVQYRLAPE
     HTFPAAHDDA QRGAELVRQH AERLGVDKQR ITLAGDSAGG HLALVTALRL KRAGEWQPAQ
     LILIYPMLDA TAHFESYIRN GHDYIITRDT LLSGFEMYLP GIERRHPEAS PIWRNDFNGL
     PPVHIITAEY DPLCDEGEAL YHRMTGQGVQ CTCQRYLGVI HGFFQLGGIS EAARSALRDV
     AWRAGR
//
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