(data stored in SCRATCH zone)

SWISSPROT: C8U1X0_ECO10

ID   C8U1X0_ECO10            Unreviewed;       414 AA.
AC   C8U1X0;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 58.
DE   RecName: Full=Esterase FrsA {ECO:0000256|HAMAP-Rule:MF_01063};
DE            EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_01063};
GN   Name=frsA {ECO:0000256|HAMAP-Rule:MF_01063,
GN   ECO:0000313|EMBL:BAI29128.1};
GN   OrderedLocusNames=ECO103_0254 {ECO:0000313|EMBL:BAI29128.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29128.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29128.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC   -!- FUNCTION: Displays esterase activity toward pNP-butyrate.
CC       {ECO:0000256|HAMAP-Rule:MF_01063}.
CC   -!- SIMILARITY: Belongs to the UPF0255 family. {ECO:0000256|HAMAP-
CC       Rule:MF_01063, ECO:0000256|SAAS:SAAS00560997}.
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DR   EMBL; AP010958; BAI29128.1; -; Genomic_DNA.
DR   RefSeq; WP_000189539.1; NC_013353.1.
DR   SMR; C8U1X0; -.
DR   ESTHER; ecoli-yafa; Duf_1100-R.
DR   EnsemblBacteria; BAI29128; BAI29128; ECO103_0254.
DR   KEGG; eoh:ECO103_0254; -.
DR   HOGENOM; HOG000282295; -.
DR   KO; K11750; -.
DR   OMA; NWIYEWV; -.
DR   BioCyc; ECOL585395:ECO103_RS01335-MONOMER; -.
DR   Proteomes; UP000000959; Chromosome.
DR   GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   HAMAP; MF_01063; UPF0255; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR010520; UPF0255.
DR   Pfam; PF06500; DUF1100; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8U1X0.
DR   SWISS-2DPAGE; C8U1X0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01063,
KW   ECO:0000313|EMBL:BAI29128.1};
KW   Serine esterase {ECO:0000256|HAMAP-Rule:MF_01063}.
SQ   SEQUENCE   414 AA;  46951 MW;  4879E5BDFB07FCBB CRC64;
     MTQANLSETL FKPRFKHPET STLVRRFNHG AQPPVQSALD GKTIPHWYRM INRLMWIWRG
     IDPREILDVQ ARIVMSDAER TDDDLYDTVI GYRGGNWIYE WATQAMVWQQ KACAEEDPQL
     SGRHWLHAAT LYNIAAYPHL KGDDLAEQAQ ALSNRAYEEA AQRLPGTMRQ MEFTVPGGAP
     ITGFLHMPKG DGPFPTVLMC GGLDAMQTDY YSLYERYFAP RGIAMLTIDM PSVGFSSKWK
     LTQDSSLLHQ HVLKALPNVP WVDHTRVAAF GFRFGANVAV RLAYLESPRL KAVACLGPVV
     HTLLSDFKCQ QQVPEMYLDV LASRLGMHDA SDDALRVELN RYSLKVQGLL GRRCPTPMLS
     GYWKNDPFSP EEDSRLITSS SADGKLLEIP FNPVYRNFDK GLQEITGWIE KRLC
//

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